Please click for a complete list of publications from The Schimmel-Yang Laboratory

Please click for complete list of publications from Prof. Xiang-Lei Yang

Selected Publications for the Schimmel-Yang Laboratory:

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.

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. (2009). Orthogonal use of active of human tRNA synthetase to achieve multifunctionality, Nature Str. Mol. Biol, in press.

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, in press.

The Schimmel-Yang Laboratory
The Scripps Research Institute
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