Selected Publications
Please click for a complete list of publications from Prof. Paul Schimmel
Please click for complete list of publications from Prof. Xiang-Lei Yang
Please click for complete list of publications from Prof. Min Guo
Cantor, C. R. and Schimmel, P. R. (1980). Biophysical Chemistry (3 volumes) Part I: The Conformation of Biological Macromolecules. Part II: Techniques for the Study of Biological Structure and Function. Part III: The Behavior of Biological Macromolecules. 1369pp. (San Francisco, W. H. Freeman).
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.
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.
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.
Putney, S.D., Herlihy, W.C. , 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.
Jasin, M., Regan, L. and Schimmel, P. (1984). Dispensable Pieces of an Aminoacyl tRNA Synthetase Which Activate the Catalytic Site, Cell 36: 1089-1095.
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.
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.
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.
Starzyk, R. M., Webster, T. A., and Schimmel, P. (1987). Evidence for Insertion of Dispensable Sequences into a Nucleotide Fold. Science 237: 1614-1618.
Clarke, Neil D., Lien, Donald C. and Schimmel, P. (1988). Cassette Mutagenesis Can Provide Evidence for a Structure-Function Motif in a Protein of Unknown Structure. Science 240: 521-523.
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.
Francklyn, C. and Schimmel, P. (1989). RNA Minihelices Can Be Aminoacylated with Alanine. Nature 337: 478-481.
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.
Francklyn, C., Shi, J.-P. and Schimmel, P. (1992). Overlapping Nucleotide Determinants for Specific Aminoacylation of RNA Microhelices. Science 255: 1121-1125.
Musier-Forsyth, K. and Schimmel, P. (1992). Functional Contacts of a tRNA Synthetase with 2'-Hydroxyl Groups in the RNA Minor Groove. Nature 357: 513-515.
Schmidt, E. and Schimmel, P. (1994). Mutational Isolation of a Sieve for Editing in a Transfer RNA Synthetase. Science 264: 265-267
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.
Lin, L., Hale, S. P. and Schimmel, P. (1996). Aminoacylation Error Correction. Nature 384: 33-34.
Hale, S. P., Auld, D. S., Schmidt, E., and Schimmel, P. (1997). Discrete Nucleotides in tRNA for Editing and Aminoacylation. Science 276: 1250-1252.
Wakasugi, K. and Schimmel, P. (1999). Two distinct cytokines released from a human aminoacyl tRNA synthetase. Science 284: 147-151.
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.
Döring, V., Mootz, H. D., Nangle, L. A., Hendrickson, T. L., De Crécy-Lagard, V., Schimmel, P.* and Marlière, P.* (2001) (*Corresponding authors). Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway. Science 292: 501-504.
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. USA 99: 173-177.
Tamura, K. and Schimmel, P. (2004). Chiral selective aminoacylation of an RNA minihelix. Science 305: 1253.
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 turmors targets tRNA synthetase. Science 309: 1533
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 in the sticky mouse. Nature 443: 50-55.
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—RNA complex: implications for protein synthesis. EMBO J. 25: 2919-2929.
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
Beebe, K., Mock, M., Merriman, E., and Schimmel, P. (2008). Distinct domains of tRNA synthetase recognize the same base pair. Nature 451: 90-94
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. and Biol. 16: 531–539.
Guo, M., Chong, Y. E., Yang, X.-L., and Schimmel, P. (2009). The C-Ala domain brings together editing and aminoacylation functions on a single tRNA. Science 325: 744-747.
Guo, M., Chong, Y. E., Shapiro, R., Beebe, K., Yang, X.-L., and Schimmel, P. (2009). Mistranslation from Serine Paradox Caused by AlaRS Recognition Dilemma, Nature 462: 808-812.
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 active of human tRNA synthetase to achieve multifunctionality, Nature Str. Mol. Biol 17: 57-61.
Guo, M., Yang, X.-L., and Schimmel, P. (2010). New functions of aminoacyl tRNA synthetases beyond translation. Nature Rev. Mol. Cell. Biol. 11: 668-674.
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. USA 108:2723-2728.
Schimmel, P. (2011). The RNP bridge between two worlds. Nat Rev Mol Cell Biol. 12:135.
Vo MN, Yang XL, Schimmel P. (2011). Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase. J. Biol Chem. 286:11563-8.
Fang P, Zhang HM, Shapiro R, Marshall AG, Schimmel P, Yang XL, Guo M. (2011). Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex. Proc Natl Acad Sci USA 108:8239-44.
Yang XL, Schimmel P. (2011). Functional expansion of the tRNA world under stress. Mol Cell 43:500-2.
Schimmel, P. (2011). Mistranslation and its control by tRNA synthetases. Philos Trans R Soc Lond B Biol Sci. 366:2965-71.
Guo M, Schimmel P. (2012). Structural analyses clarify the complex conrol of mistranslation by tRNA synthetases. Curr Opin Struct Biol. 1:119-26.
Wang J, Fang P, Schimmel P, Guo M. (2012). Side Chain Independent Recognition of Aminoacyl Adenylates by the Hint1 Transcription Suppressor. J Phys Chem B.
Park MC, Kang T, Jin D, Han JM, Kim SB, Park YJ, Cho K, Park YW, Guo M, He W, Yang XL, Schimmel P, Kim S. (2012). Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis. Proc Natl Acad Sci USA.109:E640-7
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