Publications
Publications of Paul Schimmel, Ph.D
515. Schimmel, P. Richard A. Lerner: Memories and Reflections. Isr. J. Chem. 2023, 63, doi.org/10.1002/ijch.202300149.
514. de Potter B, Vallee I, Camacho N, Filipe Costa Póvoas L, Bonsembiante A, Pons I Pons A, Eckhard U, Gomis-Rüth FX, Yang XL, Schimmel P, Kuhle B, Ribas de Pouplana L. Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase. Nucleic Acids Res. 2023 Aug 28:gkad696. doi: 10.1093/nar/gkad696. Epub ahead of print. PMID: 37638745.
513. Chen W, Rehsi P, Thompson K, Yeo M, Stals K, He L, Schimmel P, Chrzanowska-Lightowlers ZMA, Wakeling E, Taylor RW, Kuhle B. Clinical and molecular characterization of novel FARS2 variants causing neonatal mitochondrial disease. Mol Genet Metab. 2023 Jul 24;140(3):107657. doi: 10.1016/j.ymgme.2023.107657. Epub ahead of print. PMID: 37523899.
512. Kuhle B, Hirschi M, Doerfel LK, Lander GC, Schimmel P. Structural basis for a degenerate tRNA identity code and the evolution of bimodal specificity in human mitochondrial tRNA recognition. Nat Commun. 2023 Aug 9;14(1):4794. doi: 10.1038/s41467-023-40354-2. PMID: 37558671; PMCID: PMC10412605.
511. Cui H, Diedrich JK, Wu DC, Lim JJ, Nottingham RM, Moresco JJ, Yates JR 3rd, Blencowe BJ, Lambowitz AM, Schimmel P. Arg-tRNA synthetase links inflammatory metabolism to RNA splicing and nuclear trafficking via SRRM2. Nat Cell Biol. 2023 Apr;25(4):592-603. doi: 10.1038/s41556-023-01118-8. Epub 2023 Apr 14. PMID: 37059883
510. Istvan ES, Guerra F, Abraham M, Huang KS, Rocamora F, Zhao H, Xu L, Pasaje C, Kumpornsin K, Luth MR, Cui H, Yang T, Palomo Diaz S, Gomez-Lorenzo MG, Qahash T, Mittal N, Ottilie S, Niles J, Lee MCS, Llinas M, Kato N, Okombo J, Fidock DA, Schimmel P, Gamo FJ, Goldberg DE, Winzeler EA. Cytoplasmic isoleucyl tRNA synthetase as an attractive multistage antimalarial drug target. Sci Transl Med. 2023 Mar 8;15(686):eadc9249. doi: 10.1126/scitranslmed.adc9249. Epub 2023 Mar 8. PMID: 36888694.
509. Han L, Luo Z, Ju Y, Chen B, Zou T, Wang J, Xu J, Gu Q, Yang XL, Schimmel P, Zhou H. The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements. Sci Adv. 2023 Feb 10;9(6):eadf1027. doi: 10.1126/sciadv.adf1027. Epub 2023 Feb 8. PMID: 36753552.
508. Morodomi Y, Kanaji S, Sullivan BM, Zarpellon A, Orje JN, Won E, Shapiro R, Yang XL, Ruf W, Schimmel P, Ruggeri ZM, Kanaji T. Inflammatory platelet production stimulated by tyrosyl-tRNA synthetase mimicking viral infection. Proc Natl Acad Sci U S A. 2022 Nov 29;119(48):e2212659119. doi: 10.1073/pnas.2212659119. Epub 2022 Nov 21. PMID: 36409883.
507. Kuhle, B., Hirschi, M., Doerfel, L.K. et al. Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA. Nat Commun 13, 5100 (2022). https://doi.org/10.1038/s41467-022-32544-1
506. Ju Y, Han L, Chen B, Luo Z, Gu Q, Xu J, Yang XL, Schimmel P, Zhou H. (2021) X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications. Nucleic Acids Res. Sep 27;49(17):10106-10119. doi: 10.1093/nar/gkab707. PMID: 34390350
505. Shi J, Zhang Y, Tan D, Zhang X, Yan M, Zhang Y, Franklin R, Shahbazi M, Mackinlay K, Liu S, Kuhle B, James ER, Zhang L, Qu Y, Zhai Q, Zhao W, Zhao L, Zhou C, Gu W, Murn J, Guo J, Carrell DT, Wang Y, Chen X, Cairns BR, Yang XL, Schimmel P, Zernicka-Goetz M, Cheloufi S, Zhang Y, Zhou T, Chen Q. (2021) PANDORA-seq expands the repertoire of regulatory small RNAs by overcoming RNA modifications. Nat Cell Biol. Apr;23(4):424-436. doi: 10.1038/s41556-021-00652-7. Epub 2021 Apr 5. Erratum in: Nat Cell Biol. 2021 Jun;23(6):676. PMID: 33820973.
504. Sun L, Wei N, Kuhle B, Blocquel D, Novick S, Matuszek Z, Zhou H, He W, Zhang J, Weber
T, Horvath, R, Latour P, Pan T, Schimmel P, Griffin P, Yang X-L. (2021) CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS. Proc. Natl. Acad. Sci. U.S.A., Mar 2021, 118(13) e2012898118; DOI: 10.1073/pnas.2012898118.
503. Cui H, Kapur M, Diedrich JK, Yates Iii JR, Ackerman S, Schimmel P. (2020) Regulation of ex-translational activities is the primary function of the multi-tRNA synthetase complex. Nucleic Acids Res., Dec 21:gkaa1183. doi:10/1093/nar/gkaa1183. Epub ahead of print.
502. Schimmel P. (2020) The endless frontier of tRNA synthetases. In L.R. de Pouplana & L.S. Kaguni (Eds). The Enzymes - Biology of Aminoacyl-tRNA Synthetases (Volume 48, pp. 1-10) Academic Press
501. Won E, Morodomi Y, Kanaji S, Shapiro R, Vo MN, Orje JN, Thornburg CD, Yang XL, Ruggeri ZM, Schimmel P, Kanaji T. (2020) Extracellular tyrosyl-tRNA synthetase cleaved by plasma proteinases and stored in platelet α-granules: Potential role in monocyte activation. Res Pract Thromb Haemost, doi: 10.1002/rth2.12429, in press
500. Kuhle B, Chihade J, Schimmel P. (2020) Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs. Nat Commun.,11, 969. doi.org/10.1038/s41467-020-14725-y
499. Adams R, Fernandes-Cerqueira C, Notarnicola A, Mertsching E, Xu Z, Lo WS, Ogilvie K, Chiang KP, Ampudia J, Rosengren S, Cubitt A, King DJ, Mendlein JD, Yang XL, Nangle LA, Lundberg IE, Jakobsson PJ, Schimmel P. (2019) Serum-circulating His-tRNA synthetase inhibits organ-targeted immune responses. Nature Cell Mol Immunol. Dec 4. doi: 10.1038/s41423-019-0331-0. [Epub ahead of print]
498. Blocquel D, Sun L, Matuszek Z, Li S, Weber T, Kuhle B, Kooi G, Wei N, Baets J, Pan T, Schimmel P, Yang XL. (2019) CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells. PNAS, 116(39):19440-19448.
497. Kanaji T, Vo MN, Kanaji S, Zarpellon A, Shapiro R, Morodomi Y, Yuzuriha A, Eto K, Belani R, Do MH, Yang XL, Ruggeri ZM, Schimmel P. (2018) Tyrosyl-tRNA synthetase stimulates thrombopoietin-independent hematopoiesis accelerating recovery from thrombocytopenia. PNAS, 115(35): E8228-E8235. doi: 10.1073/pnas.1807000115. Epub 2018 Aug 13.
496. Xu Z, Lo WS, Beck DB, Schuch LA, Oláhová M, Kopajtich R, Chong YE, Alston CL, Seidl E, Zhai L, Lau CF, Timchak D, LeDuc CA, Borczuk AC, Teich AF, Juusola J, Sofeso C, Müller C, Pierre G, Hilliard T, Turnpenny PD, Wagner M, Kappler M, Brasch F, Bouffard JP, Nangle LA, Yang XL, Zhang M, Taylor RW, Prokisch H, Griese M, Chung WK, Schimmel P. (2018) Bi-allelic Mutations in Phe-tRNA Synthetase Associated with a Multi-system Pulmonary Disease Support Non-translational Function. Am J Hum Genet, 103(1):100-114.
495. Chong YE, Guo M, Yang XL, Kuhle B, Naganuma M, Sekine SI, Yokoyama S, Schimmel P. (2018) Distinct ways of G:U recognition by conserved tRNA binding motifs. PNAS, 15(29):7527-7532
494. Vo MN, Terrey M, Lee JW, Roy B, Moresco JJ, Sun L, Fu H, Liu Q7, Weber TG, Yates JR 3rd, Fredrick K, Schimmel P*, Ackerman SL.* (2018) ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase. Nature, 557(7706): 510-515. (*Co-corresponding authors)
493. Schimmel, P. (2018) The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis. Nature Rev. Mol. Cell Biol. Jan;19(1):45-58. doi: 10.1038/nrm.2017.77.
492. Song, Y., Zhou, H., Vo, MN, Shi, Y., Nawaz, MH, Vargas-Rodrigues, O., Diedrich, JK, Yates, JR, Kishi, S., Musier-Forsyth, K., Schimmel, P. (2017) Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid. Nat. Commun. Dec 22;8(1):2281. doi: 10.1038/s41467-017-02201-z.
491. Xu, X., Zhou, H., Zhou, Q., Hong, F., Vo, MN, Niu, W., Wang, Z., Xiong, X., Nakamura, K., Wakasugi, K., Schimmel, P., Yang, XL. (2017) An alternative conformation of human TrpRS suggests a role of zinc in activating non-enzymatic function. RNA Biol. Sep 14:1-10. doi: 10.1080/15476286.2017.1377868.
490. Blocquel, D., Li, S., Wei, N., Daub, H., Sajish, M., Erfurth, M-L., Kooi, G., Zhou, J., Bai, G., Schimmel, P., Jordanova, A., Yang, X.L. (2017) Alternative stable conformation capable of protein misinteraction links tRNA synthetase to peripheral neuropathy. Nucleic Acids Res., 45:8091-8104.
489. Sun, L., Song, Y., Blocquel, D., Yang, X-L., and Schimmel, P. (2016). Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS. Proc Natl Acad Sci U.S.A. 113:14300-14305
488. Sun L., Gomes, AC., He, W., Zhou, H., Wang, X., Pan, DW., Schimmel, P., Pan, T., Yang, XL. (2016). Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair. J Am Chem Soc. 138: 12948-12955.
487. Song, Y., Shi, Y., Carland, T.M., Shanshan, L., Sasaki, T., Schork, N.J., Head, S. R., Kishi, S.*, and Schimmel, P.* (2016). P53-Dependent DNA Damage Response Sensitive to Editing-Defective tRNA Synthetase in Zebrafish. PNAS 113: 8460-8465. (*co-corresponding authors)
486. Wei, Z., Xu, Z., Liu, X., Lo, W.-S., Ye, F., Lau, C.-F., Wang, F., Zhou, J. J., Nangle, L. A., Yang, X.-L., Zhang, M., and Schimmel, P. (2016). Alternative Splicing Creates Two New Architectures for Human tyrosyl-tRNA Synthetase. Nucleic Acids Res. 44: 1247-1255.
485. Schimmel, P. (2015). The mystery of the LUCA: Franklin M. Harold in search of cell history: The evolution of life's building blocks. The University of Chicago Press, Chicago, 2014 FASEB J. 29: 2205-2206.
484. Schimmel, P. (2015). Alexander Rich (1924-2015). Nature 521: 291.
483. Herman, J. D., Pepper, L. R., Cortese, J. F., Estiu, G., Galinsky, K., Zuzarte-Luis, V., Derbyshire, E. R., Ribacke, U., Lukens, A. K., Santos, S. A., Patel, V., Clish, C. B., Sullivan Jr., W. J., Zhou, H., Bopp, S. E., Schimmel, P., Lindquist, S., Clardy, J., Mota, M. M., Keller, T. L., Whitman, M., Wiest, O., Wirth, D. F., Mazitschek, R. (2015). The cytoplasmic prolyl-tRNA synthetase of the malaria parasite is a dual-stage target of febrifugine and its analogs. Sci. Transl. Med. 7, 288ra77.
482. Sajish, M. and Schimmel, P. (2015). A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. Nature 519: 370-373.
481. Liu, Y., Satz, J. S., Vo, M. N., Nangle, L., Schimmel, P., and Ackerman, S. L. (2014). Deficiencies in tRNA synthetase editing cause cardioproteinopathy. Proc. Natl. Acad. Sci. U S A. 111: 17570-17575.
480. Ishimura, R., Nagy, G., Dotu, I., Zhou, H., Yang, X.-L., Schimmel, P., Senju, S., Nishimura, Y., Chuang, J. H., and Ackerman, S. L. (2014). Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration. Science 345: 455-459.
479. Lo, W.-S., Gardiner, E., Xu, Z., Lau, C.-F., Wang, F., Zhou, J., Mendlein, J. D., Nangle, L. A., Chiang, K., Yang, X.-L., Au, K.-F., Wong, W. H., Guo, M., Zhang, M., and Schimmel, P. (2014). Human tRNA synthetase catalytic nulls with diverse functions. Science 345: 328-332.
478. Naganuma, M., Sekine, S., Chong, Y.-E., Guo, M., Yang, X.-L., Gamper, H., Hou, Y.-M., Schimmel, P., and Yokoyama, S. (2014). The selective tRNA aminoacylation mechanism based on a single G·U pair. Nature 510: 507-511.
477. Zhou, M. J., Wang, F., Xu, Z., Lo, W.-S., Lau, C.-F., Chiang, K. P., Nangle, L. A., Ashlock, M. A., Mendlein, J. D., Yang, X.-L., Zhang, M., and Schimmel, P. (2014). Secreted HisRS splice variants elaborate major epitopes for autoantibodies in inflammatory myositis. J. Biol. Chem. 289: 19269-19275.
476. Wang, F., Xu, Z., Zhou, J., Lo, W.-S., Lau, C.-F., Nangle, L. A., Yang, X.-L., Zhang, M., and Schimmel, P. (2013). Regulated capture by exosomes of mRNAs for cytoplasmic tRNA synthetases. J. Biol. Chem. 288: 29223-29228.
475. Klipcan, L., Safro, M., and Schimmel, P. (2013). Anticodon G-recognition mimics the tRNA core. Trends Biochem. Sci. 34: 229-232.
474. Zhou, H., Sun, L., Yang, X.-L., and Schimmel, P. (2013). ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. Nature 9: 145-153.
473. Guo, M. and Schimmel, P. (2013). Essential nontranslational functions of tRNA synthetases. Nat. Chem. Biol. 9: 145-53.
472. Ofir-Birin, Y., Fang, P., Bennett, S. P., Zhang, H.-M., Wang, J., Rachmin, I., Shapiro, R., Song, J., Dagan, A., Pozo, J., Kim, S., Marshall, A. G., Schimmel, P., Yang, X.-L., Nechushtan, H., Razin, E., and Guo, M. (2013). Structural switch of lysyl-tRNA synthetase between translaton and transcription. Mol. Cell 49: 30-42.
471. Xu, Z., Wei, Z., Zhou, J. J., Ye, F., Lo, C. W. S., Wang, F., Wu, J., Lau, C. C. F., Nangle, L. A., Chiang, K. P., Yang, X.-L., Zhang, M., and Schimmel, P. (2012). Internally deleted human tRNA synthetase suggests evolutionary pressure for repurposing. Structure 20: 1470-1477.
470. Guo, M. and Schimmel, P. (2012). Homeostatic mechanisms by alternative forms of tRNA synthetases. Trends Biochem. Sci. 37: 401-403
469. Cantor, C. R. and Schimmel, P. (2012). Cantor and Schimmel - 30 Years Later. In Comprehensive Biophysics Volume 1. (H. J. Dyson ed.), Academic Press, Oxford. pp. 2-3.
468. Lee, P. S., Zhang, H.-M., Marshall, A. G., Yang, X.-L., and Schimmel, P. (2012). Uncovering of a short internal peptide activates a tRNA synthetase procytokine. J. Biol. Chem. 287: 20504-20508.
467. Wang, J., Fang, P., Schimmel, P., and Guo, M. (2012). Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor. J. Phys. Chem. B. 116: 6798-6805.
466. Mathew, S., Zhou, Q., Kishi, S., Valdez Jr, D. M., Kapoor, M., Guo, M., Lee, S., Kim, S., Yang, X.-L., Schimmel, P. (2012) Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-γ and p53 signaling. Nat. Chem. Biol. 8: 547-554.
465. Park, M. C., Kang, T., Jin, D., Han, J. M., Kim, S. B., Park, Y. J., Cho, K., Park, Y. W., Guo, M., He, W., Yang, X.-L., Schimmel, P., and Kim, S. (2012). Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis. Proc. Natl. Acad. Sci. U S A. 109: E640-647.
464. Guo, M. and Schimmel, P. (2012). Structural analyses clarify the complex control of mistranslation by tRNA synthetases. Curr. Opin. Struct. Biol. 22: 119-126.
463. Yang, X.-L. and Schimmel, P. (2011). Functional expansion of the tRNA world under stress. Mol. Cell 43: 500-502.
462. Schimmel, P. (2011). The RNP bridge between two worlds. Nat. Rev. Mol. Cell Biol. 12: 135.
461. Schimmel, P. (2011). Mistranslation and its control by tRNA synthetases. Phil. Trans. R. Soc. Lond. B. Biol. Sci. 366: 2965-2971.
460. Fang, P., Zhang, H.-M., Shapiro, R., Marshall, A. G., Schimmel, P., Yang, X.-L., and Guo, M. (2011). Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex. Proc. Natl. Acad. Sci. U S A. 108: 8239-8244.
459. Vo, M. N., Yang, X.-L., and Schimmel, P. (2011). Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase. J. Biol. Chem. 286: 11563-11568.
458. Nawaz, M. H., Merriman, E., Yang, X.-L., and Schimmel, P. (2011). p23H implicated as cis/trans regulator of AlaXp-directed editing for mammalian cell homeostasis. Proc. Natl. Acad. Sci. U S A. 108: 2723-2728.
457. Han, G. W., Yang, X.-L., Schimmel, P., Wilson I. A., et al (2010). Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66: 1326-1334.
456. Guo, M., Shapiro, R., Yang, X.-L., and Schimmel, P. (2010). Packaging HIV virion components through dynamic equilibria of a human tRNA synthetase. J. Phys. Chem. B 114: 16273-16279.
455. Guo, M., Yang, X.-L., and Schimmel, P. (2010). New functions of aminoacyl tRNA synthetases beyond translation. Nat. Rev. Mol. Cell Biol. 11: 668-674.
454. Guo, M., Schimmel, P., and Yang, X.-L. (2010). Functional expansion of human tRNA synthetases achieved by structural inventions. FEBS Lett. 584: 434-442.
453. Guo, M., Shapiro, R., Schimmel, P., and Yang, X.-L. (2010). Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase. Acta Crystallogr. D Biol. Crystallogr. 66: 243-250.
452. Zhou, Q., Kapoor, M., Guo, M., Belani, R., Xu, X., Kiosses, W. B., Hanan, M., Park, C., Armour, E., Do, M.-H., Nangle, L. A., Schimmel, P., and Yang, X.-L. (2010). Orthogonal use of a human tRNA synthetase active site to achieve multifunctionality. Nat. Struct. Mol. Biol. 17: 57-61.
451. Sankaran, B., Bonnett, S. A., Shah, K., Gabriel, S., Reddy, R., Schimmel, P., Rodionov, D. A., de Crécy-Lagard, V., Helman, J. D., Iwata-Reuyl, D., and Swairjo, M. A. (2009). Zinc-independent folate biosynthesis: Genetic, biochemical, structural investigations reveal new metal dependence for GTP cyclohydrolyase IB. J. Bacteriol. 191: 6936-6949.
450. Guo, M., Chong, Y. E., Shapiro, R., Beebe, K., Yang, X.-L., and Schimmel, P. (2009). Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. Nature 462: 808-812..
449. Storkebaum, E., Leitao-Goncalves, R., Godenschwege, T., Nangle, L., Mejia, M., Bosmans, I., Ooms, T., Jacobs, A., Van Dijck, P., Yang, X.-L., Schimmel, P., Norga, K., Timmerman, V., Callaerts, P., and Jordanova, A. (2009). Dominant mutations in the tyrosyl-tRNA synthetase gene recapitulate in Drosophila features of human Charcot-Marie-Tooth neuropathy. Proc. Natl. Acad. Sci. U S A. 106: 11782-11787.
448. El Yacoubi, B., Lyons, B., Cruz, Y., Reddy, R., Nordin, B., Agnelli, F., Williamson, J. R., Schimmel, P., Swairjo, M. A., and de Crécy-Lagard, V. (2009). The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA. Nucleic Acids Res. 37: 2894-2909.
447. Guo, M., Chong, Y. E., Yang, X.-L., and Schimmel, P. (2009). The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science 325: 744-747.
446. Schimmel, P. and Guo, M. (2009). Ancient tRNA synthetase meets modern structural biology. Structure 17: 315-317.
445. Kapoor, M., Otero, F. J., Slike, B. M., Ewalt, K. L., and Yang, X.-L. (2009). Mutational separation of aminoacylation and cytokine activities of human tyrosyl-tRNA synthetase. Chem. Biol. 16: 531–539.
444. Schimmel, P. and Guo, M. (2009) A tipping point for mistranslation and disease. Nat. Struct. Mol. Biol. 16: 348-349.
443. Cheng, G., Zhang, H., Yang, X.-L., Tzima, E., Ewalt, K. L., Schimmel, P., and Faber, J. E. (2008). Effect of mini-tyrosyl-tRNA synthetase on ischemic angiogenesis, leukocyte recruitment, and vascular permeability. Am. J. Physiol. Regul. Integr. Comp. Physiol. 295: R1138–1146.
442. Schimmel, P. (2008). Development of tRNA synthethases and connection to genetic code and disease. Protein Sci. 17: 1643-1652.
441. Schimmel, P. (2008). An editing activity that prevents mistranslation and connection to disease. J. Biol. Chem. 283: 28777-28782.
440. Chong, Y. E., Yang, X.-L., and Schimmel, P. (2008). Natural homology of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. J. Biol. Chem. 283: 30073-30078.
439. Park, S. G., Schimmel, P., and Kim, S. (2008). Aminoacyl tRNA synthetases and their connections to disease. Proc. Natl. Acad. Sci. U S A. 105: 11043-11049.
438. Guo, M., Ignatov, M., Musier-Forsyth, K., Schimmel, P., and Yang, X.-L. (2008). Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation. Proc. Natl. Acad. Sci. U S A. 105: 2331-2336.
437. Zhou, Q., Kiosses, W. B., Liu, J., and Schimmel, P. (2008). Tumor endothelial cell tube-formation model for determining anti-angiogenic activity of a tRNA synthetase cytokine. Methods 44: 190-195.
436. Kapoor, M., Zhou, Q., Otero, F., Myers, C., Bates, A., Belani, R., Liu, J., Luo, J.-K., Tzima, E., Yang, X.-L., Zhang, D.-E., and Schimmel, P. (2008). Evidence for annexin II-S100A10 complex and plasmin in mobilization of cytokine activity of human TrpRS. J. Biol. Chem. 283: 2070-2077.
435. Beebe, K., Mock, M., Merriman, E., and Schimmel, P. (2008). Distinct domains of tRNA synthetase recognize the same base pair. Nature 451: 90-94.
434. Greenberg, Y., King, M., Kiosses, W. B., Ewalt, K., Yang, X.-L., Schimmel, P., Reader, J. S., and Tzima, E. (2008). The novel fragment of tyrosyl-tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells. FASEB J. 22: 1-9.
433. Waas, W. F. and Schimmel, P. (2007). Evidence that tRNA synthetase-directed proton transfer stops mistranslation. Biochemistry 46: 12062-12070.
432. Yang, X.-L., Kapoor, M., Otero, F. J., Slike, B., Tsuruta, H., Frausto, R., Bates, A., Ewalt, K. L., Cheresh, D. A., and Schimmel, P. (2007). Gain-of-function mutational activation of human tRNA synthetase procytokine. Chem. Biol. 14: 1323-1333.
431. Bacher, J., Waas, W. F., Metzgar, D., de Crécy-Lagard, V., and Schimmel, P. (2007). Genetic code ambiguity confers a selective advantage on Acinetobacter baylyi. J. Bacteriol. 139: 6494-6496.
430. Chloe Zubieta, Paul Schimmel, and Ian A. Wilson, et al. (2007). Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Proteins: Structure, Function, Bioinf. 69: 234-243.
429. Chloe Zubieta, Paul Schimmel, and Ian A. Wilson, et al. (2007). Crystal structures of two novel dye-decolorizing peroxidases reveal a β-barrel fold with a conserved heme-binding motif. Proteins: Structure, Function, Bioinf. 69: 223-233.
428. Waas, W. F., Druzina, Z., Hanan, M., and Schimmel, P. (2007). Role of a tRNA modification and its precursors in frameshifting in eukaryotes. J. Biol. Chem. 282: 26026-26034.
427. Nangle, L., Zhang, W., Xie, W., Yang, X.-L., and Schimmel, P. (2007). Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect. Proc. Natl. Acad. Sci. U S A. 104: 11239-11244.
426. Xie, W., Nangle, L. A., Zhang, W., Schimmel, P., and Yang, X.-L. (2007). Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 104: 9976-9981.
425. Yang, X.-L., Guo, M., Kapoor, M., Ewalt, K. L., Otero, F. J., Skene, R. J., McRee, D. E., and Schimmel, P. (2007). Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase. Structure 15: 793-805.
424. Beebe, K., Waas, W., Druzina, Z., Guo, M., and Schimmel, P. (2007). A universal plate format for increased throughput of assays that monitor multiple aminoacyl transfer RNA synthetase activities. Anal. Biochem. 368: 111-121.
423. Bacher, J. and Schimmel, P. (2007). An editing-defective aminoacyl-tRNA synthetase is mutagenic in aging bacteria via the SOS response. Proc. Natl. Acad. Sci. U S A. 104: 1907-1912.
422. Schimmel, P. and Yang, X.-L. (2006). Perfecting the genetic code with an RNP complex. Structure 14: 1729-1730.
421. Xie, W., Schimmel, P., and Yang, X.-L. (2006). Crystallization and preliminary X-ray analysis of a native human tRNA synthetase whose allelic variants are associated with Charcot-Marie-Tooth disease. Acta. Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62: 1243-1246.
420. Nangle, L., Motta, C., and Schimmel, P. (2006). Global effects of mistranslation from an editing defect in a mammalian cell. Chem. Biol., 13: 1091-1100.
419. Tamura, K. and Schimmel, P. (2006). Chiral-selective aminoacylation of an RNA minihelix: Mechanistic features and chiral suppression. Proc. Natl. Acad. Sci. U S A. 103: 13750-13752.
418. Yang, X.-L., Otero, F. J., Ewalt, K. L., Liu, J., Swairjo, M. A., Kohrer, C., RajBhandary, U. L., Skene, R. J., McRee, D. E., and Schimmel, P. (2006). Two conformations of a crystalline human tRNA synthetase—tRNA complex: Implications for protein synthesis. EMBO J. 25: 2919-2929.
417. Lee, J. W., Beebe, K., Nangle, L. A., Jang, J., Longo-Guess, C. M., Cook, S. A., Davisson, M. T., Sundberg, J. P., Schimmel, P., and Ackerman, S. L. (2006). Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration. Nature 443: 50-55.
416. Seburn, K. L., Nangle, L.,A., Cox, G. A., Schimmel, P., and Burgess, R. W. (2006). An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model. Neuron 51: 715-726.
415. Tzima, E. and Schimmel, P. (2006). Inhibition of tumor angiogenesis by a natural fragment of a tRNA synthetase. Trends Biochem. Sci. 31: 7-10.
414. Reader, J. S., Ordoukhanian, P. T., Kim, J.-G., de Crécy-Lagard, V., Hwang, I., Farrand, S., and Schimmel, P. (2005). Major biocontrol of plant tumors targets tRNA synthetase. Science 309: 1533.
413. Swairjo, M. A., Reddy, R. R., Lee, B., Van Lanen, S. G., Brown, S., de Crécy-Lagard, V., Iwata-Reuyl, D., and Schimmel, P. (2005). Crystallization and preliminary X-ray characterization of the nitrile reductase QueF: A queosine-biosynthesis enzyme. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61: 945-948.
412. Waas, W. F., de Crécy-Largard, V., and Schimmel, P. (2005). Discovery of a gene family critical to wyosine base formation in a subset of phenylalanine-specific transfer RNAs. J. Biol. Chem. 280: 37616-37622.
411. Ewalt, K., Yang, X.-L., Otero, F., Liu, J., Slike, B., and Schimmel, P. (2005). Variant of human enzyme sequesters reactive intermediate. Biochemistry 44: 4216-4221.
410. Schimmel, P. and Beebe, K. (2006). From the RNA world to the theatre of proteins. In The RNA World (R. R. Gesteland, T. R. Cech, and J. F. Atkins, eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp. 227-255.
409. Ribas de Pouplana, L., Musier-Forsyth, K., and Schimmel, P. (2005). Alanyl tRNA synthetases. In Aminoacyl tRNA Synthetases (M. Ibba, C. Francklyn, and S. Cusack, eds.), Landes Biosciences, Eurekah.com, Georgetown, TX, pp. 241-249.
408. Nordin, B. E. and Schimmel, P. (2005). Isoleucyl tRNA synthetase. In Aminoacyl tRNA Synthetases (M. Ibba, C. Francklyn, and S. Cusack, eds.), Landes Biosciences, Eurekah.com, Georgetown, TX, pp. 24-35.
407. Schimmel, P. and Söll, D. (2005). The world of tRNA synthetases. In Aminoacyl tRNA Synthetases (M. Ibba, C. Francklyn, and S. Cusack, eds.), Landes Biosciences, Eurekah.com, Georgetown, TX, pp. 1-2.
406. Bacher, J. M., de Crécy-Lagard, V., and Schimmel, P. (2005). Inhibited cell growth and protein functional changes from an editing-defective tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 102: 1697-1701.
405. Swairjo, M. A. and Schimmel, P. R. (2005). Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 102: 988-993.
404. Tzima, E., Reader, J. S., Irani-Tehrani, M., Ewalt, K. L., Schwartz, M. A., and Schimmel, P. (2005). VE-cadherin links tRNA synthetase cytokine to anti-angiogenic function. J. Biol. Chem. 280: 2405-2408.
403. Tamura, K. and Schimmel, P. (2004). Non-enzymatic aminoacylation of an RNA minihelix with an aminoacyl phosphate oligonucleotide. Nucleic Acids Symp. Ser. 48: 269-270.
402. Metzgar, D., Bacher, J. M., Pezo, V., Reader, J. Doring, V., Schimmel, P., Marlière, and de Crécy-Lagard, V. (2004). Acinetobacter sp. ADP1: An ideal model organism for genetic analysis and genome engineering. Nucleic Acids Res. 32: 5780-5790.
401. Schimmel, P. and Ewalt, K. (2004). Translation silenced by fused pair of tRNA synthetases. Cell 119: 147-148.
400. Tang, H.-L., Yeh, L.-S., Chen, N.-K., Ripmaster, T. L., Schimmel, P., and Wang, C.-C. (2004). Translation of a yeast mitochondrial tRNA synthetase initiated at redundant non-AUG codons. J. Biol. Chem. 279: 49656-49663.
399. Schimmel, P. and Beebe, K. (2004). Genetic code seizes pyrrolysine. Nature 431: 257-258.
398. Schimmel, P. and Yang, X.-L. (2004). Two classes give lessons about CCA. Nat. Struct. Mol. Biol. 11: 807-808.
397. Tamura, K. and Schimmel, P. (2004). Chiral selective aminoacylation of an RNA minihelix. Science 305: 1253.
396. Pezo, V., Metzgar, D., Hendrickson, T. L., Waas, W. F., Hazebrouck, S., Döring V., Marlière, P., Schimmel, P.*, and de Crécy-Lagard, V.* (2004). Artificially ambiguous genetic code confers growth yield advantage. Proc. Natl. Acad. Sci. U S A. 101: 8593-8597. (*corresponding authors)
395. Beebe, K., Merriman, E., Ribas de Pouplana, L., and Schimmel, P. (2004). A domain for editing by an archaebacterial tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 101: 5958-5963.
394. Yang, X.-L., Schimmel, P., and Ewalt, K. L. (2004). Relationship of two human tRNA synthetases used for cell signaling. Trends Biochem. Sci. 29: 250-256.
393. Schimmel, P. (2004). Genetic Code. In Encyclopedia of Science & Technology Online, DOI 10.1036/1097-8542.284900.
392. Lovato, M. A., Swairjo, M. A., and Schimmel, P. (2004). Positional recognition of a tRNA determinant dependent on a peptide insertion. Mol. Cell 13: 843-851.
391. Swairjo, M. A., Otero, F. J., Yang, X.-L., Lovato, M. A., Skene, R. J., McRee, D. E., Ribas de Pouplana, L., and Schimmel, P. (2004). Alanyl-tRNA synthetase crystal structure and design for acceptor-stem recognition. Mol. Cell 13: 829-841.
390. Hendrickson, T. L., de Crécy-Lagard, V. and Schimmel, P. (2004). Incorporation of non-natural amino acids into proteins. Ann. Rev. Biochem. 73: 147-176.
389. Liu, J., Shue, E., Ewalt, K. L., and Schimmel, P. (2004). A new gamma-interferon-inducible promoter and splice variants of an anti-angiogenic human tRNA synthetase. Nucleic Acids Res. 32: 719-727.
388. Ribas de Pouplana, L. and Schimmel, P. (2004). Aminoacyl tRNA synthetases as potential markers for the development of the genetic code. In Life Sciences for the 21st Century (E. Keinan, I. Schechter, M. Sela, eds.), Wiley-VCH Verlag GmbH & Co. KgaA, Weinheim, pp. 81-92.
387. Reader, J. S., Metzgar, D., Schimmel, P.*, and de Crécy-Lagard, V.* (2004). Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine. J. Biol. Chem. 279: 6280-6285. (*corresponding authors).
386. de Pereda, J. M., Waas, W. F., Jan, Y., Ruoslahti, E., Schimmel, P., and Pascual, J. (2004). Crystal structure of a human peptidyl-tRNA hyrolase reveals a new fold and suggests basis for a bifunctional activity. J. Biol. Chem. 279: 8111-8115.
385. Ribas de Pouplana, L. and Schimmel, P. (2004). Aminoacylations of tRNAs: Record-keepers for the genetic code. In Protein Synthesis and Ribosome Structure (K. H. Nierhaus and D. N. Wilson, eds.), Wiley-VCH, Weinheim, 169-184.
384. Ewalt, K. L. and Schimmel, P. (2003). tRNA synthetases. In Encyclopedia of Biological Chemistry (P. Modrich and W. J. Lennarz, eds.), Elsevier (Academic Press), 4: 263-266.
383. Yang, X.-L., Otero, F. J., Skene, R. J., McRee, D. E., Schimmel, P.* and Ribas de Pouplana, L.* (2003). Crystal structures that suggest late development of genetic code components for differentiating aromatic amino acids. Proc. Natl. Acad. Sci. U S A. 100: 15376-15380. (*corresponding authors)
382. Tzima, E., Reader, J. S., Irani-Tehrani, M., Ewalt, K. L., Schwartz, M. A., and Schimmel, P. (2003). Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells. Proc. Natl. Acad. Sci. U S A. 100: 14903-14907.
381. Beebe, K., Merriman, E., and Schimmel, P. (2003). Structure-specific tRNA determinants for editing a mischarged amino acid. J. Biol. Chem. 278: 45056-45061.
380. Nordin, B. E. and Schimmel, P. (2003). Transiently misacylated tRNA is a primer for editing of misactivated adenylates by class I aminoacyl-tRNA synthetases. Biochemistry 42: 12989-12997.
379. Frugier, M., Giegé, R., and Schimmel, P. (2003). RNA recognition by designed peptide creates “artificial” tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 100: 7471-7475.
378. Schimmel, P. and Tamura, K. (2003). tRNA structure goes from L to l. Cell 113: 276-278.
377. Hendrickson, T. L. and Schimmel, P. (2003). Transfer RNA-dependent amino acid discrimination by aminoacyl-tRNA synthetases. In Translational Mechanisms (J. LaPointe and L. Brakier-Gingras, eds.), Eurekah .com and Klumer Academic/Plenum Publishers, New York, pp. 34-64.
376. Yang, X-L., Liu, J., Skene, R. J., McRee, D. E., and Schimmel, P. (2003). Crystal structure of an EMAP-II-like cyotokine released from a human tRNA synthetase. Helv. Chim. Acta. 86: 1246-1257.
375. Tamura, K. and Schimmel, P. (2003). Peptide synthesis with a template-like RNA guide and aminoacyl phosphate adaptors. Proc. Natl. Acad. Sci. U S A. 100: 8666-8669.
374. Beebe, K., Ribas de Pouplana, L., and Schimmel, P. (2003). Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 22: 668-675.
373. Wang, C.-C., Chang, K.-J., Tang, H.-L., Hsieh, C.-J., and Schimmel, P. (2003). Mitochondrial form of a tRNA synthetase can be made bifunctional by manipulating its leader peptide. Biochemistry 42: 1646-1651.
372. Bishop, A. C., Beebe, K., and Schimmel, P. (2003). Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase. Proc. Natl. Acad. Sci. U S A 100: 490-494.
371. Kushiro, T. and Schimmel, P. (2002). Trbp111 selectively binds a non-covalently assembled tRNA-like structure. Proc. Natl. Acad. Sci. U S A. 99: 16631-16635.
370. Yang, X.-L., Skene, R. J., McRee, D. E., and Schimmel, P. (2002). Crystal structure of an aminoacyl tRNA synthetase cytokine. Proc. Natl. Acad. Sci. U S A. 99: 15369-15374.
369. Cen, S., Javanbakht, H., Kim, S., Shiba, K., Craven, R., Rein, A., Ewalt, K., Schimmel, P., Musier-Forsyth, K., and Kleiman, L. (2002). Retrovirus-specific packaging of aminoacyl tRNA synthetases with cognate primer tRNAs. J. Virology 76: 13111-13115.
368. Schimmel, P. (2002). The protein synthesis world. Trends Biochem. Sci. 27: 505-06.
367. Ewalt, K. L. and Schimmel, P. (2002). Activation of angiogenic signaling pathways by two human tRNA synthetases. Biochemistry 41: 13344-13349.
366. Liu, J., Yang, X.-L., Ewalt, K. L., and Schimmel, P. (2002). Mutational switching of a yeast tRNA synthetase into a mammalian-like synthetase cytokine. Biochemistry 41: 14232-14237.
365. Nangle, L., de Crécy-Lagard, V., Döring, V., and Schimmel, P. (2002). Genetic code ambiguity. Cell viability related to the severity of editing defects in mutant tRNA synthetases. J. Biol. Chem. 277: 45729-45733.
364. Tamura, K. and Schimmel, P. (2002). Ribozyme programming extends the protein code. Nat. Biotechnol. 20: 669-670.
363. Bishop, A. C., Xu, J., Johnson, R. C., Schimmel, P., and de Crécy-Lagard, V. (2002). Identification of the tRNA-dihydrouridine synthase family. J. Biol. Chem. 277: 25090-25095.
362. Wakasugi, K., Slike, B. M., Hood, J., Ewalt, K. L., Cheresh, D. A., and Schimmel, P. (2002). Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase. J. Biol. Chem. 277: 20124-20126.
361. Otani, A., Kinder, K., Ewalt, K., Otero, F. J., Schimmel, P., and Friedlander, M. (2002). Bone marrow-derived stem cells target retinal astrocytes and can promote or inhibit retinal angiogenesis. Nat. Med. 8: 1004-1010 .
360. Nordin, B. E. and Schimmel, P. (2002). Plasticity of recognition of the 3’-end of mischarged tRNA by class I aminoacyl tRNA synthetases. J. Biol. Chem. 277: 20510-20517.
359. Bishop, A. C., Nomanbhoy, T. K., and Schimmel, P. (2002). Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 99: 585-590.
358. Otani, A., Slike, B., Dorrell, M. I., Hood, J., Kinder, K., Ewalt, K. L., Cheresh, D. A., Schimmel, P*., and Friedlander, M.* (2002). A fragment of human TrpRS as a potent antagonist of ocular angiogenesis. Proc. Natl. Acad. Sci. U S A. 99: 178-183. (*corresponding authors)
357. Wakasugi, K., Slike, B., Hood, J., Otani, A., Ewalt, K. L., Friedlander, M., Cheresh, D. A., and Schimmel, P. (2002). A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. Proc. Natl. Acad. Sci. U S A. 99: 173-177.
356. Hendrickson, T. L., Nomanbhoy, T. K., de Crécy-Lagard, V., and Schimmel, P. (2002). Mutational separation of two pathways for editing by a class I tRNA synthetase. Mol. Cell 9: 353-362.
355. Lovato, M. A., Chihade, J. W., and Schimmel, P. (2001). Translocation within acceptor helix of a major tRNA identity determinant. EMBO J. 20: 4846-4853.
354. Schimmel, P. and Ribas de Pouplana, L. (2001). Formation of two classes of tRNA synthetases in relation to editing functions and genetic code. Cold Spring Harbor Symposium on Quantitative Biology 66: 161-166.
353. Alexander, R. W. and Schimmel, P. (2001). Domain-domain communication in aminoacyl tRNA synthetases. Prog. Nucleic Acid Res. Mol. Biol. 69: 317-349.
352. Ribas de Pouplana, L. and Schimmel, P. (2001). Aminoacyl-tRNA synthetases: Potential markers of genetic code development. Trends Biochem. Sci. 26: 591-596.
351. Ribas de Pouplana, L., Brown, J. R., and Schimmel, P. (2001). Structure-based phylogeny of class IIa tRNA synthetases in relation to an unusual biochemistry. J. Mol. Evol. 53: 261-268.
350. Schimmel, P. (2001). Reflections on the 20th Taniguichi International Symposium—Tracing Biological Evolution in Protein and Gene Structures. Biophysics 233: 42-45.
349. Döring, V., Mootz, H. D., Nangle, L. A., Hendrickson, T. L., de Crécy-Lagard, V., Schimmel, P.*, and Marlière, P.* (2001). Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway. Science 292:501-504. (*corresponding authors)
348. Fabrega, C., Farrow, M. A., Mukhopadhyay, B., de Crécy-Lagard, V., Ortiz, A. R., and Schimmel, P. (2001). An aminoacyl tRNA synthetase whose sequence fits into neither of the two known classes. Nature 411: 110-114.
347. Ribas de Pouplana, L. and Schimmel, P. (2001). Operational RNA code for amino acids in relation to genetic code in evolution. J. Biol. Chem. 276: 6881-6884.
346. Nomanbhoy, T. and Schimmel, P. (2001). Active site of an aminoacyl-tRNA synthetase dissected by energy-transfer-dependent fluorescence. Bioorg. Med. Chem. Lett. 11:1485-1491.
345. Nomanbhoy, T., Morales, A. J., Abraham, A. T., Vörtler, C. S., Giegé, R., and Schimmel, P. (2001). Simultaneous binding of two proteins to opposite sides of a single transfer RNA. Nat. Struct. Biol. 8: 344-348.
344. Alexander, R. W. and Schimmel, P. (2001). Protein synthesis. Encyclopedia of Physical Science and Technology (R. A. Myers, ed.), Third Edition. Academic Press, San Diego. pp 219-240.
343. Tamura, K. and Schimmel, P. (2001). Oligonucleotide-directed peptide synthesis in a ribosome- and ribozyme-free system. Proc. Natl. Acad. Sci. U S A. 98: 1393-1397.
342. Farrow, M. and Schimmel, P. (2001). Editing by a tRNA synthetase: DNA aptamer-induced translocation and hydrolysis of a misactivated amino acid. Biochemistry 40: 4478-4483.
341. Ribas de Pouplana, L. and Schimmel, P. (2001). Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stems. Cell 104: 191-193.
340. Kelley, S. O., Steinberg, S. V., and Schimmel, P. (2001). Fragile T-stem in disease-associated human mitochondrial tRNA sensitizes structure to local and distant mutations. J. Biol. Chem. 276: 10607-10611.
339. Alexander, R. W. and Schimmel, P. (2001). Wobble hypothesis. Encyclopedia of Genetics (S. Brenner and J. Miller, eds.), Academic Press, London. pp 2141.
338. Alexander, R. W. and Schimmel, P. (2001). Suppression. Encyclopedia of Genetics (S. Brenner and J. Miller, eds), Academic Press, London. pp 1897-1899.
337. Schimmel, P. (2000). Public funding of intellectual curiosity. IUBMB Life 50: 345-346.
336. Houman, F., Rho, S. B., Zhang, J., Shen. X., Wang, C.-C., Schimmel, P., and Martinis, S. A. (2000). A prokaryote and human tRNA synthetase provide an essential RNA splicing function in yeast mitochondria. Proc. Natl. Acad. Sci. U S A. 97: 13743-13748.
335. Schimmel, P. (2000). Industry benefits from the public funding of intellectual curiosity. Nature 406: 826.
334. Tao, J. and Schimmel, P. (2000). Inhibitors of aminoacyl-tRNA synthetases as novel anti-infectives. Expert Opin. Investig. Drugs 9: 1767-1775.
333. Swairjo, M. A., Morales, A. J., Wang, C.-C., Ortiz, A. R., and Schimmel, P. (2000). Crystal structure of Trbp111: A structure-specific tRNA-binding protein. EMBO J. 19: 6287-6298.
332. Kelley, S. O., Steinberg, S. V., and Schimmel, P. (2000). Functional defects of pathogenic human mitochondrial tRNAs related to structural fragility. Nat. Struct. Biol. 7: 862-865
331. Turner, R. J., Lovato, M., and Schimmel, P. (2000). One of two genes encoding glycyl-tRNA synthetase in Saccharomyces cerevisiae provides mitochondrial and cytoplasmic functions. J. Biol. Chem. 275: 27681-27688.
330. Wang, C.-C., Morales, A. J., and Schimmel, P. (2000). Functional redundancy in the nonspecific RNA binding domain of a class I tRNA synthetase. J. Biol. Chem. 275: 17180-17186.
329. Ribas de Pouplana, L. and Schimmel, P. (2000). A view into the origin of life: Aminoacyl tRNA synthetases. Cell. Mol. Life Sci. 57: 865-870.
328. Tamura, K. and Schimmel, P. (2000). Trial for peptide bond formation using model molecules based on the interactions between the CCA sequence of tRNA and 23S rRNA. Nucleic Acids Symp. Ser. 44: 251-252.
327. Hendrickson, T. L., Nomanbhoy, T. K., and Schimmel, P. (2000). Errors from selective disruption of the editing center in a tRNA synthetase. Biochemistry 39: 8180-8186.
326. Nomanbhoy, T. K. and Schimmel, P. (2000). Misactivated amino acids translocate at similar rates across the surface of a tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 97: 5119-5122.
325. Chihade, J. W., Brown, J., Schimmel, P., and Ribas de Pouplana, L. (2000). Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 97: 12153-12157.
324. Alexander, R. W. and Schimmel, P. (2000). Multifunctional proteins. McGraw-Hill 2001 Yearbook of Science & Technology, McGraw-Hill, New York. pp. 265-266.
323. Schimmel, P. and Kelley, S. O. (2000). Exiting an RNA world. Nat. Struct. Biol. 7: 5-7.
322. Schimmel, P. and Ribas de Pouplana, L. (2000). Footprints of aminoacyl tRNA synthetases are everywhere. Trends Biochem. Sci. 25: 207-209.
321. Sardesai, N. Y. Stagg, S. M., VanLoock, M. S., Harvey, S. C., and Schimmel, P. (2000). RNA scaffolds for minihelix-based aminoacyl transfer: Design of “transpeptizymes”. J. Biomol. Struct. Dyn. Conversation 11, 29-37.
320. Tao, J., Wendler, P., Connelly, G., Lim, A., Zhang, J., King, M., Li, T., Silverman, J. A., Schimmel, P., and Tally, F. P. (2000). Drug target validation: Lethal infection blocked by inducible peptide. Proc. Natl. Acad. Sci. U S A. 97: 783-786.
319. Chihade, J. W. and Schimmel, P. (1999). Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains. Proc. Natl. Acad. Sci. U S A. 96: 12316-12321.
318. Steer, B. A. and Schimmel, P. (1999). Domain-domain communication in a miniature archaebacterial tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 96: 13644-13649.
317. Farrow, M. A., Nordin, B. E., and Schimmel, P. (1999). Nucleotide determinants for tRNA-dependent amino acid discrimination by a class I tRNA synthetase. Biochemistry 38: 16898-16903.
316. Alexander, R. W. and Schimmel, P. (1999). Evidence for breaking domain-domain communication in synthetase-tRNA complex. Biochemistry 38: 16359-16365.
315. Steer, Brian A. and Schimmel, P. (1999). Major anticodon-binding region missing from an archaebacterial tRNA synthetase. J. Biol. Chem. 274: 35601-35606.
314. Wakasugi, K. and Schimmel, P. (1999). Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. J. Biol. Chem. 274: 23155-23159.
313. Schimmel, P. (1999). Looking for Lamarck’s signature. (Review of Lamarck’s Signature. How Retrogenes are Changing Darwin’s Natural Selection Paradigm, E. J. Steele, R. A. Lindley, R. V. Blanden). Q. Rev. Biol. 74: 471.
312. Schimmel, P. (1999). Bringing RNA back to the future. (Review of The RNA World 2nd edition, R. F. Gesteland, T. R. Cech, J. F. Atkins, eds.), Trends Biochem. Sci. 24: 408-409.
311. Sardesai, N. Y., Green, R., and Schimmel, P. (1999). Efficient 50S ribosome-catalyzed peptide bond synthesis with an aminoacyl minihelix. Biochemistry 38: 12080-12088.
310. Nomanbhoy, T., Hendrickson, T. L., and Schimmel, P. (1999). Transfer RNA-dependent translocation of misactivated amino acids to prevent errors of protein synthesis. Mol. Cell 4: 519-528.
309. Morales, A. J., Swairjo, A. M., and Schimmel, P. (1999). Structure-specific tRNA binding protein from the extreme thermophile Aquifex aeolicus. EMBO J. 18: 3475-3483.
308. Wang, C.-C. and Schimmel, P. (1999). Species barrier to RNA recognition overcome with non-specific RNA binding domains. J. Biol. Chem. 274: 16508-16512.
307. Steer, B. A. and Schimmel, P. (1999). Different adaptations of the same peptide motif for tRNA functional contacts by closely homologous tRNA synthetases. Biochemistry 38: 4965-4971.
306. Schimmel, P. and Wang, C.-C. (1999). Getting tRNA synthetases into the nucleus. Trends Biochem. Sci. 24: 127-128.
305. Schimmel, P. and Ribas de Pouplana, L. (1999). Genetic code origins: Experiments confirm phylogenetic predictions and may explain a puzzle. Proc. Natl. Acad. Sci. U S A. 96: 327-328.
304. Nureki, O., Vassylyev, D. G., Tateno, M., Shimada, A., Nakama, T., Fukai, S. Konno, M., Hendrickson, T. L., Schimmel, P., and Yokoyama, S. (1999). Proofreading by isoleucyl tRNA synthetase: Response. Science 283: 459a.
303. Nordin, B. E. and Schimmel, P. (1999). RNA determinants for translational editing: Mischarging a minihelix substrate by a tRNA synthetase. J. Biol. Chem. 274: 6835-6838.
302. Schimmel, P. (1999). Translational Editing. The Encyclopedia of Molecular Biology, Vol. 4, (T. E. Creighton, ed.), John Wiley & Sons, New York. pp. 2642-2647.
301. Schimmel, P. (1999). Aminoacyl tRNA Synthetases. Encyclopedia of Molecular Biology, Vol. 1, (T. E. Creighton, ed.), John Wiley & Sons, New York. pp. 111-119.
300. Wakasugi, K. and Schimmel, P. (1999). Two distinct cytokines released from a human aminoacyl tRNA synthetase. Science 284: 147-151.
299. Musier-Forsyth, K. and Schimmel, P. (1999). Atomic determinants for aminoacylation of RNA minihelices and relationship to genetic code. Acc. Chem. Res. 32: 368-375.
298. Alexander, R., Nordin, B., and Schimmel, P. (1998). Activation of microhelix charging by localized helix destabilization. Proc. Natl. Acad. Sci. U S A. 95: 12214-12219.
297. Schimmel, P. and Alexander, R. (1998). Diverse substrates for aminoacylation: Clues to origins? Proc. Natl. Acad. Sci. U S A. 95: 10351-10353.
296. Schimmel, P. and Alexander, R. (1998). All you need is RNA. Science 281: 658-659.
295. Schimmel, P., Tao, J., and Hill, J. (1998). Aminoacyl-tRNA synthetases as targets for new anti-infectives. FASEB J. 12: 1599-1609.
294. Ribas de Pouplana, L., Buechter, D., Sardesai, N., and Schimmel, P. (1998). Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA binding domains. EMBO J. 17: 5449-5457.
293. Ribas de Pouplana, L., Turner, R. J., Steer, B. A., and Schimmel, P. (1998). Genetic code origins: tRNAs older than their synthetases? Proc. Natl. Acad. Sci. U S A. 95: 11295-11300.
292. Henderson, B. S., Beuning, P. J., Shi, J.-P., Bald, R., Fürste, J. P., Erdmann, V. A., Musier-Forsyth, K., and Schimmel, P. (1998). Subtle functional interactions in the RNA minor groove at a nonessential base pair. J. Am. Chem. Soc. 120: 9110-9111.
291. Chihade, J., Hayashibara, K., Shiba, K., and Schimmel, P. (1998). Strong selective pressure to mark an RNA acceptor stem for alanine. Biochemistry 37: 9193-9202.
290. Nureki, O., Vassylyev, D. G., Tateno, M., Shimada, A., Nakama, T., Fukai, S. Konno, M., Hendrickson, T. L., Schimmel, P., and Yokoyama, S. (1998). Enzyme structure with two catalytic sites for double-sieve selection of substrate. Science 280: 578-582.
289. Sardesai, N. Y. and Schimmel, P. (1998). Non-covalent assembly of microhelix recognition by a class II tRNA synthetase. J. Am. Chem. Soc. 120: 3269-3270.
288. Wakasugi, K., Quinn, C., Tao, N., and Schimmel, P. (1998). Genetic Code in Evolution: Switching Species-Specific Aminoacylation with a Peptide Transplant. EMBO J. 17: 297-305.
287. Schimmel, P. (1997). Why Bother to Study the Origins of Life? (Review of Origins of Life on the Earth and in the Cosmos, G. Zubay). Q. Rev. Biol. 72: 469-470.
286. Schimmel P., Frugier, M., and Glasfeld, E. (1997). Peptides for RNA discrimination and for assembly of enzymes that act on RNA. Nucleic Acids Symp. Ser. 36: 1.
285. Schimmel, P. (1997). Molecular Recognition of Transfer RNAs. In Encyclopedia of Human Biology (R. Dulbecco, ed.), 2nd edition, Academic Press, San Diego. pp. 475-479.
284. Schimmel, P. (1997). Protein Engineering, In McGraw-Hill Encyclopedia of Science & Technology, (S. P. Parker, ed.), McGraw-Hill, New York. pp. 498-499.
283. Schimmel, P. and Wendler, H. E. (1997). Genetic Code, McGraw-Hill Encyclopedia of Science & Technology 8, (S. P. Parker, ed.), McGraw-Hill, New York. pp. 759-762.
282. Schimmel, P. and Söll, D. (1997). When protein engineering confronts the tRNA world. Proc. Natl. Acad. Sci. U S A. 94: 10007-10009.
281. Frugier, M. and Schimmel, P. (1997). Subtle atomic group recognition in the RNA minor groove. Proc. Natl. Acad. Sci. U S A. 94: 11291-11294.
280. Ribas de Pouplana, L. and Schimmel, P. (1997). Reconstruction of quaternary structures of class II tRNA synthetases by rational mutagenesis of a conserved domain. Biochemistry 36: 15041-15048.
279. Beuning, P. J., Yang, F., Schimmel, P., and Musier-Forsyth, K. (1997). Specific atomic groups and RNA helix geometry in acceptor stem recognition by a tRNA synthetase. Proc. Natl. Acad. Sci. U S A. 94: 10150-10154.
278. Shiba, K., Hiromi, H., and Schimmel, P. (1997). Maintaining genetic code through adaptations of tRNA synthetases to taxonomic domains. Trends Biochem. Sci. 22: 453-457.
277. Shiba, K., Stello, T., Motegi, H., Noda, T., Musier-Forsyth, K., and Schimmel, P. (1997). Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. J. Biol. Chem. 272: 22809-22816.
276. Sen, S., Zhou, H., Ripmaster, T., Hittleman, W. N., Schimmel, P. and White, R. A. (1997). Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent. Proc. Natl. Acad. Sci. U S A. 94: 6164-6169.
275. Hale, S. P., Auld, D. S., Schmidt, E., and Schimmel, P. (1997). Discrete determinants in transfer RNA for editing and aminoacylation. Science 276: 1250-1252.
274. Glasfeld, E. and Schimmel, P. (1997). Zinc-dependent tRNA binding by a peptide element within a tRNA synthetase. Biochemistry 36: 6739-6744.
273. Nair, S., Ribas de Pouplana, L., Houman, F., Avruch, A., Shen, X., and Schimmel, P. (1997). Species-specific tRNA recognition in relation to tRNA synthetase contact residues. J. Mol. Biol. 269: 1-9.
272. Hale, S. P. and Schimmel, P. (1997). DNA aptamer targets translational editing motif in a tRNA synthetase. Tetrahedron 53: 11985-11994.
271. Whelihan, E. F. and Schimmel, P. (1997). Rescuing an essential protein-RNA complex with a nonessential appended domain. EMBO J. 16: 2968-2974.
270. Henderson, B. S. and Schimmel, P. (1997). RNA-RNA interactions between oligonucleotide substrates for aminoacylation. Bioorgan. Med. Chem. 5: 1071-1079.
269. Schimmel, P. and Musier-Forsyth, K. (1996). ‘Distorted’ RNA helix recognition. Nature 384: 422.
268. Michaels, J.-E. A., Schimmel, P., Shiba, K., and Miller, W. T. (1996). Dominant negative inhibition by fragments of a monomeric enzyme. Proc. Natl. Acad. Sci. U S A. 93: 14452-14455.
267. Lin, L., Hale, S. P. and Schimmel, P. (1996). Aminoacylation error correction. Nature 384: 33-34.
266. Schimmel, P. (1996). A two-way street between the university and the biotechnology enterprise. J. NIH Res. 8: 41-43.
265. Schimmel, P. (1996). Origin of Genetic Code: Searching for the Needle in the Haystack of tRNA Sequences. Proc. Natl. Acad. Sci. U S A. 93: 4521-4522.
264. Sassanfar, M., Kranz, J. E., Gallant, P., Schimmel, P., and Shiba, K. (1996). A Eubacterial Mycobacterium tuberculosis tRNA Synthetase is Eukaryote-like and Resistant to a Eubacterial-Specific Anti-Synthetase Drug. Biochemistry 35: 9995-10003.
263. Ribas de Pouplana, L., Auld, D. S., Kim, S., and Schimmel, P. (1996). A Mechanism for Reducing Entropic Cost of Induced Fit in Protein-RNA Recognition. Biochemistry 35: 8095-8102.
262. Gale, A. J. and Schimmel, P. (1996). Affinity Co-Electrophoresis for Dissecting Protein-RNA Domain-Domain Interactions in a tRNA Synthetase System. Pharm. Acta Helv. 71: 45-50.
261. Lin, L. and Schimmel, P. (1996). Mutational Analysis Suggests Common Design for Editing Activities of Two tRNA Synthetases. Biochemistry 35: 5596-5601.
260. Hale, S. and Schimmel, P. (1996). Protein synthesis editing by a DNA aptamer. Proc. Natl. Acad. Sci. U S A. 93: 2755-2758.
259. Glasfeld, E., Landro, J. A. and Schimmel, P. (1996). C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetase. Biochemistry 35: 4139-4145.
258. Auld, D. S. and Schimmel, P. (1996). Single sequence of helix-loop peptide confers functional anticodon recognition on two tRNA synthetases. EMBO J. 15: 1142-1148.
257. Schimmel, P. (1996). Protein Pharmaceuticals Under Scrutiny. (Review of Physical Methods to Characterize Pharmaceutical Proteins, edited by J. N. Herron, W. Jiskoot, and D. J. A. Crommelin). Protein Sci. 5: 398-399.
256. Gale, A. J., Shi, J.-P., and Schimmel, P. (1996). Evidence that Specificity of Microhelix Charging by a Class I tRNA Synthetase Occurs in Transition State of Catalysis. Biochemistry 35: 608-615.
255. Ribas de Pouplana, L., Frugier, M., Quinn, C. L., and Schimmel, P. (1996). Evidence that Two Present Day Components of the Genetic Code Appeared After Nucleated Cells Separated from Eubacteria. Proc. Natl. Acad. Sci. U S A. 93: 166-170.
254. Schimmel, P. (1996). The Tree of Life as a Miraculous Necessity (Review of Vital Dust: Life as a Cosmic Imperative by Christian de Duve). Am. Sci. 84: 72-74.
253. Martinis, S. A. and Schimmel, P. (1996). Aminoacyl tRNA Synthetases: General Features and Relationships. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd edition, Vol. 1 (F. C. Neidhardt, ed.), ASM Press, Washington, pp. 887-901.
252. Guo, M. and Schimmel, P., (eds). (1995). Tracing Biological Evolution in Protein and Gene Structures, Elsevier Science B. V, Amsterdam, pp. 314.
251. Schimmel, Paul (1995). Implications of an Operational RNA Code for Amino Acids. in Tracing Biological Evolution in Protein and Gene Structures. (M. Guo and P. Schimmel, eds.). Elsevier Science B. V., Amsterdam, pp. 1-10.
250. Schimmel, P. and Ripmaster, T. L. (1995). Modular Design of Components of Operational RNA Code for Alanine in Evolution. Trends Biochem. Sci. 20: 333-334.
249. Quinn, C. L., Tao, N., and Schimmel, P. (1995). Species-Specific Microhelix Aminoacylation by a Eukaryote Pathogen tRNA Synthetase Dependent on a Single Base Pair. Biochemistry 34: 12489-12495.
248. Schimmel, P. and Ribas de Pouplana, L. (1995). Transfer RNA: From Minihelix to Genetic Code. Cell 81: 983-986.
247. Schmidt, E. and Schimmel, P. (1995). Residues in a Class I tRNA Synthetase Which Determine Selectivity of Amino Acid Recognition in the Context of tRNA. Biochemistry 34: 11204-11210.
246. Gale, A. J. and Schimmel, P. (1995). Isolated RNA binding domain of a class I tRNA synthetase. Biochemistry 34: 8896-8903.
245. Musier-Forsyth, K., Shi. J.-P., Henderson, B., Bald, R., Fürste, J. P., Erdmann, V. A., and Schimmel, P. (1995). Base analog-induced aminoacylation of an RNA helix by a tRNA synthetase. J. Am. Chem. Soc. 117: 7253-7254.
244. Hipps, D. and Schimmel, P. (1995). Cell growth inhibition by sequence-specific RNA minihelices. EMBO J 14: 4050-4055.
243. Kirkpatrick, C. R. and Schimmel, P. (1995). Detection of Leucine-Independent DNA-Site Occupancy of the Yeast Leu3p Transcriptional Activator In Vivo. Mol. Cell. Biol. 15: 4021-4030.
242. Buechter, D. D. and Schimmel, P. (1995). Minor Groove Recognition of Critical Acceptor Helix Base Pair by an Appended Module of a Class II tRNA Synthetase. Biochemistry 34: 6014-6019.
241. Hipps, D., Shiba, K., and Schimmel, P. (1995). Operational RNA Code for Amino Acids: Species-Specific Aminoacylation Switched by A Single Nucleotide. Proc. Natl. Acad. Sci. U S A. 92: 5550-5552.
240. Ripmaster, T., Shiba, K., and Schimmel, P. (1995). Wide Cross-Species tRNA Synthetase Replacement in Vivo: Yeast Cytoplasmic Alanine Enzyme Replaced by Human Polymyositis Serum Antigen. Proc. Natl. Acad. Sci. U S A. 92: 4932-4936.
239. Shiba, K., Ripmaster, T., Suzuki, N., Nichols, R., Plotz, P., Noda, T., and Schimmel, P. (1995). Human Alanyl-tRNA Synthetase: Conservation in Evolution of Catalytic Core and Microhelix Recognition. Biochemistry 34: 10340-10349.
238. Auld, D. S. and Schimmel, P. (1995). Switching Recognition of Two tRNA Synthetases with an Amino Acid Swap in a Designed Peptide. Science 267: 1994-1996.
237. Schimmel, P. (1995). An Operational RNA Code for Amino Acids and Variations in Critical Nucleotide Sequences in Evolution. J. Mol. Evol. 40: 531-536.
236. Schimmel, P. and Schmidt, E. (1995). Making Connections: RNA-Dependent Amino Acid Recognition. Trends Biochem. Sci. 20: 1-2.
235. Martinis, S. A. and Schimmel, P. (1995). Small RNA Oligonucleotide Substrates for Specific Aminoacylations. tRNA Structure, Biosynthesis and Function (D. Söll and U. L. RajBhandary, eds.). ASM Press. Washington, D. C., pp. 349-370.
234. Schimmel, P. (1994). The Research University in the 21st Century. Chimica Oggi (Chemistry Today) 12: 9-10.
233. Schimmel, P. and Henderson, B. (1994). Possible Role of Aminoacyl-RNA Complexes in Noncoded Peptide Synthesis and Origin of Coded Synthesis. Proc. Natl. Acad. Sci. U S A. 91: 11283-11286.
232. Shiba, K., Schimmel, P., Motegi, H. and Noda, T. (1994). Human Glycyl-tRNA Synthetase: Wide Divergence of Primary Structure from Bacterial Counterpart and Species-Specific Aminoacylation. J. Biol. Chem. 269: 30049-30055.
231. Landro, J. A., Schmidt, E., Schimmel, P., Tierney, D. L., and Penner-Hahn, J. E. (1994). Thiol Ligation of Two Zinc Atoms to a Class I tRNA Synthetase: Evidence for Unshared Thiols and Role in Amino Acid Binding and Utilization. Biochemistry 33: 14213-14220.
230. Schimmel, P. (1994). Areas of Specialization of Graduate Research Training Grants May Miss the Big Picture. Protein Sci. 3: 995-996.
229. Kim, S., Ribas de Pouplana, L., and Schimmel, P. (1994). An RNA Binding Site in a tRNA Synthetase with a Reduced Set of Amino Acids. Biochemistry 33: 11040-11045.
228. Landro, J. A. and Schimmel, P. (1994). Zinc-Dependent Cell Growth Conferred by Mutant tRNA Synthetase. J. Biol. Chem. 269: 20217-21220.
227. Davis, M. W., Buechter, D. D., and Schimmel, P. (1994). Functional Dissection of a Predicted Class-Defining Motif in a Class II tRNA Synthetase of Unknown Structure. Biochemistry 33: 9904-9911.
226. Shiba, K., Suzuki, N., Shigesada, K., Namba, Y., Schimmel, P., and Noda, T. (1994). Human Cytoplasmic Isoleucyl-tRNA Synthetase: Selective Divergence of the Anticodon-Binding Domain and Acquisition of a New Structural Unit. Proc. Natl. Acad. Sci. U S A. 91: 7435-7439.
225. Schmidt, E. and Schimmel, P. (1994). Mutational Isolation of a Sieve for Editing in a Transfer RNA Synthetase. Science 264: 265-267.
224. Shi, J.-P., Musier-Forsyth, K. and Schimmel, P. (1994). Region of a Conserved Sequence Motif in a Class II tRNA Synthetase Needed for Transfer of an Activated Amino Acid to an RNA Substrate. Biochemistry 33: 5312-5318.
223. Musier-Forsyth, K. and Schimmel, P. (1994). Acceptor Helix Interactions in a Class II tRNA Synthetase: Photoaffinity Cross-Linking of an RNA Miniduplex Substrate. Biochemistry 33: 773-779.
222. Wright, D. J., Martinis, S. A., Jahn, M., Söll, D., and Schimmel, P. (1993). Acceptor Stem and Anticodon RNA Hairpin Helix Interactions with Glutamine tRNA Synthetase. Biochimie 75: 1041-1049.
221. Frugier, M., Florentz, C., Giegé, R. and Schimmel, P. (1993). Triple Aminoacylation Specificity of a Chimerized Transfer RNA. Biochemistry 32: 14053-14061.
220. Schimmel, P. (1993). Functional Analysis Suggests Unexpected Role for Conserved Active Site Residue in Enzyme of Known Structure. Proc. Natl. Acad. Sci. U S A. 90: 9235-9236.
219. Kim S., Ribas de Pouplana, L. and Schimmel, P. (1993). Diversified Sequences of Peptide Epitope for Same RNA Recognition. Proc. Natl. Acad. Sci. U S A. 90: 10046-10050.
218. Schimmel, P., Giegé, R., Moras, D., and Yokoyama, S.(1993). An Operational RNA Code for Amino Acids and Potential Relationship to the Genetic Code. Proc. Natl. Acad. Sci. U S A. 90: 8763-8768.
217. Ribas de Pouplana, L., Buechter, D. D., Davis, M. W., and Schimmel, P. (1993). Idiographic Representation of Conserved Domain of a Class II tRNA Synthetase of Unknown Structure. Protein Sci. 2: 2259-2262.
216. Kim, S., Landro, J. A., Gale, A. J., and Schimmel, P. (1993). C-Terminal Peptide Appendix in a Class I tRNA Synthetase Needed for Acceptor Helix Contacts and Microhelix Aminoacylation. Biochemistry 32: 13026-13031.
215. Schimmel, P., Landro, J. A., and Schmidt, E. (1993). Evidence for Distinct Locations for Metal Binding Sites in Two Closely Related Class I tRNA Synthetases. J. Biomol. Struct. Dynam. 11: 571-581.
214. Schmidt, E. and Schimmel, P. (1993). Dominant Lethality by Expression of a Catalytically Inactive Class I tRNA Synthetase. Proc. Natl. Acad. Sci. U S A. 90: 6919-6923.
213. Landro, J. A. and Schimmel, P. (1993). Non-Covalent Protein Assembly. Curr. Opin. Struct. Biol. 3: 549-554.
212. Schimmel, P. (1993). Perception of an Academic Welfare State. Protein Sci. 2: 1549-1550.
211. Buechter, D. D. and Schimmel, P. (1993). Aminoacylation of RNA Minihelices: Implications for tRNA Synthetase Structural Design and Evolution. CRC Critical Reviews in Biochemistry 28: 309-322.
210. Buechter, D. D. and Schimmel, P. (1993). Dissection of a Class II tRNA Synthetase: Determinants for Minihelix Recognition are Tightly Associated with Domain for Amino Acid Activation. Biochemistry 32: 5267-5272.
209. Schimmel, P. (1993). Cost of Failure to Project Impact of Protein Science on Human Health and Economy. Protein Sci. 2: 139-140.
208. Schimmel, P. (1993). GTP Hydrolysis in Protein Synthesis: Two for Tu? Science 259: 1264-1265.
207. Landro, J. A. and Schimmel, P. (1993). Metal-Binding Site in a Class I tRNA Synthetase Localized to a Cysteine Cluster Inserted into Nucleotide Binding Fold. Proc. Natl. Acad. Sci. U S A. 90: 2261-2265.
206. Martinis, S. A. and Schimmel, P. (1993). Microhelix Aminoacylation by a Class I tRNA Synthetase: Non-Conserved Base Pairs Required for Specificity. J. Biol. Chem. 268: 6069-6072.
205. Schimmel, P. (1993). Charging of RNA Microhelices and Decoding Genetic Information: Evaluation of Functional Coupling Between Distal Parts of a tRNA Structure. In The Translation Apparatus: Structure, Function, Regulation, Evolution (K. H. Nierhaus, F. Franceschi, A. R. Subramanian, V. A. Erdmann, and B. Wittmann-Liebold, eds.), Plenum Press, New York, pp. 13-21.
204. Musier-Forsyth, K. and Schimmel, P. (1993). Aminoacylation of RNA Oligonucleotides: Minimalist Structures and Origin of Specificity. FASEB J 7: 282-289.
203. Ludmerer, S. W., Wright, D. J., and Schimmel, P. (1993). Purification of Glutamine tRNA Synthetase from Saccharomyces cerevisiae: A Monomeric Aminoacyl-tRNA Synthetase with a Large and Dispensable NH2-Terminal Domain. J. Biol. Chem. 268: 5519-5523.
202. Schimmel, P., Shepard, A., and Shiba, K. (1992). Intron Locations and Functional Deletions in Relation to the Design and Evolution of a Subgroup of Class I tRNA Synthetases. Protein Sci. 1: 1387-1391.
201. Shepard, A., Shiba, K., and Schimmel, P. (1992). RNA Binding Determinant in Some Class I tRNA Synthetases Identified by Alignment-Guided Mutagenesis. Proc. Natl. Acad. Sci. U S A. 89: 9964-9968.
200. Shiba, K. and Schimmel, P. (1992). Tripartite Functional Assembly of a Large Class I tRNA Synthetase. J. Biol. Chem. 267: 22703-22706.
199. Hou, Y.-M. and Schimmel, P. (1992). Functional Compensation of a Recognition-Defective Transfer RNA by a Distal Base Pair Substitution. Biochemistry 31: 10310-10314.
198. Kim, S. and Schimmel, P. (1992). Functional Independence of Microhelix Aminoacylation from Anticodon Binding in a Class I tRNA Synthetase. J. Biol. Chem. 267: 15563-15567.
197. Musier-Forsyth, K. and Schimmel, P. (1992). Functional Contacts of a transfer RNA Synthetase with 2'-Hydroxyl Groups in the RNA Minor Groove. Nature 357: 513-515.
196. Schimmel, P. (1992). Molecular Biology and the Transformation of Protein Science. Protein Sci. 1: 307-308.
195. Shi, J.-P., Martinis, S. A., and Schimmel, P. (1992). RNA Tetraloops as Minimalist Substrates for Aminoacylation Biochemistry 31: 4931-4936.
194. Miller, W. T. and Schimmel, P. (1992). A Metal Binding Motif Implicated in RNA Recognition by an Aminoacyl-tRNA Synthetase and by a Retroviral Gene Product. Mol. Microbiol. 6: 1259-1262.
193. Hou, Y.-M. and Schimmel, P. (1992). Novel Transfer RNAs that are Active in Escherichia coli. Biochemistry 31: 4157-4160.
192. Francklyn, C., Musier-Forsyth, K., and Schimmel, P. (1992). Small RNA Helices as Substrates for Aminoacylation and their Relationship to the Charging of Transfer RNAs. Eur. J. Biochem. 206: 315-321.
191. Miller, W. T. and Schimmel, P. (1992). A Retroviral-like Metal Binding Motif in an Aminoacyl tRNA Synthetase is Important for tRNA Recognition. Proc. Natl. Acad. Sci. U S A. 89: 2032-2035.
190. Shiba, K. and Schimmel, P. (1992). Functional Assembly of a Randomly Cleaved Protein. Proc. Natl. Acad. Sci. U S A. 89: 1880-1884.
189. Burbaum, J. J. and Schimmel, P. (1992). Amino Acid Binding by the Class I Aminoacyl-tRNA Synthetases: Role for a Conserved Proline in the Signature Sequence. Protein Sci. 1: 575-581.
188. Francklyn, C., Shi, J.-P., and Schimmel, P. (1992). Overlapping Nucleotide Determinants for Specific Aminoacylation of RNA Microhelices. Science 255: 1121-1125.
187. Martinis, S. A. and Schimmel, P. (1992). Enzymatic Aminoacylation of Sequence-Specific RNA Minihelices and Hybrid Duplexes with Methionine. Proc. Natl. Acad. Sci. U S A. 89: 65-69.
186. Burbaum, J. J. and Schimmel, P. (1991). Structural Relationships and the Classification of Aminoacyl-tRNA Synthetases. J. Biol. Chem. 266: 16965-16968.
185. Schimmel, P. (1991). Mutant Enzymes and Dissected Transfer RNAs that Elucidate Motifs for Protein-RNA Recognition. Curr. Op. Struct. Biol. 1: 811-816.
184. Wendler, H. E. and Schimmel, P. (1992). Genetic Code. In McGraw-Hill Encyclopedia of Science & Technology Volume 7. (S. P. Parker, ed.), McGraw-Hill, New York. pp. 675-678.
183. Yi, T.-M., Walsh, K., and Schimmel, P. (1991). Rabbit Muscle Creatine Kinase: Genomic Cloning, Sequencing, and Analysis of Upstream Sequences Important for Expression in Myocytes. Nucleic Acids Res. 19: 3027-3033.
182. Musier-Forsyth, K., Usman, N., Scaringe, S., Doudna, J., Green, R., and Schimmel, P. (1991). Specificity for Aminoacylation of an RNA Helix: An Unpaired, Exocylic Amino Group in the Minor Groove. Science 253: 784-786.
181. Miller, W. T., Hill, K. A., and Schimmel, P. (1991). Evidence for a "Cysteine-Histidine Box" Metal Binding Site in an Escherichia coli Aminoacyl-tRNA Synthetase. Biochemistry 30: 6970-6976.
180. Schimmel, P. and Burbaum, J.(1991). Transfer RNA with Double Identity for in Vitro Kinetic Modeling of tRNA Identity in Vivo. Meth. Enzymol. 203: 485-500.
179. Schimmel, P. (1991). Molecular Recognition of Transfer RNAs. Encyclopedia of Human Biology 5: 75-80.
178. Trézéguet, V., Edwards, H., and Schimmel, P. (1991). A Single Base Pair Dominates Over the Novel Identity of an Escherichia coli Tyrosine tRNA in Saccharomyces cerevisiae. Mol. Cell Biol. 11: 2744-2751 .
177. Schimmel, P. (1991). RNA Minihelices and the Decoding of Genetic Information. FASEB J. 5: 2180-2187.
176. Hou, Y.-M., Shiba, K., Mottes, C., and Schimmel, P. (1991). Sequence Determination and Modeling of Structural Motifs for the Smallest Aminoacyl tRNA Synthetase. Proc. Natl. Acad. Sci. U S A. 88: 976-980.
175. Shi, J.-P. and Schimmel, P. (1991). Aminoacylation of Alanine Minihelices: "Discriminator" Base Modulates Transition State of Single Turnover Reaction. J. Biol. Chem. 266: 2705-2708.
174. Schimmel, P. (1991). Classes of Aminoacyl tRNA Synthetases and the Establishment of the Genetic Code. Trends in Biochem. Sci. 16: 1-3.
173. Miller, W. T., Hou, Y.-M., and Schimmel, P. (1991). Mutant Aminoacyl tRNA Synthetase that Compensates for a Mutation in the Major Identity Determinant of Its tRNA. Biochemistry 30: 2635-2631.
172. Burbaum, J. J. and Schimmel, P. (1991). Assembly of A Class I tRNA Synthetase from Products of an Artificially Split Gene. Biochemistry 30: 319-324.
171. Edwards, H., Trézéguet, V., and Schimmel, P. (1991). An Escherichia coli Tyrosine Transfer RNA is a Leucine-Specific Transfer RNA in the Yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U S A. 88: 1153-1156.
170. Musier-Forsyth, K., Scaringe, S., Usman, N., and Schimmel, P. (1991). Enzymatic Aminoacylation of Single-Stranded RNA with an RNA Cofactor. Proc. Natl. Acad. Sci. U S A. 88: 209-213.
169. Francklyn, C. and Schimmel, P. (1990). Enzymatic Aminoacylation of an Eight Base Pair Microhelix with Histidine. Proc. Natl. Acad. Sci. U S A. 87: 8655-8659.
168. Francklyn, C. and Schimmel, P. (1990). Synthetic RNA Molecules as Substrates for Enzymes that Act on tRNA and tRNA-like Molecules. Chemical Reviews 90: 1327-1342.
167. Park, S.-J., Miller, W. T., and Schimmel, P. (1990). Synthetic Peptide Model of an Essential Region of an Aminoacyl tRNA Synthetase. Biochemistry 29: 9212-9218.
166. Schimmel, P. (1990). Hazards and Their Exploitation in the Applications of Molecular Biology to Structure-Function Relationships. Biochemistry 29: 9495-9502.
165. Schimmel, P. (1989). Molecular Recognition of Transfer RNA Studied with Dissected Enzyme and RNA Molecules. Protein Engineering: Protein Design in Basic Research, Medicine, and Industry, (M. Ikehara, ed.), Japan Scientific Societies Press; Springer-Verlag, Kobe, Japan, pp. 165-170.
164. Ch'ng, J. L. C., Shoemaker, D. L., Schimmel, P., and Holmes, E. W. (1990). Reversal of Creatine Kinase Translational Repression by 3' Untranslated Sequences. Science 248: 1003-1006.
163. Shi, J.-P., Francklyn, C., Hill, K. and Schimmel (1990). A Nucleotide that Enhances the Charging of RNA Minihelix Sequence Variants with Alanine. Biochemistry 29: 3621-3626.
162. Edwards, H. and Schimmel, P. (1990). A Bacterial Amber Suppressor in Saccharomyces cerevisiae Is Selectively Recognized by a Bacterial Aminoacyl-tRNA Synthetase. Mol. Cell. Biol. 10: 1633-1641.
161. Kaddurah-Daouk, R., Lillie, J. W., Daouk, G. H., Green, M. R., Kingston, R., and Schimmel, P. (1990). Induction of a Cellular Enzyme for Energy Metabolism by Transforming Domains of Adenovirus E1a. Mol. Cell. Biol. 10: 1476-1483.
160. Schimmel, P. (1990). A Base Pair that Specifies tRNA Identity in Different Sequence Contexts and in Evolution. Frontiers of Chemistry: Proceedings of the Frontiers of Chemistry Conference (R. E. Stobaugh, ed.), Chemical Abstracts Service, Columbus, Ohio, 1 Biotechnology, pp. 127-139.
159. Hill, K. and Schimmel, P. (1990). The Dissection and Engineering of Sites that Affect the Activity of an Enzyme of Unknown Structure. Biotechnology 14: 65-79.
158. Schimmel, P. (1990). Interpretation of Experiments that Delineate Transfer RNA Recognition in Vivo and in Vitro. In Nucleic Acids & Molecular Biology Volume 4 (F. A. Eckstein and D. M. J. Lilley, eds.), Springer-Verlag, Berlin, pp. 274-287.
157. Schimmel, P. (1990). Genetic Code. in McGraw-Hill Yearbook of Science & Technology: 1990 (S. P. Parker, ed.), McGraw-Hill Publishing Co., New York, pp. 163-165.
156. Toth, M. J. and Schimmel, P. (1990). A Mutation in the Small (Alpha) Subunit of Glycyl-tRNA Synthetase Affects Amino Acid Activation and Subunit Association Parameters. J. Biol. Chem. 265: 1005-1009.
155. Toth, M. J. and Schimmel, P. (1990). Deletions in the Large (Beta) Subunit of a Hetero-Oligomeric Aminoacyl-tRNA Synthetase. J. Biol. Chem. 265: 1000-1004.
154. Schimmel, P. (1990). Alanine Transfer RNA Synthetase: Structure-Function Relationships and Molecular Recognition of Transfer RNA. Adv. Enzymol Relat. Areas Mol. Biol. 63: 233-270.
153. Burbaum, J. J., Starzyk, R. M., and Schimmel, P. (1990). Understanding Structural Relationships in Proteins of Unsolved Three-Dimensional Structure. PROTEINS: Structure, Function, and Genetics 7: 99-111.
152. Ch'ng, J. L. C., Mulligan, R. C., Schimmel, P., and Holmes, E. W. (1989). Anti-Sense RNA Complementary to 3' Coding and Non-Coding Sequences of Creatine Kinase Is A Potent Inhibitor of Translation in Vivo. Proc. Natl. Acad. Sci. U S A. 86: 10006-10010.
151. Starzyk, R. and Schimmel, P. (1989). Construction of Intra-Domain Chimeras of Aminoacyl-tRNA Synthetases. J. Biomol. Struct. Dyn. 7: 225-234.
150. Walsh, K. and Schimmel, P. (1989). Preliminary Characterizations of Muscle Actin Promoter Factors 1 and 2 and Their Interactions with the Skeletal Actin Promoter. In Cellular and Molecular Biology of Muscle Development (L. H. Kedes and F. E. Stockdale, eds.), A. R. Liss, New York pp. 669-676.
149. Schimmel, P. (1989). RNA Pseudoknots that Interact with Components of the Translation Apparatus. Cell 58: 9-12.
148. Starzyk, R. M., Burbaum, J. J., and Schimmel, P. (1989). Insertion of New Sequences into the Catalytic Domain of an Enzyme. Biochemistry 28: 8479-8484.
147. Hou, Y-M. and Schimmel, P. (1989). Evidence that a Major Determinant for the Identity of a Transfer RNA Is Conserved in Evolution. Biochemistry 28: 6800-6804.
146. Friden, P., Reynolds, C., and Schimmel, P. (1989). A Large Internal Deletion Converts Yeast LEU3 to A Constitutive Transcriptional Activator. Mol. Cell Biol. 9: 4056-4060.
145. Hou, Y-M., Francklyn, C., and Schimmel(1989). Molecular Dissection of A Transfer RNA and the Basis for Its Identity. Trends Biochem. Sci. 14: 233-237.
144. Hou, Y-M. and Schimmel, P. (1989). Modeling with in Vitro Kinetic Parameters for the Elaboration of Transfer RNA Identity in Vivo. Biochemistry 28: 4942-4947.
143. Schimmel, P. (1989). Hazards of Deducing Enzyme Structure-Activity Relationships Based on Chemical Applications of Molecular Biology. Acc. Chem. Res. 22: 232-233.
142. Schimmel, P. (1989). Parameters for the Molecular Recognition of Transfer RNAs. Biochemistry 28: 2747-2759.
141. Francklyn, C. and Schimmel, P. (1989). Aminoacylation of RNA Minihelices with Alanine. Nature 337: 478-481.
140. Park, S. J., Hou, Y.-M., and Schimmel, P. (1989). A Single Base Pair Affects Binding and Catalytic Parameters in the Molecular Recognition of a Transfer RNA. Biochemistry 28: 2740-2746.
139. Hill, K. and Schimmel, P. (1989). Evidence that the 3'-end of a Transfer RNA Binds to a Site in the Adenylate Synthesis Domain of an Aminoacyl Transfer RNA Synthetase. Biochemistry 28: 2577-2586.
138. Schimmel, P. (1988). "Who Will Watch the Watchdogs?" Cell 54: 596.
137. Park, S. J. and Schimmel, P. (1988). Evidence for Interaction of an Aminoacyl Transfer RNA Synthetase with a Region Important for the Identity of its Cognate Transfer RNA. J. Biol. Chem. 263: 16527-16530.
136. Schimmel, P. (1988). Third Thoughts on Second Code. Science News 133: 387.
135. Regan, L., Buxbaum, L., Hill, K., and Schimmel, P. (1988). Rationale For Engineering an Enzyme by Introducing a Mutation That Compensates for a Deletion. J. Biol. Chem. 263: 18598-18600.
134. Frederick, C., Wang, A., Rich, A., Regan, L., and Schimmel, P. (1988). Crystallization of a Small Fragment of an Aminoacyl tRNA Synthetase. J. Mol. Biol. 203: 521-522.
133. Friden, P. and Schimmel, P. (1988). LEU3 of Saccharomyces cerevisiae Activates Multiple Genes for Branched Chain Amino Acid Biosynthesis by Binding to a Common Decanucleotide Core Sequence. Mol. Cell Biol. 8: 2690-2697.
132. Hou, Y.-M. and Schimmel, P. (1988) A Simple Structural Feature is a Major Determinant of the Identity of a Transfer RNA. Nature 333: 140-145.
131. Clarke, Neil D., Lien, Donald C., and Schimmel, P. (1988). Evidence From Cassette Mutagenesis for a Structure-Function Motif in a Protein of Unknown Structure. Science 240: 521-523.
130. Walsh, K. and Schimmel, P. (1988). DNA Binding Site for Two Skeletal Actin Promoter Factors Is Important For Expression in Muscle Cells. Mol. Cell. Biol. 8: 1800-1802.
129. Drain, P. and Schimmel, P. (1988). Multiple New Genes That Determine Activity for the First Step of Leucine Biosynthesis in Saccharomyces cerevisiae. Genetics 119: 13-20.
128. Toth, M. J., Murgola, E. J., and Schimmel, P. (1988). Evidence for a Unique First Position Codon-Anticodon Mismatch in Vivo. J. Mol. Biol. 201: 451-454.
127. Profy. A. T. and Schimmel, P. (1988). Complementary Use of Chemical Modification and Site-Directed Mutagenesis to Probe Structure-Activity Relationships in Enzymes. Prog. Nucl. Acid. Res. Mol. Biol. 35: 1-26.
126. Daouk, G. H., Kaddurah-Daouk, R., Putney, S., Kingston, R., and Schimmel, P. (1988). Isolation of a Functional Human Gene for Brain Creatine Kinase. J. Biol. Chem. 263: 2442-2446.
125. Schimmel, P. (1988). The Evolution and Future of Biotechnology. In The Impact of Chemistry on Biotechnology. ACS Symposium Series 362. (M. Phillips, S. P. Shoemaker, R. D. Middlekauff, and R. M. Ottenbrite, eds.), American Chemical Society, Washington, D. C. pp. 30-35.
124. Regan, L. and Schimmel, P. (1987). Selection of Aminoacyl tRNA Synthetases with Enhanced Catalytic Activity. in Protein Structure, Folding and Design 2: Proceedings of a Dupont-UCLA Symposium held in Steamboat Springs, Colorado, April 4-11, 1987. (D. L. Oxender, ed.), A. R. Liss, New York, 69: 293-300.
123. Schimmel, P. (1987). Active Sites Up Close. Cell 51: 517-518.
122. Edwards, H. and Schimmel, P. (1987). An E. coli Aminoacyl tRNA Synthetase Can Substitute for Yeast Mitochondrial Enzyme Function in vivo. Cell 51: 643-649.
121. Starzyk, R. M. Webster, T. A., and Schimmel, P. (1987). Evidence for Dispensable Sequences Inserted into a Nucleotide Fold. Science 237: 1614-1618.
120. Friden, P., and Schimmel, P. (1987). LEU3 of Saccharomyces cerevisiae Encodes a Factor for Control of RNA Levels of a Group of Leucine-Specific Genes. Mol. Cell. Biol. 7: 2708-2717.
119. Ludmerer, S. W. and Schimmel, P. (1987). Construction and Analysis of Deletions in the Amino Terminal Extension of Glutamine tRNA Synthetase of Saccharomyces cerevisiae. J. Biol. Chem., 262: 10807-10813.
118. Ludmerer, S. W. and Schimmel, P. (1987). Gene for Yeast Glutamine tRNA Synthetase Encodes a Large Amino Terminal Extension and Provides a Strong Confirmation of the Signature Sequence for Aminoacyl tRNA Synthetases. J. Biol. Chem. 262: 10801-10806.
117. Walsh, K. and Schimmel, P. (1987). Two Nuclear Factors Compete for the Skeletal Muscle Actin Promoter. J. Biol. Chem. 262: 9429-9432.
116. Schimmel, P. (1987). Aminoacyl tRNA Synthetases: General Scheme of Structure-Function Relationships in the Polypeptides and Recognition of Transfer RNAs. Annu. Rev. Biochem. 56: 125-158.
115. Regan, L., Bowie, J., and Schimmel, P. (1987). Polypeptide Sequences Essential for RNA Recognition by an Enzyme. Science 235: 1651-1653.
114. Profy, A. T. and Schimmel, P. (1986). A Sulfhydryl Presumed Essential is not Required for Catalysis by an Aminoacyl-tRNA Synthetase. J. Biol. Chem. 261: 15474-15479
113. Drain, P. and Schimmel, P. (1986). Yeast LEU5 is a Pet-Like Gene That is not Essential for Leucine Biosynthesis. Mol. Gen. Genet. 204: 397-403.
112. Toth, M. and Schimmel, P. (1986). Internal Structural Features of E. coli Glycyl-tRNA Synthetase Examined by Subunit Polypeptide Chain Fusions. J. Biol. Chem. 261: 6643-6646.
111. Regan, L., Dignam, J. D., and Schimmel, P. (1986). A Bacterial and Silkworm Aminoacyl tRNA Synthetase Have a Common Epitope Which Maps to the Catalytic Domain of Each. J. Biol. Chem. 261: 5241-5244.
110. Schimmel, P. (1985). RNA Recognition in the Aminoacyl tRNA Synthetase System. In Robert A. Welch Foundation Symposium on Genetic Chemistry XXIX. pp. 219-236.
109. Schimmel, P. (1985). In Biology, Neither Smaller Nor Larger is Necessarily Better. Cell 42: 1.
108. Schimmel, P. (1985). High Priority Scores. Science 229: 706.
107. Schimmel, Paul (1985). Protein Structures and Molecular Principles. Amer. Sci. Rev. November. pp. 583-584.
106. Ludmerer, S. W. and Schimmel, P. (1985). Cloning of GLN4: An Essential Gene that Encodes Glutamine tRNA Synthetase in Saccharomyces cerevisiae. J. Bacteriol. 163: 763-768.
105. Ho, C., Jasin, M., and Schimmel, P. (1985). Amino Acid Replacements That Compensate for a Large Polypeptide Deletion in an Enzyme. Science 229: 389-393.
104. Freedman, R., Gibson, B., Donovan, D., Biemann, K., Eisenbeis, S., Parker, J., and Schimmel, P. (1985). Primary Structure of Histidine tRNA Synthetase and Characterization of hisS Transcripts. J. Biol. Chem. 260: 10063-10068.
103. Pickering, L., Pang, H., Biemann, K., Munro, H., and Schimmel, P. (1985). Two Tissue Specific Isozymes of Creatine Kinase Have Closely Matched Amino Acid Sequences. Proc. Natl. Acad. Sci. U S A. 82: 2310-2314.
102. Middleton, T., Herlihy, W. C., Schimmel, P. R. and Munro, H.N. (1985). Synthesis and Purification of Oligoribonucleotides Using T4 RNA Ligase and Reverse-Phase Chromatography. Anal. Biochem. 144: 110-117.
101. Jasin, M., Regan, L., and Schimmel, P, (1985). Two Mutations in the Dispensable Part of Alanine tRNA Synthetase Which Affect the Catalytic Activity. J. Biol. Chem. 260: 2226-2230.
100. Starzyk, R., Schoemaker, H., and Schimmel P. (1985). Covalent Enzyme-RNA Complex: A Transfer RNA Modification That Prevents A Covalent Enzyme Interaction Also Prevents Aminoacylation, Proc. Natl. Acad. Sci. U S A. 82: 339-342.
99. Putney, S., Herlihy, W., Royal, N., Pang, H., Aposhian, H. V., Pickering, L., Belagaje, R., Biemann, K., Page, D., Kuby, S., and Schimmel, P. (1984). Rabbit Muscle Creatine Phosphokinase: cDNA Cloning, Primary Structure, and Detection of Human Homologues. J. Biol. Chem. 259: 14317-14320.
98. Webster, T., Tsai, H., Kula, M., Mackie, G., and Schimmel, P. (1984). Specific Sequence Homology and Three-Dimensional Structure of an Aminoacyl Transfer RNA Synthetase. Science 226: 1315-1317.
97. Jasin, M. and Schimmel, P. (1984). Deletion of an Essential Gene in E. coli by Site-Specific Recombination with Linear DNA Fragments. J. Bacteriol. 159: 783-786.
96. Andreadis, A., Hsu, Y.-P., Hermodson, M., Kohlhaw, G., and Schimmel, P. (1984). Yeast LEU2: Repression of mRNA Levels by Leucine and Primary Structure of the Gene Product. J. Biol. Chem. 259: 8059-8062.
95. Jasin, M., Regan, L., and Schimmel, P. (1984). Dispensable Pieces of an Aminoacyl tRNA Synthetase Which Activate the Catalytic Site. Cell 36: 1089-1095.
94. Hsu, Y.-P. and Schimmel, P. (1984). Yeast LEU1: Repression of mRNA Levels by Leucine and Relationship of 5'-Noncoding Region to that of LEU2. J. Biol. Chem. 259: 3714-3719.
93. Schimmel, P., Jasin, M., and Regan, L. (1984). Size Polymorphism and the Structure of Aminoacyl tRNA Synthetases. Fed. Proc. 43: 2987-2990.
92. Jasin, M. and Schimmel, P. (1984). Two Approaches to Mapping Functional Domains of an Enzyme: Applications to an Aminoacyl tRNA Synthetase. In Gene Expression, Alfred Benzon Symposium 19, Munksgaard, Copenhagen. pp. 223-235.
91. Keng, T. and Schimmel, P. (1983). Synthesis of Two Polypeptide Subunits of an Aminoacyl tRNA Synthetase as a Single Polypeptide Chain. J. Biomol. Struct. Dyn. 1: 225-229.
90. Webster, T. A., Gibson, B. W., Keng, T., Biemann, K., and Schimmel, P. (1983). Primary Structures of Both Subunits of Escherichia coli Glycyl tRNA Synthetase. J. Biol. Chem. 258: 10637-10641.
89. Jasin, M., Regan, L. and Schimmel, P. (1983). Modular Arrangement of Functional Domains Along the Sequence of an Aminoacyl tRNA Synthetase. Nature 306: 441-447.
88. Putney, S. D., Herlihy, W. C., and Schimmel, P. R. (1983). A New Troponin T Isotype and cDNA Clones for 13 Muscle Proteins, Found By Shotgun Sequencing of a Rabbit Muscle cDNA Library. Nature 302: 718-721.
87. Andreadis, A., Hsu, Y.-P., Kohlhaw, G. B., and Schimmel, P. (1982). Nucleotide Sequence of Yeast LEU2 Shows 5'-Noncoding Region Has Sequences Cognate to Leucine. Cell 31: 319-325.
86. Keng, T., Webster, T., Sauer, R., and Schimmel, P. (1982). Gene for Escherichia coli Glycyl-tRNA Synthetase has Tandem Subunit Coding Regions in the Same Reading Frame. J. Biol. Chem. 257: 12503-12508.
85. Schimmel, P., Keng, T., and Putney, S. (1982). Genes for Two E. coli Aminoacyl tRNA Synthetases. Devel. in Biochem. 24: 49-56.
84. Starzyk, R. M., Koontz, S. W., and Schimmel, P. (1982). A Covalent Adduct Between the Uracil Ring and the Active Site of an Aminoacyl tRNA Synthetase. Nature 298: 136-140.
83. Schimmel, P., Putney, S., and Starzyk, R. (1982). RNA and DNA Sequence Recognition and Structure-Function of Aminoacyl tRNA Synthetases. Trends in Biochem. Sci. 7: 209-212.
82. Putney, S. D., Benkovic, S. J., and Schimmel, P. R. (1981). A DNA Fragment With an alpha-Phosphorothioate Nucleotide at One End is Asymmetrically Blocked from Digestion by Exonuclease III and Can Be Replicated in Vivo. Proc. Nat. Acad. Sci. U S A. 78: 7350-7354.
81. Putney, S. D., Royal, N. J., Neuman de Vegvar, H., Herlihy, W. C., Biemann, K., and Schimmel, P. (1981). Primary Structure of a Large Aminoacyl tRNA Synthetase. Science 213: 1497-1501.
80. Freedman, R. and Schimmel, P. (1981). In Vitro Transcription of the Histidine Operon. Identification of the His Promoter, and Leader and Readthrough Transcripts. J. Biol. Chem. 256: 10747-10750.
79. Putney, S. D. and Schimmel, P. R. (1981). An Aminoacyl tRNA Synthetase Binds to a Specific DNA Sequence and Regulates Its Gene Transcription. Nature 291: 632-635.
78. Putney, S. D., Melendez, D. L., and Schimmel, P. R. (1981). Cloning, Partial Sequencing, and in Vitro Transcription of the Gene for Alanine tRNA Synthetase. J. Biol. Chem. 256: 205-211.
77. Putney, S. D., Sauer, R., and Schimmel, P. R. (1981). Purification and Properties of Alanine tRNA Synthetase from Escherichia coli a Tetramer of Identical Subunits. J. Biol. Chem. 256: 198-204.
76. Schimmel, P. R. (1980). Five Specific Protein-Transfer RNA Interactions. Crit. Rev. in Biochem. 9: 207-251.
75. Cantor, C. R. and Schimmel, P. R. (1980). Biophysical Chemistry, Part III: The Behavior of Biological Macromolecules (San Francisco, W. H. Freeman).
74. Cantor, C. R. and Schimmel, P. R. (1980). Biophysical Chemistry, Part II: Techniques for the Study of Biological Structure and Function (San Francisco, W. H. Freeman).
73. Cantor, C. R. and Schimmel, P. R. (1980). Biophysical Chemistry, Part I: The Conformation of Biological Macromolecules (San Francisco, W. H. Freeman).
72. Herlihy, W. C., Royal, N. J., Biemann, K., Putney, S. D., and Schimmel, P. R. (1980). Mass Spectra of Partial Protein Hydrolysates as a Multiple Phase Check for Long Polypeptides Deduced from DNA Sequences: NH2-Terminal Segment of Alanine tRNA Synthetase. Proc. Nat. Acad. Sci. U S A. 77: 531-6535.
71. Schimmel, P. R., Melendez, D. L., and Putney, S. D. (1980). Molecular Dissection of an Enzyme that Recognizes Transfer RNA. Macromolecules 13: 716-721.
70. Schimmel, P. R. and Redfield, A. G. (1980). Transfer RNA in Solution: Selected Topics. Ann. Rev. Biophys. Bioeng. 9: 181-221.
69. Söll, D., Abelson, J., and Schimmel, P. R., (eds). (1980). Transfer RNA Part 2: Biological Aspects, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
68. Koontz, S. W. and Schimmel, P. R. (1979). Aminoacyl-tRNA Synthetase-Catalyzed Cleavage of the Glycosidic Bond of 5-Halogenated Uridines. J. Biol. Chem. 254: 12277-12280.
67. Schimmel, P. R. (1979). Similarities in the Structural Organization of Complexes of Transfer RNAs with Aminoacyl Transfer RNA Synthetases and the Mechanism of Recognition, in Transfer RNA, Part 1: Structure, Properties, and Recognition (Schimmel, P. R., Söll, D., and Abelson, J. eds.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. pp 297-310.
66. Schimmel, P. R., Söll, D., and Abelson, J., (eds). (1979). Transfer RNA, Part 1: Structure, Properties, and Recognition, Vol. 9A, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
65. Schimmel, P R. (1979). Recent Results on How Aminoacyl Transfer RNA Synthetases Recognize Specific Transfer RNAs. Mol. Cell. Biochem. 25: 3-14.
64. Schimmel, P. R. (1979). How Proteins Bind to Transfer RNA, in Nmr and Biochemistry: A Symposium Honoring Mildred Cohn (S. J. Opella and P. Lu, eds.), M. Dekker, New York. pp 75-89.
63. Schimmel, P. R. and Söll, D. (1979). Aminoacyl tRNA Synthetases. General Features and Recognition of Transfer RNAs. Ann. Rev. Biochem. 48: 601-648.
62. Schimmel, P. R. (1979). Understanding the Recognition of Transfer RNAs by Aminoacyl Transfer RNA Synthetases. Adv. Enzymol. Relat. Areas Mol. Biol. 49: 187-222.
61. Schimmel, P. R. and Schoemaker, H. J. P. (1979). Mapping the Structure of Specific Protein-Transfer RNA Complexes by a Tritium Labeling Method. Methods in Enzymol. 59: 332-350.
60. Cole, F. X. and Schimmel, P. R. (1978). Dynamics of Tautomerization of Formycin. J. Amer. Chem. Soc. 100: 3957-3958.
59. Gamble, R. C. and Schimmel, P. R. (1978). Nanosecond Relaxation Processes of Phospholipid Bilayers in the Transition Zone. Proc. Nat. Acad. Sci. U S A. 75: 3011-3014.
58. Schimmel, P. R. (1977). A Review of Entropy-Drive Process in Biology. (M. A. Lauffer, ed.), New York, Springer-Verlag. Quart. Rev. Biol. 52: 188.
57. Schoemaker, H. J. P. and Schimmel, P. R. (1977). Inhibition of an Aminoacyl Transfer RNA Synthetase by a Specific Trinucleotide Derived from the Sequence of its Cognate Transfer RNA. Biochemistry 16: 5461-5464.
56. Schoemaker, H. J. P. and Schimmel, P. R. (1977). Effect of Aminoacyl Transfer RNA Synthetases on H-5 Exchange of Specific Pyrimidines in Transfer RNAs. Biochemistry 16: 5454-5460.
55. Schimmel, P. R. (1977). Approaches to Understanding the Mechanism of Specific Protein-Transfer RNA Interactions. Acc. Chem. Res. 10: 411-418.
54. Rich, A. and Schimmel, P. R. (1977). Introduction to Transfer RNA. Acc. Chem. Res. 10: 385-387.
53. Schimmel, P. R. (1977). Proteins and Nucleotides. Science 195: 170.
52. Rich, A. and Schimmel, P. R. (1977). Structural Organization of Complexes of Transfer RNAs with Aminoacyl Transfer RNA Synthetases. Nucleic Acids Res. 4: 1649-1665.
51. Jekowsky, E., Miller, D. L., and Schimmel, P. R. (1977). Isolation, Characterization, and Structural Implications of a Nuclease Digested Complex of Aminoacyl Transfer RNA and Escherichia coli Elongation Factor Tu. J. Mol. Biol. 114: 451-458.
50. Yue, V. T. and Schimmel, P. R. (1977). Direct and Specific Photochemical Crosslinking of Adenosine 5' Triphosphate to an Aminoacyl tRNA Synthetase. Biochemistry 16: 4678-4684.
49. Schimmel, P. R. and Yue, V. T. (1977). Structural Relationships in Macromolecular Complexes Determined by Photochemical Crosslinking, In Research in Photobiology, (A. Castellani, ed.), Springer US. pp. 41-51.
48. Schimmel, P. R. and Budzik, G. P. (1977). Photo-Crosslinking of Protein-Nucleic Acid Complexes. Methods Enzymol. 46: 168-180.
47. Schoemaker, H. J. P. and Schimmel, P. R. (1976). Isotope Labeling of Free and Aminoacyl Transfer RNA Synthetase Bound Transfer RNA. J. Biol. Chem. 251: 6823-6830.
46. Schoemaker, H. J. P., Gamble, R. C., Budzik, G. P., and Schimmel, P. R. (1976). Comparison of Isotope Labeling Patterns of Purines in Three Specific Transfer RNAs. Biochemistry 15: 2800-2803.
45. Gamble, R. C. Schoemaker, H. J. P., Jekowsky, E., and Schimmel, P. R. (1976). Rate of Tritium Labeling of Specific Purines in Relation to Nucleic Acid and Particularly Transfer RNA Conformation. Biochemistry 15: 2791-2799.
44. Schimmel, P. R. (1976). Equilibrium and Kinetic Investigations of the Cooperative Interaction of Cations with Transfer RNA. J. Polymer Sci.: Polymer Symposia 54: 387-401.
43. Schimmel, P. R., Budzik, G. P., Lam, S. S. M., and Schoemaker, H. J. P. (1976). In Vitro Studies of Photochemically Cross-Linked Protein-Nucleic Acid Complexes. Determination of Cross-Linked Regions and Structural Relationships in Specific Complexes. in Aging, Carcinogenesis and Radiation Biology: The Role of Nucleic Acid Addition Reactions: [Proceedings] (K. C. Smith, ed.), Plenum Press. pp. 123-148.
42. Schimmel, P. R. (1975). The Interaction of Transfer RNAs with Aminoacyl Transfer RNA Synthetases. In Proceedings of the 10th FEBS Meeting, Paris (Y. Raoul, ed.), pp. 219-232.
41. Lam, S. S. M. and Schimmel, P. R. (1975). Equilibrium Measurements of Cognate and Non-Cognate Interactions Between Aminoacyl Transfer RNA Synthetases and Transfer RNA. Biochemistry 14: 2775-2780.
40. Dickson, L. A. and Schimmel, P. R. (1975). Structure of Transfer RNA-Aminoacyl Transfer RNA Synthetase Complexes Investigated by Nuclease Digestion. Arch. Biochem. Biophys. 67: 638-645.
39. Schoemaker, H. J. P., Budzik, G. P., Giegé, R., and Schimmel, P. (1975). Three Photo-Cross-Linked Complexes of Yeast Phenylalanine Specific Transfer Ribonucleic Acid with Aminoacyl Transfer Ribonucleic Acid Synthetases. J. Biol. Chem. 250: 4440-4444.
38. Budzik, G. P., Lam, S. S. M., Schoemaker, H. J. P. and Schimmel, P. R. (1975). Two Photo-Cross-Linked Complexes of Isoleucine Specific Transfer Ribonucleic Acid with Aminoacyl Transfer Ribonucleic Acid Synthetases. J. Biol. Chem. 250: 4440-4444.
37. Schreier, A. A. and Schimmel, P. R. (1975). Interaction of Polyamines with Fragments and Whole Molecules of Yeast Phenylalanine Specific Transfer RNA. J. Mol. Biol. 93: 323-329.
36. Schwartz, A. M. and Schimmel, P. R. (1974). Relaxation Spectra of the Iron Spin Transition in Methemoglobin. J. Mol. Biol. 89: 505-510.
35. Schreier, A. A. and Schimmel, P. R. (1974). Interaction of Manganese with Fragments, Complementary Fragment Recombinations, and Whole Molecules of Yeast Phenylalanine Specific Transfer RNA. J. Mol. Biol. 86: 601-620.
34. Rhodes, L. M. and Schimmel, P. R. (1974). Intermolecular Proton Transfer Reaction Between Base and Phosphate Moieties of Mononucleotides in Solution. J. Amer. Chem. Soc. 96: 2609-2611.
33. Gamble, R. C. and Schimmel, P. R. (1974). Transfer RNA Conformation in Solution Investigated by Isotope Labeling. Proc. Natl. Acad. Sci. U S A. 71: 1356-1360.
32. Lynch, D. C. and Schimmel, P. R. (1974). Effects of Abnormal Base Ionizations on Mg2 plus Binding to Transfer Ribonucleic Acid as Studied by a Fluorescent Probe. Biochemistry 13: 1852-1861.
31. Lynch, D. C. and Schimmel, P. R. (1974). Cooperative Binding of Magnesium to Transfer Ribonucleic Acid Studied by a Fluorescent Probe. Biochemistry 13: 1841-1851.
30. Schoemaker, H. J. P. and Schimmel, P. R. (1974). Photo-Induced Joining of a Transfer RNA with its Cognate Aminoacyl Transfer RNA Synthetase. J. Mol. Biol. 84: 503-513.
29. Söll, D. and Schimmel, P. R. (1974). Aminoacyl tRNA Synthetases. In The Enzymes pp. 489-538.
28. Schimmel, P. R. (1973). Mechanism of Aminoacyl Transfer Ribonucleic Acid Synthetase. Acc. Chem. Res. 6: 299-305.
27. Schimmel, P. R. and Lynch, D. C. (1973). Interactions and Conformational Transitions of a Transfer RNA Monitored by a Covalently Attached Fluorescent Probe. Polymer Preprints 14: 143-148.
26. Eldred, E. W. and Schimmel, P. R. (1973). Release of Aminoacyl Transfer Ribonucleic Acid from Transfer Ribonucleic Acid Synthetase Studied by Rapid Molecular Sieve Chromatography. Anal. Biochem. 51: 229-239.
25. McNeil, M. R. and Schimmel, P. R. (1972). Effect of Transfer Ribonucleic Acid on the Rate Law and Mechanism of the Adenosine Triphosphate-Pyrophosphate Isotope Exchange Reaction of an Aminoacyl Transfer Ribonucleic Acid Synthetase. Arch. Biochem. Biophys. 152: 175-179.
24. Eldred, E. W. and Schimmel, P. R. (1972). Rapid Deacylation by Isoleucyl Transfer Ribonucleic Acid Synthetase of Isoleucine Specific Transfer Ribonucleic Acid Aminoacylated with Valine. J. Biol. Chem. 247: 2961-2964.
23. Schreier, A. A. and Schimmel, P. R. (1972). Transfer Ribonucleic Acid Synthetase Catalyzed Deacylation of Aminoacyl Transfer Ribonucleic Acid in the Absence of Adenosine Monophosphate and Pyrophosphate. Biochemistry 11: 1582-1589.
22. Lo, H. H. and Schimmel, P. R. (1972). Effect of 2-3-Diphosphoglycerate and ATP on Ethyl Isocyanide Binding to Human Hemoglobin. Biochim. Biophys. Acta 263: 304-308.
21. Schimmel, P. R., Uhlenbeck, O. C., Lewis J. B., Dickson, L. A., Eldred, E. W., and Schreier, A. A. (1972). Binding of Complementary Oligonucleotides to Free and Aminoacyl Transfer Ribonucleic Acid Synthetase Bound Transfer Ribonucleic Acid. Biochemistry 11: 642-646.
20. Eldred, E. W. and Schimmel, P. R. (1972). Investigation of the Transfer of Amino Acid from a Transfer Ribonucleic Acid Synthetase Aminoacyl Adenylate Complex to Transfer Ribonucleic Acid. Biochemistry 11: 17-23.
19. Rhodes, L. M. and Schimmel, P. R. (1971). Nanosecond Relaxation Processes in Aqueous Mononucleoside Solutions. Biochemistry 10: 4426-4433.
18. Schimmel, P. R. (1971). On the Calculation of Chemical Relaxation Amplitudes. J. Chem. Phys. 54: 4136-4137.
17. Schimmel, P. R. and Leung, J. G.-M. (1970). Dipole Moments of Nonzwitterionic Polypeptide Chain Molecules. Macromolecules 3: 704-705.
16. Cole, F. X. and Schimmel, P. R. (1970). Isoleucyl Transfer Ribonucleic Acid Synthetase. The Role of Magnesium in Amino Acid Activation. Biochemistry 9: 3143-3148.
15. Hammes, G. G. and Schimmel, P. R. (1970). Rapid Reactions and Transient States. Enzymes 2: 67-114.
14. Cole, F. X. and Schimmel, P. R. (1970). On the Rate Law and Mechanism of the Adenosine Triphosphate-Pyrophosphate Isotope Exchange Reaction of Amino Acyl Transfer Ribonucleic Acid Synthetases. Biochemistry 9: 480-489.
13. Lo, H. H. and Schimmel, P. R. (1969). Interaction of Human Hemoglobin with Adenine Nucleotides. J. Biol. Chem. 244: 5084-5086.
12. Kowalski, C. J. and Schimmel, P. R. (1969). Interaction of Lysozyme with alpha-N-Acetyl-D-Glucosamine. J. Biol. Chem. 244: 3643-3646.
11. Chipman, D. M. and Schimmel, P. R. (1968). Dynamics of Lysozyme-Saccharide Interactions. J. Biol. Chem. 243: 3771-3774.
10. Schimmel, P. R. and Flory, P. J. (1968). Conformational Energies and Configurational Statistics of Copolypeptides Containing L-Proline. J. Mol. Biol. 34: 105-120.
9. Flory, P. J. and Schimmel, P. R. (1967). Dipole Moments in Relation to Configuration of Polypeptide Chains. J. Am. Chem. Soc. 89: 6807-6813.
8. Brant, D. A. and Schimmel, P. R. (1967). Analysis of the Skeletal Configuration of Crystalline Hen Egg-White Lysozyme. Proc. Natl. Acad. Sci. U S A. 58, 428-435.
7. Schimmel, P. R. and Flory, P. J. (1967). Conformational Energy and Configurational Statistics of Poly-L-Proline. Proc. Nat. Acad. Sci. U S A. 58: 52-59.
6. Hammes, G. G. and Schimmel, P. R. (1967). Relaxation Spectra of Enzymatic Reactions. J. Phys. Chem. 71: 917-923.
5. Hammes, G. G. and Schimmel, P. R. (1967). An Investigation of Water-Urea and Water-Urea Polyethylene Glycol Interactions. J. Am. Chem. Soc. 89: 442-446.
4. Hammes, G. G. and Schimmel, P. R. (1966). Chemical Relaxation Spectra: Calculation of Relaxation Times for Complex Mechanisms. J. Phys. Chem. 70: 2319-2324.
3. Cathou, R. E., Hammes, G. G., and Schimmel, P. R. (1965). Optical Rotatory Dispersion of Ribonuclease and Ribonuclease-Nucleotide Complexes. Biochemistry 4: 2687-2690.
2. Hammes, G. G. and Schimmel, P. R. (1965). Equilibrium Measurements of the Binding of Cytidine 3'-Phosphate to Ribonuclease. J. Am. Chem. Soc. 87: 4665-4669.
1. Fasella, P., Hammes, G. G., and Schimmel, P. R. (1965). A Sephadex Dialysis Method of Determining Small Molecule-Macromolecule Binding Constants. Biochim. Biophys. Acta 103: 708-710.
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