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Schimmel, Paul
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Schimmel, Paul

Faculty Member
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Positions

  • 2017 - Professor, Molecular Medicine , Scripps Research
  • 2013 - Professor (Joint Appointment), Chemistry , Scripps Research
  • 1997 - Faculty Member, Skaggs Graduate School of Chemical and Biological Sciences , Scripps Research
  • 1997 - Member, The Skaggs Institute for Chemical Biology , Scripps Research
  • John D. and Catherine T. MacArthur Professor of Biochemistry and Biophysics, Massachusetts Institute of Technology
  • 2013 - 2017 Professor, Cell and Molecular Biology (CMB) , Scripps Research
  • 1997 - 2012 Ernest and Jean Hahn Professor, Molecular Biology , Scripps Research
Dr. Paul Schimmel is examining the nature, origins, and boundaries of the genetic code, probing the molecular basis of tRNA specificity and the manipulative potential of tRNAs and their enzymes as tools for developing new proteins, cellular functions, and potential therapeutics.

Contact

  • schimmel@scripps.edu

Websites

  • Paul Schimmel, Ph.D.
  • Schimmel-Yang Laboratory
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Publications

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    • Kuhle, B., Chihade, J., Schimmel, P. Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs Nature Communications  2020 11  DOI:10.1038/s41467-020-14725-y  PMID:32080176  PMCID:PMC7033119
    • Blocquel, D., Sun, L., Matuszekc, Z., Li, S., Weber, T., Kuhle, B., Kooi, G., Wei, N., Baets, J., Pan, T., Schimmel, P., Yang, X. L. CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells Proceedings of the National Academy of Sciences of the United States of America  2019 116:19440-19448  DOI:10.1073/pnas.1908288116  PMID:31501329
    • Kanaji, T., Vo, M. N., Kanaji, S., Zarpellon, A., Shapiro, R., Morodomi, Y., Yuzuriha, A., Eto, K., Belani, R., Do, M. H., Yang, X. L., Ruggeri, Z. M., et al. Tyrosyl-tRNA synthetase stimulates thrombopoietin-independent hematopoiesis accelerating recovery from thrombocytopenia Proceedings of the National Academy of Sciences of the United States of America  2018 115:EB228-EB235  DOI:10.1073/pnas.1807000115  PMID:30104364  PMCID:PMC6126720
    • Chong, Y. E., Guo, M., Yang, X. L., Kuhle, B., Naganuma, M., Sekine, S., Yokoyama, S., Schimmel, P. Distinct ways of G:U recognition by conserved tRNA binding motifs Proceedings of the National Academy of Sciences of the United States of America  2018 115:7527-7532  DOI:10.1073/pnas.1807109115  PMID:29967150  PMCID:PMC6055181
    • Xu, Z., Lo, W. S., Beck, D. B., Schuch, L. A., Olahova, M., Kopajtich, R., Chong, Y. E., Alston, C. L., Seidl, E., Zhai, L., Lau, C. F., Timchak, D., et al. Bi-allelic mutations in phe-tRNA synthetase associated with a multi-system pulmonary disease Support non-translational function American Journal of Human Genetics  2018 103:100-114  DOI:10.1016/j.ajhg.2018.06.006  PMID:29979980  PMCID:PMC6035289
    • Vo, M. N., Terrey, M., Lee, J. W., Roy, B., Moresco, J. J., Sun, L. T., Fu, H. J., Liu, Q., Weber, T. G., Yates III, J. R., Fredrick, K., Schimmel, P., et al. ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase Nature  2018 557:510-515  DOI:10.1038/s41586-018-0137-8  PMID:29769718  PMCID:PMC5973781
    • Xu, X., Zhou, H., Zhou, Q., Hong, F., Vo, M. N., Niu, W., Wang, Z., Xiong, X., Nakamura, K., Wakasugi, K., Schimmel, P., Yang, X. L. An alternative conformation of human TrpRS suggests a role of zinc in activating non-enzymatic function Rna Biology  2018 15:649-658  DOI:10.1080/15476286.2017.1377868  PMID:28910573  PMCID:PMC6103731
    • Schimmel, P. The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis Nature Reviews Molecular Cell Biology  2018 19:45-58  DOI:10.1038/nrm.2017.77  PMID:28875994
    • Song, Y., Zhou, H., Vo, M. N., Shi, Y., Nawaz, M. H., Vargas-Rodriguez, O., Diedrich, J. K., Yates III, J. R., Kishi, S., Musier-Forsyth, K., Schimmel, P. Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid Nature Communications  2017 8  DOI:10.1038/s41467-017-02201-z  PMID:29273753  PMCID:PMC5741666
    • 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. Alternative stable conformation capable of protein misinteraction links tRNA synthetase to peripheral neuropathy Nucleic Acids Research  2017 45:8091-8104  DOI:10.1093/nar/gkx455  PMID:28531329
    • Sun, L., Song, Y., Blocquel, D., Yang, X. L., Schimmel, P. Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS Proceedings of the National Academy of Sciences of the United States of America  2016 113:14300-14305  DOI:10.1073/pnas.1617316113  PMID:27911835  PMCID:PMC5167178
    • Sun, L., Gomes, A. C., He, W., Zhou, H., Wang, X., Pan, D. W., Schimmel, P., Pan, T., Yang, X. L. Evolutionary gain of alanine mischarging to noncognate tRNAs with a G4:U69 base pair Journal of the American Chemical Society  2016 138:12948-12955  DOI:10.1021/jacs.6b07121  PMID:27622773
    • Song, Y., Shi, Y., Carland, T. M., Lian, S., Sasaki, T., Schork, N. J., Head, S. R., Kishi, S., Schimmel, P. p53-Dependent DNA damage response sensitive to editing-defective tRNA synthetase in zebrafish Proceedings of the National Academy of Sciences of the United States of America  2016 113:8460-8465  DOI:10.1073/pnas.1608139113  PMID:27402763  PMCID:PMC4968768
    • 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., Schimmel, P. Alternative splicing creates two new architectures for human tyrosyl-tRNA synthetase Nucleic Acids Research  2016 44:1247-1255  DOI:10.1093/nar/gkw002  PMID:26773056  PMCID:PMC4756856
    • Schimmel, P. Alexander Rich (1924-2015) Nature  2015 521:291  DOI:10.1038/521291a  PMID:25993953
    • 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., et al. The cytoplasmic prolyl-tRNA synthetase of the malaria parasite is a dual-stage target of febrifugine and its analogs Science Translational Medicine  2015 7  DOI:10.1126/scitranslmed.aaa3575  PMID:25995223  PMCID:PMC4675670
    • Sajish, M., Schimmel, P. A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol Nature  2015 519:370-373  DOI:10.1038/nature14028  PMID:25533949  PMCID:PMC4368482
    • Liu, Y., Satz, J. S., Vo, M. N., Nangle, L. A., Schimmel, P., Ackerman, S. L. Deficiencies in tRNA synthetase editing activity cause cardioproteinopathy Proceedings of the National Academy of Sciences of the United States of America  2014 111:17570-17575  DOI:10.1073/pnas.1420196111  PMID:25422440  PMCID:PMC4267364
    • Ishimura, R., Nagy, G., Dotu, I., Zhou, H., Yang, X. L., Schimmel, P., Senju, S., Nishimura, Y., Chuang, J. H., Ackerman, S. L. Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration Science  2014 345:455-459  DOI:10.1126/science.1249749  PMID:25061210  PMCID:PMC4281038
    • Lo, W. S., Gardiner, E., Xu, Z., Lau, C. F., Wang, F., Zhou, J. J., Mendlein, J. D., Nangle, L. A., Chiang, K. P., Yang, X. L., Au, K. F., Wong, W. H., et al. Human tRNA synthetase catalytic nulls with diverse functions Science  2014 345:328-332  DOI:10.1126/science.1252943  PMID:25035493  PMCID:PMC4188629
    • Zhou, J. 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., Schimmel, P. Secreted histidyl-tRNA synthetase splice variants elaborate major epitopes for autoantibodies in inflammatory myositis Journal of Biological Chemistry  2014 289:19269-19275  DOI:10.1074/jbc.C114.571026  PMID:24898250  PMCID:PMC4094037
    • Naganuma, M., Sekine, S., Chong, Y. E., Guo, M., Yang, X. L., Gamper, H., Hou, Y. M., Schimmel, P., Yokoyama, S. The selective tRNA aminoacylation mechanism based on a single G.U pair Nature  2014 510:507-511  DOI:10.1038/nature13440  PMID:24919148  PMCID:PMC4323281
    • Wang, F., Xu, Z., Zhou, J., Lo, W. S., Lau, C. F., Nangle, L. A., Yang, X. L., Zhang, M., Schimmel, P. Regulated capture by exosomes of mRNAs for cytoplasmic tRNA synthetases Journal of Biological Chemistry  2013 288:29223-29228  DOI:10.1074/jbc.C113.490599  PMID:24003230  PMCID:PMC3795223
    • Klipcan, L., Safro, M., Schimmel, P. Anticodon G recognition by tRNA synthetases mimics the tRNA core Trends in Biochemical Sciences  2013 38:229-232  DOI:10.1016/j.tibs.2012.11.002  PMID:23266103  PMCID:PMC3634914
    • Guo, M., Schimmel, P. Essential nontranslational functions of tRNA synthetases Nature Chemical Biology  2013 9:145-153  DOI:10.1038/nchembio.1158  PMID:23416400  PMCID:PMC3773598
    • Zhou, H. H., Sun, L. T., Yang, X. L., Schimmel, P. ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase Nature  2013 494:121-124  DOI:10.1038/nature11774  PMID:23263184  PMCID:PMC3569068
    • Ofir-Birin, Y., Fang, P. F., Bennett, S. P., Zhang, H. M., Wang, J., Rachmin, I., Shapiro, R., Song, J., Dagan, A., Pozo, J., Kim, S., Marshall, A. G., et al. Structural switch of lysyl-tRNA synthetase between translation and transcription Molecular Cell  2013 49:30-42  DOI:10.1016/j.molcel.2012.10.010  PMID:23159739  PMCID:PMC3766370
    • Guo, M., Schimmel, P. Homeostatic mechanisms by alternative forms of tRNA synthetases Trends in Biochemical Sciences  2012 37:401-403  DOI:10.1016/j.tibs.2012.07.003  PMID:22858252  PMCID:PMC3459177
    • Xu, Z. W., Wei, Z. Y., Zhou, J. J., Ye, F., Lo, W. S., Wang, F., Lau, C. F., Wu, J. J., Nangle, L. A., Chiang, K. P., Yang, X. L., Zhang, M. J., et al. Internally deleted human tRNA synthetase suggests evolutionary pressure for repurposing Structure  2012 20:1470-1477  DOI:10.1016/j.str.2012.08.001  PMID:22958643  PMCID:PMC3485694
    • Wang, J., Fang, P. F., Schimmel, P., Guo, M. Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor Journal of Physical Chemistry B  2012 116:6798-6805  DOI:10.1021/jp212457w  PMID:22329685  PMCID:PMC3375047
    • Lee, P. S., Zhang, H. M., Marshall, A. G., Yang, X. L., Schimmel, P. Uncovering of a short internal peptide activates a tRNA synthetase procytokine Journal of Biological Chemistry  2012 287:20504-20508  DOI:10.1074/jbc.C112.369439  PMID:22549774  PMCID:PMC3370235
    • Sajish, M., Zhou, Q. S., Kishi, S., Valdez, D. M., Kapoor, M., Guo, M., Lee, S., Kim, S., Yang, X. L., Schimmel, P. Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-γ and p53 signaling Nature Chemical Biology  2012 8:547-554  DOI:10.1038/nchembio.937  PMID:22504299  PMCID:PMC3780985
    • 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., et al. Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis Proceedings of the National Academy of Sciences of the United States of America  2012 109:E640-E647  DOI:10.1073/pnas.1200194109  PMID:22345558  PMCID:PMC3306665
    • Guo, M., Schimmel, P. Structural analyses clarify the complex control of mistranslation by tRNA synthetases Current Opinion in Structural Biology  2012 22:119-126  DOI:10.1016/j.sbi.2011.11.008  PMID:22155179  PMCID:PMC3288634
    • Schimmel, P. Mistranslation and its control by tRNA synthetases Philosophical Transactions of the Royal Society B-Biological Sciences  2011 366:2965-2971  DOI:10.1098/rstb.2011.0158  PMID:21930589  PMCID:PMC3158927
    • Yang, X. L., Schimmel, P. Functional expansion of the tRNA world under stress Molecular Cell  2011 43:500-502  DOI:10.1016/j.molcel.2011.08.004  PMID:21855789  PMCID:PMC3163667
    • Fang, P. F., Zhang, H. M., Shapiro, R., Marshall, A. G., Schimmel, P., Yang, X. L., Guo, M. Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex Proceedings of the National Academy of Sciences of the United States of America  2011 108:8239-8244  DOI:10.1073/pnas.1100224108  PMID:21536907  PMCID:PMC3100937
    • Vo, M. N., Yang, X. L., Schimmel, P. Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase Journal of Biological Chemistry  2011 286:11563-11568  DOI:10.1074/jbc.C110.213876  PMID:21310955  PMCID:PMC3064210
    • Schimmel, P. The RNP bridge between two worlds Nature Reviews Molecular Cell Biology  2011 12:135  DOI:10.1038/nrm3061  PMID:21285979
    • Nawaz, M. H., Merriman, E., Yang, X. L., Schimmel, P. p23(H) implicated as cis/trans regulator of AlaXp-directed editing for mammalian cell homeostasis Proceedings of the National Academy of Sciences of the United States of America  2011 108:2723-2728  DOI:10.1073/pnas.1019400108  PMID:21285375  PMCID:PMC3041069
    • Guo, M., Shapiro, R., Morris, G. M., Yang, X. L., Schimmel, P. Packaging HIV virion components through dynamic equilibria of a human tRNA synthetase Journal of Physical Chemistry B  2010 114:16273-16279  DOI:10.1021/jp1082517  PMID:21058683  PMCID:PMC3042951
    • Han, G. W., Yang, X. L., McMullan, D., Chong, Y. E., Krishna, S. S., Rife, C. L., Weekes, D., Brittain, S. M., Abdubek, P., Ambing, E., Astakhova, T., Axelrod, H. L., et al. Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster Acta Crystallographica Section F-Structural Biology and Crystallization Communications  2010 66:1326-1334  DOI:10.1107/s1744309110037619  PMID:20944229  PMCID:PMC2954223
    • Guo, M., Yang, X. L., Schimmel, P. New functions of aminoacyl-tRNA synthetases beyond translation Nature Reviews Molecular Cell Biology  2010 11:668-674  DOI:10.1038/nrm2956  PMID:20700144  PMCID:PMC3042954
    • Guo, M., Shapiro, R., Schimmel, P., Yang, X. L. Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase Acta Crystallographica Section D-Biological Crystallography  2010 66:243-250  DOI:10.1107/s0907444909055462  PMID:20179335  PMCID:PMC2827346
    • Guo, M., Schimmel, P., Yang, X. L. Functional expansion of human tRNA synthetases achieved by structural inventions FEBS Letters  2010 584:434-442  DOI:10.1016/j.febslet.2009.11.064  PMID:19932696  PMCID:PMC2826164
    • Zhou, Q. S., Kapoor, M., Guo, M., Belani, R., Xu, X. L., Kiosses, W. B., Hanan, M., Park, C., Armour, E., Do, M. H., Nangle, L. A., Schimmel, P., et al. Orthogonal use of a human tRNA synthetase active site to achieve multifunctionality Nature Structural & Molecular Biology  2010 17:57-61  DOI:10.1038/nsmb.1706  PMID:20010843  PMCID:PMC3042952
    • Guo, M., Chong, Y. E., Shapiro, R., Beebe, K., Yang, X. L., Schimmel, P. Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma Nature  2009 462:808-812  DOI:10.1038/nature08612  PMID:20010690  PMCID:PMC2799227
    • Sankaran, B., Bonnett, S. A., Shah, K., Gabriel, S., Reddy, R., Schimmel, P., Rodionov, D. A., de Crecy-Lagard, V., Helmann, J. D., Iwata-Reuyl, D., Swairjo, M. A. Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence for GTP cyclohydrolase IB Journal of Bacteriology  2009 191:6936-6949  DOI:10.1128/jb.00287-09  PMID:19767425  PMCID:PMC2772490
    • 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., et al. Dominant mutations in the tyrosyl-tRNA synthetase gene recapitulate in Drosophila features of human Charcot-Marie-Tooth neuropathy Proceedings of the National Academy of Sciences of the United States of America  2009 106:11782-11787  DOI:10.1073/pnas.0905339106  PMID:19561293  PMCID:PMC2702257
    • El Yacoubi, B., Lyons, B., Cruz, Y., Reddy, R., Nordin, B., Agnelli, F., Williamson, J. R., Schimmel, P., Swairjo, M. A., de Crecy-Lagard, V. The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA Nucleic Acids Research  2009 37:2894-2909  DOI:10.1093/nar/gkp152  PMID:19287007  PMCID:PMC2685093
    • Schimmel, P., Guo, M. A tipping point for mistranslation and disease Nature Structural & Molecular Biology  2009 16:348-349  DOI:10.1038/nsmb0409-348  PMID:19343067
    • Schimmel, P., Guo, M. Ancient tRNA synthetase meets modern structural biology Structure  2009 17:315-317  DOI:10.1016/j.str.2009.02.002  PMID:19278642
    • Guo, M., Chong, Y. E., Beebe, K., Shapiro, R., Yang, X. L., Schimmel, P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA Science  2009 325:744-747  DOI:10.1126/science.1174343  PMID:19661429  PMCID:PMC4559334
    • Chong, Y. E., Yang, X. L., Schimmel, P. Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation Journal of Biological Chemistry  2008 283:30073-30078  DOI:10.1074/jbc.M805943200  PMID:18723508  PMCID:PMC2573062
    • Schimmel, P. An editing activity that prevents mistranslation and connection to disease Journal of Biological Chemistry  2008 283:28777-28782  DOI:10.1074/jbc.X800007200  PMID:18640977  PMCID:PMC2661996
    • Schimmel, P. Development of tRNA synthetases and connection to genetic code and disease Protein Science  2008 17:1643-1652  DOI:10.1110/ps.037242.108  PMID:18765819  PMCID:PMC2548368
    • Cheng, G., Zhang, H., Yang, X. L., Tzima, E., Ewalt, K. L., Schimmel, P., Faber, J. E. Effect of mini-tyrosyl-tRNA synthetase on ischemic angiogenesis, leukocyte recruitment, and vascular permeability American Journal of Physiology-Regulatory Integrative and Comparative Physiology  2008 295:R1138-R1146  DOI:10.1152/ajpregu.90519.2008  PMID:18753262
    • Park, S. G., Schimmel, P., Kim, S. Aminoacyl tRNA synthetases and their connections to disease Proceedings of the National Academy of Sciences of the United States of America  2008 105:11043-11049  DOI:10.1073/pnas.0802862105  PMID:18682559  PMCID:PMC2516211
    • Greenberg, Y., King, M., Kiosses, W. B., Ewalt, K., Yang, X., Schimmel, P., Reader, J. S., Tzima, E. The novel fragment of tyrosyl tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells FASEB Journal  2008 22:1597-1605  DOI:10.1096/fj.07-9973com  PMID:18165356
    • Guo, M., Ignatov, M., Musier-Forsyth, K., Schimmel, P., Yang, X. L. Crystal structure of tetrameric form of human lysyl-tRNA synthetase: implications for multisynthetase complex formation Proceedings of the National Academy of Sciences of the United States of America  2008 105:2331-2336  DOI:10.1073/pnas.0712072105  PMID:18272479  PMCID:PMC2268136
    • Zhou, Q. S., Kiosses, W. B., Liu, J., Schimmel, P. Tumor endothelial cell tube formation model for determining anti-angiogenic activity of a tRNA synthetase cytokine Methods  2008 44:190-195  DOI:10.1016/j.ymeth.2007.10.004  PMID:18241800  PMCID:PMC3835186
    • Kapoor, M., Zhou, Q., Otero, F., Myers, C. A., Bates, A., Belani, R., Liu, J., Luo, J. K., Tzima, E., Zhang, D. E., Yang, X. L., Schimmel, P. Evidence for annexin II-S100A10 complex and plasmin in mobilization of cytokine activity of human TrpRS Journal of Biological Chemistry  2008 283:2070-2077  DOI:10.1074/jbc.M706028200  PMID:17999956
    • Beebe, K., Mock, M., Merriman, E., Schimmel, P. Distinct domains of tRNA synthetase recognize the same base pair Nature  2008 451:90-93  DOI:10.1038/nature06454  PMID:18172502
    • Yang, X. L., Kapoor, M., Otero, F. J., Slike, B. M., Tsuruta, H., Frausto, R., Bates, A., Ewalt, K. L., Cheresh, D. A., Schimmel, P. Gain-of-function mutational activation of human tRNA synthetase procytokine Chemistry & Biology  2007 14:1323-1333  DOI:10.1016/j.chembiol.2007.10.016  PMID:18096501  PMCID:PMC2693404
    • Zubieta, C., Krishna, S. S., Kapoor, M., Kozbial, P., McMullan, D., Axelrod, H. L., Miller, M. D., Abdubek, P., Ambing, E., Astakhova, T., Carlton, D., Chiu, H. J., et al. Crystal structures of two novel dye-decolorizing peroxidases reveal a β-barrel fold with a conserved heme-binding motif Proteins-Structure Function and Bioinformatics  2007 69:223-233  DOI:10.1002/prot.21550  PMID:17654545
    • Zubieta, C., Joseph, R., Krishna, S. S., McMullan, D., Kapoor, M., Axelrod, H. L., Miller, M. D., Abdubek, P., Acosta, C., Astakhova, T., Carlton, D., Chiu, H. J., et al. Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA Proteins-Structure Function and Bioinformatics  2007 69:234-243  DOI:10.1002/prot.21673  PMID:17654547
    • Waas, W. F., Schimmel, P. Evidence that tRNA synthetase-directed proton transfer stops mistranslation Biochemistry  2007 46:12062-12070  DOI:10.1021/bi7007454  PMID:17924654
    • Waas, W. F., Druzina, Z., Hanan, M., Schimmel, P. Role of a tRNA base modification and its precursors in frameshifting in eukaryotes Journal of Biological Chemistry  2007 282:26026-26034  DOI:10.1074/jbc.M703391200  PMID:17623669
    • Beebe, K., Waas, W., Druzina, Z., Guo, M., Schimmel, P. A universal plate format for increased throughput of assays that monitor multiple aminoacyl transfer RNA synthetase activities Analytical Biochemistry  2007 368:111-121  DOI:10.1016/j.ab.2007.05.013  PMID:17603003  PMCID:PMC3833075
    • Bacher, J. A., Waas, W. F., Metzgar, D., de Crecy-Lagard, V., Schimmel, P. Genetic code ambiguity confers a selective advantage on Acinetobacter baylyi Journal of Bacteriology  2007 189:6494-6496  DOI:10.1128/jb.00622-07  PMID:17616603  PMCID:PMC1951902
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    • Schimmel, P., Kelley, S. O. Exiting an RNA world Nature Structural Biology  2000 7:5-7  DOI:10.1038/71194  PMID:10625414
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    • Chihade, J. W., Schimmel, P. Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains Proceedings of the National Academy of Sciences of the United States of America  1999 96:12316-12321  DOI:10.1073/pnas.96.22.12316  PMID:10535919  PMCID:PMC22914
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    • Schimmel, P., Ribas de Pouplana, L. Genetic code origins: experiments confirm phylogenetic predictions and may explain a puzzle Proceedings of the National Academy of Sciences of the United States of America  1999 96:327-328  DOI:10.1073/pnas.96.2.327  PMID:9892630  PMCID:PMC33543
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    • Schimmel, P., Tao, J. S., Hill, J. Aminoacyl tRNA synthetases as targets for new anti-infectives FASEB Journal  1998 12:1599-1609  PMID:9837850
    • Alexander, R. W., Nordin, B. E., Schimmel, P. Activation of microhelix charging by localized helix destabilization Proceedings of the National Academy of Sciences of the United States of America  1998 95:12214-12219  DOI:10.1073/pnas.95.21.12214  PMID:9770466  PMCID:PMC22811
    • Henderson, B. S., Beuning, P. J., Shi, J. P., Bald, R., Furste, J. P., Erdmann, V. A., Musier-Forsyth, K., Schimmel, P. Subtle functional interactions in the RNA minor groove at a nonessential base pair Journal of the American Chemical Society  1998 120:9110-9111  DOI:10.1021/ja9809152
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    • Chihade, J. W., Hayashibara, K., Shiba, K., Schimmel, P. Strong selective pressure to use G:U to mark an RNA acceptor stem for alanine Biochemistry  1998 37:9193-9202  DOI:10.1021/bi9804636  PMID:9636067
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    • Wakasugi, K., Quinn, C. L., Tao, N. J., Schimmel, P. Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant EMBO Journal  1998 17:297-305  DOI:10.1093/emboj/17.1.297  PMID:9427763  PMCID:PMC1170380
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    • Schimmel, P., Alexander, R. Perspectives: protein synthesis. All you need is RNA Science  1998 281:658-659  DOI:10.1126/science.281.5377.658  PMID:9714675
    • Shiba, K., Motegi, H., Schimmel, P. Maintaining genetic code through adaptations of tRNA synthetases to taxonomic domains Trends in Biochemical Sciences  1997 22:453-457  DOI:10.1016/s0968-0004(97)01135-3  PMID:9433122
    • Frugier, M., Schimmel, P. Subtle atomic group discrimination in the RNA minor groove Proceedings of the National Academy of Sciences of the United States of America  1997 94:11291-11294  DOI:10.1073/pnas.94.21.11291  PMID:9326602  PMCID:PMC23445
    • Beuning, P. J., Yang, F., Schimmel, P., Musier-Forsyth, K. Specific atomic groups and RNA helix geometry in acceptor stem recognition by a tRNA synthetase Proceedings of the National Academy of Sciences of the United States of America  1997 94:10150-10154  DOI:10.1073/pnas.94.19.10150  PMID:9294178  PMCID:PMC23330
    • Schimmel, P., Soll, D. When protein engineering confronts the tRNA world Proceedings of the National Academy of Sciences of the United States of America  1997 94:10007-10009  DOI:10.1073/pnas.94.19.10007  PMID:9294151  PMCID:PMC33764
    • Shiba, K., Stello, T., Motegi, H., Noda, T., Musier-Forsyth, K., Schimmel, P. Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant Journal of Biological Chemistry  1997 272:22809-22816  DOI:10.1074/jbc.272.36.22809  PMID:9278442
    • Hale, S. P., Schimmel, P. DNA aptamer targets translational editing motif in a tRNA synthetase Tetrahedron  1997 53:11985-11994  DOI:10.1016/s0040-4020(97)00711-4
    • Sen, S., Zhou, H. Y., Ripmaster, T., Hittelman, W. N., Schimmel, P., White, R. A. 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 Proceedings of the National Academy of Sciences of the United States of America  1997 94:6164-6169  DOI:10.1073/pnas.94.12.6164  PMID:9177188  PMCID:PMC21020
    • Glasfeld, E., Schimmel, P. Zinc-dependent tRNA binding by a peptide element within a tRNA synthetase Biochemistry  1997 36:6739-6744  DOI:10.1021/bi970151n  PMID:9184155
    • Henderson, B. S., Schimmel, P. RNA-RNA interactions between oligonucleotide substrates for aminoacylation Bioorganic & Medicinal Chemistry  1997 5:1071-1079  DOI:10.1016/s0968-0896(97)00043-6  PMID:9222500
    • Nair, S., Ribas de Pouplana, L., Houman, F., Avruch, A., Shen, X. Y., Schimmel, P. Species-specific tRNA recognition in relation to tRNA synthetase contact residues Journal of Molecular Biology  1997 269:1-9  DOI:10.1006/jmbi.1997.1025  PMID:9192996
    • Hale, S. P., Auld, D. S., Schmidt, E., Schimmel, P. Discrete determinants in transfer RNA for editing and aminoacylation Science  1997 276:1250-1252  DOI:10.1126/science.276.5316.1250  PMID:9157882
    • Whelihan, E. F., Schimmel, P. Rescuing an essential enzyme-RNA complex with a non-essential appended domain EMBO Journal  1997 16:2968-2974  DOI:10.1093/emboj/16.10.2968  PMID:9184240  PMCID:PMC1169904
    • Schimmel, P., Frugier, M., Glasfeld, E. Peptides for RNA discrimination and for assembly of enzymes that act on RNA Nucleic Acids Symposium Series  1997 1  PMID:9478188
    • Ribas de Pouplana, L., Schimmel, P. Reconstruction of quaternary structures of class II tRNA synthetases by rational mutagenensis of a conserved domain Biochemistry  1997 36:15041-15048  DOI:10.1021/bi971788+  PMID:9398230
    • Michaels, J. E. A., Schimmel, P., Shiba, K., Miller, W. T. Dominant negative inhibition by fragments of a monomeric enzyme Proceedings of the National Academy of Sciences of the United States of America  1996 93:14452-14455  DOI:10.1073/pnas.93.25.14452  PMID:8962072  PMCID:PMC26153
    • Schimmel, P., Musier-Forsyth, K. 'Distorted' RNA helix recognition Nature  1996 384:422  DOI:10.1038/384422a0  PMID:8945467
    • Lin, L., Hale, S. P., Schimmel, P. Aminoacylation error correction Nature  1996 384:33-34  DOI:10.1038/384033b0  PMID:8900273
    • Sassanfar, M., Kranz, J. E., Gallant, P., Schimmel, P., Shiba, K. A eubacterial Mycobacterium tuberculosis tRNA synthetase is eukaryote-like and resistant to a eubacterial-specific antisynthetase drug Biochemistry  1996 35:9995-10003  DOI:10.1021/bi9603027  PMID:8756461
    • Schimmel, P. Origin of genetic code: a needle in the haystack of tRNA sequences Proceedings of the National Academy of Sciences of the United States of America  1996 93:4521-4522  DOI:10.1073/pnas.93.10.4521  PMID:8643435
    • Lin, L., Schimmel, P. Mutational analysis suggests the same design for editing activities of two tRNA synthetases Biochemistry  1996 35:5596-5601  DOI:10.1021/bi960011y  PMID:8611551
    • Glasfeld, E., Landro, J. A., Schimmel, P. C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetase Biochemistry  1996 35:4139-4145  DOI:10.1021/bi9527810  PMID:8672449
    • Hale, S. P., Schimmel, P. Protein synthesis editing by a DNA aptamer Proceedings of the National Academy of Sciences of the United States of America  1996 93:2755-2758  DOI:10.1073/pnas.93.7.2755  PMID:8610114  PMCID:PMC39704
    • Auld, D. S., Schimmel, P. Single sequence of a helix-loop peptide confers functional anticodon recognition on two tRNA synthetases EMBO Journal  1996 15:1142-1148  PMID:8605884  PMCID:PMC450012
    • Gale, A. J., Shi, J. P., Schimmel, P. Evidence that specificity of microhelix charging by a class I tRNA synthetase occurs in the transition state of catalysis Biochemistry  1996 35:608-615  DOI:10.1021/bi9520904  PMID:8555234
    • Ribas de Pouplana, L., Auld, D. S., Kim, S. H., Schimmel, P. A mechanism for reducing entropic cost of induced fit in protein-RNA recognition Biochemistry  1996 35:8095-8102  DOI:10.1021/bi960256a  PMID:8679560
    • Schimmel, P. A two-way street between the university and the biotechnology enterprise Journal of NIH Research  1996 8:41-43
    • Gale, A. J., Schimmel, P. Affinity coelectrophoresis for dissecting protein-RNA domain-domain interactions in a tRNA synthetase system Pharmaceutica Acta Helvetiae  1996 71:45-50  DOI:10.1016/0031-6865(95)00046-1  PMID:8786999
    • Ribas de Pouplana, L., Frugier, M., Quinn, C. L., Schimmel, P. Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria Proceedings of the National Academy of Sciences of the United States of America  1996 93:166-170  DOI:10.1073/pnas.93.1.166  PMID:8552597  PMCID:PMC40199
    • Buechter, D. D., Schimmel, P. Minor groove recognition of the critical acceptor helix base pair by an appended module of a class II tRNA synthetase Biochemistry  1995 34:6014-6019  DOI:10.1021/bi00018a002  PMID:7742303
    • Quinn, C. L., Tao, N. J., Schimmel, P. Species-specific microhelix aminoacylation by a eukaryotic pathogen tRNA synthetase dependent on a single base pair Biochemistry  1995 34:12489-12495  DOI:10.1021/bi00039a001  PMID:7547995
    • Schmidt, E., Schimmel, P. Residues in a class I tRNA synthetase which determine selectivity of amino acid recognition in the context of tRNA Biochemistry  1995 34:11204-11210  DOI:10.1021/bi00035a028  PMID:7669778
    • Schimmel, P., Ripmaster, T. Modular design of components of the operational RNA code for alanine in evolution Trends in Biochemical Sciences  1995 20:333-334  DOI:10.1016/s0968-0004(00)89067-2  PMID:7482695
    • Shiba, K., Ripmaster, T., Suzuki, N., Nichols, R., Plotz, P., Noda, T., Schimmel, P. Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition Biochemistry  1995 34:10340-10349  DOI:10.1021/bi00033a004  PMID:7654687
    • Hipps, D., Schimmel, P. Cell growth inhibition by sequence-specific RNA minihelices EMBO Journal  1995 14:4050-4055  PMID:7664744  PMCID:PMC394483
    • Kirkpatrick, C. R., Schimmel, P. Detection of leucine-independent DNA site occupancy of the yeast Leu3p transcriptional activator in vivo Molecular and Cellular Biology  1995 15:4021-4030  PMID:7623798  PMCID:PMC230641
    • Gale, A. J., Schimmel, P. Isolated RNA binding domain of a class I tRNA synthetase Biochemistry  1995 34:8896-8903  DOI:10.1021/bi00027a042  PMID:7612631
    • Schimmel, P., Ribas de Pouplana, L. Transfer RNA: from minihelix to genetic code Cell  1995 81:983-986  DOI:10.1016/s0092-8674(05)80002-9  PMID:7600584
    • Hipps, D., Shiba, K., Henderson, B., Schimmel, P. Operational RNA code for amino acids: species-specific aminoacylation of minihelices switched by a single nucleotide Proceedings of the National Academy of Sciences of the United States of America  1995 92:5550-5552  DOI:10.1073/pnas.92.12.5550  PMID:7539919  PMCID:PMC41733
    • Ripmaster, T. L., Shiba, K., Schimmel, P. Wide cross-species aminoacyl-tRNA synthetase replacement in vivo: yeast cytoplasmic alanine enzyme replaced by human polymyositis serum antigen Proceedings of the National Academy of Sciences of the United States of America  1995 92:4932-4936  DOI:10.1073/pnas.92.11.4932  PMID:7761427  PMCID:PMC41821
    • Schimmel, P. An operational RNA code for amino acids and variations in critical nucleotide sequences in evolution Journal of Molecular Evolution  1995 40:531-536  PMID:7783226
    • Auld, D. S., Schimmel, P. Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptide Science  1995 267:1994-1996  DOI:10.1126/science.7701322  PMID:7701322
    • Musier-Forsyth, K., Shi, J. P., Henderson, B., Bald, R., Furste, J. P., Erdmann, V. A., Schimmel, P. Base-analog-induced aminoacylation of an RNA helix by a tRNA synthetase Journal of the American Chemical Society  1995 117:7253-7254  DOI:10.1021/ja00132a029
    • Schimmel, P., Schmidt, E. Making connections: RNA-dependent amino acid recognition Trends in Biochemical Sciences  1995 20:1-2  DOI:10.1016/s0968-0004(00)88937-9  PMID:7878729
    • Shiba, K., Schimmel, P., Motegi, H., Noda, T. Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation Journal of Biological Chemistry  1994 269:30049-30055  PMID:7962006
    • Schimmel, P., Henderson, B. Possible role of aminoacyl-RNA complexes in noncoded peptide synthesis and origin of coded synthesis Proceedings of the National Academy of Sciences of the United States of America  1994 91:11283-11286  DOI:10.1073/pnas.91.24.11283  PMID:7972050  PMCID:PMC45215
    • Davis, M. W., Buechter, D. D., Schimmel, P. Functional dissection of a predicted class-defining motif in a class II tRNA synthetase of unknown structure Biochemistry  1994 33:9904-9911  DOI:10.1021/bi00199a012  PMID:8060998
    • Landro, J. A., Schimmel, P. Zinc-dependent cell growth conferred by mutant tRNA synthetase Journal of Biological Chemistry  1994 269:20217-20220  PMID:8051111
    • Shiba, K., Suzuki, N., Shigesada, K., Namba, Y., Schimmel, P., Noda, T. Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit Proceedings of the National Academy of Sciences of the United States of America  1994 91:7435-7439  DOI:10.1073/pnas.91.16.7435  PMID:8052601  PMCID:PMC44415
    • Schimmel, P. Areas of specialization of graduate research training grants may miss the big picture Protein Science  1994 3:995-996  DOI:10.1002/pro.5560030701  PMCID:PMC2142909
    • Shi, J. P., Musier-Forsyth, K., Schimmel, P. 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  1994 33:5312-5318  DOI:10.1021/bi00183a039  PMID:8172905
    • Schmidt, E., Schimmel, P. Mutational isolation of a sieve for editing in a transfer RNA synthetase Science  1994 264:265-267  DOI:10.1126/science.8146659  PMID:8146659
    • Musier-Forsyth, K., Schimmel, P. Acceptor helix interactions in a class II tRNA synthetase: photoaffinity cross-linking of an RNA miniduplex substrate Biochemistry  1994 33:773-779  DOI:10.1021/bi00169a019  PMID:8292605
    • Kim, S. H., Ribas de Pouplana, L., Schimmel, P. An RNA binding site in a tRNA synthetase with a reduced set of amino acids Biochemistry  1994 33:11040-11045  DOI:10.1021/bi00202a025  PMID:7522052
    • Schimmel, P. The research university in the 21st century Chimica Oggi  1994 12:9-10
    • Landro, J. A., Schmidt, E., Schimmel, P., Tierney, D. L., Pennerhahn, J. E. 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  1994 33:14213-14220  DOI:10.1021/bi00251a033  PMID:7947832
    • Frugier, M., Florentz, C., Schimmel, P., Giege, R. Triple aminoacylation specificity of a chimerized transfer RNA Biochemistry  1993 32:14053-14061  DOI:10.1021/bi00213a039  PMID:8268184
    • Schimmel, P., Landro, J. A., Schmidt, E. Evidence for distinct locations for metal binding sites in two closely related class I tRNA synthetases Journal of Biomolecular Structure & Dynamics  1993 11:571-581  PMID:8129874
    • Kim, S., Ribas de Pouplana, L., Schimmel, P. Diversified sequences of peptide epitope for same-RNA recognition Proceedings of the National Academy of Sciences of the United States of America  1993 90:10046-10050  DOI:10.1073/pnas.90.21.10046  PMID:7694278  PMCID:PMC47710
    • Schimmel, P. Functional analysis suggests unexpected role for conserved active-site residue in enzyme of known structure Proceedings of the National Academy of Sciences of the United States of America  1993 90:9235-9236  DOI:10.1073/pnas.90.20.9235  PMID:8415683  PMCID:PMC47541
    • Schimmel, P., Giege, R., Moras, D., Yokoyama, S. An operational RNA code for amino acids and possible relationship to genetic code Proceedings of the National Academy of Sciences of the United States of America  1993 90:8763-8768  DOI:10.1073/pnas.90.19.8763  PMID:7692438  PMCID:PMC47440
    • Schimmel, P. Perception of an academic welfare state Protein Science  1993 2:1549-1550  DOI:10.1002/pro.5560021001  PMCID:PMC2142272
    • Landro, J. A., Schimmel, P. Noncovalent protein assembly Current Opinion in Structural Biology  1993 3:549-554  DOI:10.1016/0959-440x(93)90082-v
    • Buechter, D. D., Schimmel, P. Dissection of a class II tRNA synthetase: determinants for minihelix recognition are tightly associated with domain for amino acid activation Biochemistry  1993 32:5267-5272  DOI:10.1021/bi00070a039  PMID:8494904
    • Martinis, S. A., Schimmel, P. Microhelix aminoacylation by a class I tRNA synthetase. Non-conserved base pairs required for specificity Journal of Biological Chemistry  1993 268:6069-6072  PMID:7681057
    • Landro, J. A., Schimmel, P. Metal-binding site in a class I tRNA synthetase localized to a cysteine cluster inserted into nucleotide-binding fold Proceedings of the National Academy of Sciences of the United States of America  1993 90:2261-2265  DOI:10.1073/pnas.90.6.2261  PMID:8460131  PMCID:PMC46066
    • Ludmerer, S. W., Wright, D. J., Schimmel, P. Purification of glutamine tRNA synthetase from Saccharomyces cerevisiae. A monomeric aminoacyl-tRNA synthetase with a large and dispensable NH2-terminal domain Journal of Biological Chemistry  1993 268:5519-5523  PMID:8449914
    • Schimmel, P. GTP hydrolysis in protein synthesis: two for Tu? Science  1993 259:1264-1265  DOI:10.1126/science.8446896  PMID:8446896
    • Schimmel, P. Cost of failure to project impact of protein science on human health and economy Protein Science  1993 2:139-140  DOI:10.1002/pro.5560020201  PMID:8443594  PMCID:PMC2142341
    • Wright, D. J., Martinis, S. A., Jahn, M., Soll, D., Schimmel, P. Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase Biochimie  1993 75:1041-1049  DOI:10.1016/0300-9084(93)90003-b  PMID:8199240
    • Buechter, D. D., Schimmel, P. Aminoacylation of RNA minihelices: implications for tRNA synthetase structural design and evolution Critical Reviews in Biochemistry and Molecular Biology  1993 28:309-322  DOI:10.3109/10409239309078438  PMID:7691478
    • Musier-Forsyth, K., Schimmel, P. Aminoacylation of RNA oligonucleotides: minimalist structures and origin of specificity FASEB Journal  1993 7:282-289  PMID:7680012
    • Kim, S., Landro, J. A., Gale, A. J., Schimmel, P. C-terminal peptide appendix in a class I tRNA synthetase needed for acceptor-helix contacts and microhelix aminoacylation Biochemistry  1993 32:13026-13031  DOI:10.1021/bi00211a011  PMID:8241156
    • Schmidt, E., Schimmel, P. Dominant lethality by expression of a catalytically inactive class I tRNA synthetase Proceedings of the National Academy of Sciences of the United States of America  1993 90:6919-6923  DOI:10.1073/pnas.90.15.6919  PMID:8346197  PMCID:PMC47046
    • Ribas de Pouplana, L., Buechter, D. D., Davis, M. W., Schimmel, P. Idiographic representation of conserved domain of a class II tRNA synthetase of unknown structure Protein Science  1993 2:2259-2262  DOI:10.1002/pro.5560021225  PMID:8298469  PMCID:PMC2142315
    • Schmidt, E., Schimmel, P. Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase Proceedings of the National Academy of Sciences of the United States of America  1993 90:6919-6923  DOI:10.1073/pnas.90.15.6919  PMID:6309809
    • Shiba, K., Schimmel, P. Tripartite functional assembly of a large class I aminoacyl tRNA synthetase Journal of Biological Chemistry  1992 267:22703-22706  PMID:1429621
    • Hou, Y. M., Schimmel, P. Functional compensation of a recognition-defective transfer RNA by a distal base pair substitution Biochemistry  1992 31:10310-10314  DOI:10.1021/bi00157a019  PMID:1420150
    • Shepard, A., Shiba, K., Schimmel, P. RNA binding determinant in some class I tRNA synthetases identified by alignment-guided mutagenesis Proceedings of the National Academy of Sciences of the United States of America  1992 89:9964-9968  DOI:10.1073/pnas.89.20.9964  PMID:1329109  PMCID:PMC50254
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    • Shi, J. P., Martinis, S. A., Schimmel, P. RNA tetraloops as minimalist substrates for aminoacylation Biochemistry  1992 31:4931-4936  DOI:10.1021/bi00136a002  PMID:1599917
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    • Miller, W. T., Schimmel, P. A metal-binding motif implicated in RNA recognition by an aminoacyl-tRNA synthetase and by a retroviral gene product Molecular Microbiology  1992 6:1259-1262  DOI:10.1111/j.1365-2958.1992.tb00846.x  PMID:1379318
    • Burbaum, J. J., Schimmel, P. Amino acid binding by the class I aminoacyl-tRNA synthetases: role for a conserved proline in the signature sequence Protein Science  1992 1:575-581  DOI:10.1002/pro.5560010503  PMID:1304356  PMCID:PMC2142228
    • Miller, W. T., Schimmel, P. A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition Proceedings of the National Academy of Sciences of the United States of America  1992 89:2032-2035  DOI:10.1073/pnas.89.6.2032  PMID:1549561  PMCID:PMC48590
    • Shiba, K., Schimmel, P. Functional assembly of a randomly cleaved protein Proceedings of the National Academy of Sciences of the United States of America  1992 89:1880-1884  DOI:10.1073/pnas.89.5.1880  PMID:1542687  PMCID:PMC48557
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    • Francklyn, C., Shi, J. P., Schimmel, P. Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices Science  1992 255:1121-1125  DOI:10.1126/science.1546312  PMID:1546312
    • Martinis, S. A., Schimmel, P. Enzymatic aminoacylation of sequence-specific RNA minihelices and hybrid duplexes with methionine Proceedings of the National Academy of Sciences of the United States of America  1992 89:65-69  DOI:10.1073/pnas.89.1.65  PMID:1729719
    • Musier-Forsyth, K., Schimmel, P. Functional contacts of a transfer RNA synthetase with 2'-hydroxyl groups in the RNA minor groove Nature  1992 357:513-515  DOI:10.1038/357513a0  PMID:1608452
    • Schimmel, P., Shepard, A., Shiba, K. Intron locations and functional deletions in relation to the design and evolution of a subgroup of class I tRNA synthetases Protein Science  1992 1:1387-1391  DOI:10.1002/pro.5560011018  PMID:1303756  PMCID:PMC2142098
    • Schimmel, P. Mutant enzymes and dissected tRNAs that elucidate motifs for protein-RNA recognition Current Opinion in Structural Biology  1991 1:811-816  DOI:10.1016/0959-440X(91)90183-T
    • Burbaum, J. J., Schimmel, P. Structural relationships and the classification of aminoacyl-tRNA synthetases Journal of Biological Chemistry  1991 266:16965-16968  PMID:1894595
    • Miller, W. T., Hill, K. A. W., Schimmel, P. Evidence for a "cysteine-histidine box" metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase Biochemistry  1991 30:6970-6976  DOI:10.1021/bi00242a023  PMID:1712632
    • Yi, T. M., Walsh, K., Schimmel, P. Rabbit muscle creatine kinase: genomic cloning, sequencing, and analysis of upstream sequences important for expression in myocytes Nucleic Acids Research  1991 19:3027-3033  DOI:10.1093/nar/19.11.3027  PMID:2057360  PMCID:PMC328266
    • Trezeguet, V., Edwards, H., Schimmel, P. A single base pair dominates over the novel identity of an Escherichia coli tyrosine tRNA in Saccharomyces cerevisiae Molecular and Cellular Biology  1991 11:2744-2751  PMID:2017176  PMCID:PMC360044
    • Schimmel, P. RNA minihelices and the decoding of genetic information FASEB Journal  1991 5:2180-2187  PMID:2022314
    • Shi, J. P., Schimmel, P. Aminoacylation of alanine minihelices. "Discriminator" base modulates transition state of single turnover reaction Journal of Biological Chemistry  1991 266:2705-2708  PMID:1704363
    • Edwards, H., Trezeguet, V., Schimmel, P. An Escherichia coli tyrosine transfer RNA is a leucine-specific transfer RNA in the yeast Saccharomyces cerevisiae Proceedings of the National Academy of Sciences of the United States of America  1991 88:1153-1156  DOI:10.1073/pnas.88.4.1153  PMID:1996316  PMCID:PMC50975
    • Hou, Y. M., Shiba, K., Mottes, C., Schimmel, P. Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase Proceedings of the National Academy of Sciences of the United States of America  1991 88:976-980  DOI:10.1073/pnas.88.3.976  PMID:1992490  PMCID:PMC50937
    • Burbaum, J. J., Schimmel, P. Assembly of a class I tRNA synthetase from products of an artificially split gene Biochemistry  1991 30:319-324  DOI:10.1021/bi00216a002  PMID:1988033
    • Schimmel, P. Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code Trends in Biochemical Sciences  1991 16:1-3  DOI:10.1016/0968-0004(91)90002-d  PMID:2053131
    • Musier-Forsyth, K., Scaringe, S., Usman, N., Schimmel, P. Enzymatic aminoacylation of single-stranded RNA with an RNA cofactor Proceedings of the National Academy of Sciences of the United States of America  1991 88:209-213  DOI:10.1073/pnas.88.1.209  PMID:1986368  PMCID:PMC50779
    • Miller, W. T., Hou, Y. M., Schimmel, P. Mutant aminoacyl-tRNA synthetase that compensates for a mutation in the major identity determinant of its tRNA Biochemistry  1991 30:2635-2641  DOI:10.1021/bi00224a011  PMID:2001352
    • Musier-Forsyth, K., Usman, N., Scaringe, S., Doudna, J., Green, R., Schimmel, P. Specificity for aminoacylation of an RNA helix: an unpaired, exocyclic amino group in the minor groove Science  1991 253:784-786  DOI:10.1126/science.1876835  PMID:1876835
    • Schimmel, P., Burbaum, J. J. Transfer RNA with double identity for in vitro kinetic modeling of transfer RNA identity in vivo Methods in Enzymology  1991 203:485-500  DOI:10.1016/0076-6879(91)03027-e  PMID:1762569
    • Francklyn, C., Schimmel, P. Enzymatic aminoacylation of an eight-base-pair microhelix with histidine Proceedings of the National Academy of Sciences of the United States of America  1990 87:8655-8659  DOI:10.1073/pnas.87.21.8655  PMID:2236077  PMCID:PMC55016
    • Francklyn, C. S., Schimmel, P. Synthetic RNA molecules as substrates for enzymes that act on tRNAs and tRNA-like molecules Chemical Reviews  1990 90:1327-1342  DOI:10.1021/cr00105a013
    • Schimmel, P. Hazards and their exploitation in the applications of molecular biology to structure-function relationships Biochemistry  1990 29:9495-9502  DOI:10.1021/bi00493a001  PMID:2271597
    • Park, S. J., Miller, W. T., Schimmel, P. Synthetic peptide model of an essential region of an aminoacyl-tRNA synthetase Biochemistry  1990 29:9212-9218  DOI:10.1021/bi00491a015  PMID:2271589
    • Chng, J. L. C., Shoemaker, D. L., Schimmel, P., Holmes, E. W. Reversal of creatine kinase translational repression by 3' untranslated sequences Science  1990 248:1003-1006  DOI:10.1126/science.2343304  PMID:2343304
    • Shi, J. P., Francklyn, C., Hill, K., Schimmel, P. A nucleotide that enhances the charging of RNA minihelix sequence variants with alanine Biochemistry  1990 29:3621-3626  DOI:10.1021/bi00467a005  PMID:1692733
    • Edwards, H., Schimmel, P. A bacterial amber suppressor in Saccharomyces cerevisiae is selectively recognized by a bacterial aminoacyl-tRNA synthetase Molecular and Cellular Biology  1990 10:1633-1641  PMID:1690848  PMCID:PMC362268
    • Toth, M. J., Schimmel, P. A mutation in the small (alpha) subunit of glycyl-tRNA synthetase affects amino acid activation and subunit association parameters Journal of Biological Chemistry  1990 265:1005-1009  PMID:2295596
    • Toth, M. J., Schimmel, P. Deletions in the large (beta) subunit of a hetero-oligomeric aminoacyl-tRNA synthetase Journal of Biological Chemistry  1990 265:1000-1004  PMID:2404005
    • Schimmel, P. Alanine transfer RNA synthetase: structure-function relationships and molecular recognition of transfer RNA Advances in Enzymology and Related Areas of Molecular Biology  1990 63:233-270  PMID:2407064
    • Kaddarah-Daouk, R., Lillie, J. W., Daouk, G. H., Green, M. R., Kingston, R., Schimmel, P. Induction of a cellular enzyme for energy metabolism by transforming domains of adenovirus E1a Molecular and Cellular Biology  1990 10:1476-1483  PMID:2138706  PMCID:PMC362250
    • Hill, K., Schimmel, P. The dissection and engineering of sites that affect the activity of an enzyme of unknown structure Biotechnology  1990 14:65-79  PMID:2183901
    • Burbaum, J. J., Starzyk, R. M., Schimmel, P. Understanding structural relationships in proteins of unsolved three-dimensional structure Proteins-Structure Function and Genetics  1990 7:99-111  DOI:10.1002/prot.340070202  PMID:2183216
    • Chng, J. L. C., Mulligan, R. C., Schimmel, P., Holmes, E. W. Antisense RNA complementary to 3' coding and noncoding sequences of creatine kinase is a potent inhibitor of translation in vivo Proceedings of the National Academy of Sciences of the United States of America  1989 86:10006-10010  DOI:10.1073/pnas.86.24.10006  PMID:2481308  PMCID:PMC298631
    • Starzyk, R. M., Burbaum, J. J., Schimmel, P. Insertion of new sequences into the catalytic domain of an enzyme Biochemistry  1989 28:8479-8484  DOI:10.1021/bi00447a031  PMID:2690943
    • Starzyk, R. M., Schimmel, P. Construction of intra-domain chimeras of aminoacyl-tRNA synthetases Journal of Biomolecular Structure & Dynamics  1989 7:225-234  PMID:2690866
    • Friden, P., Reynolds, C., Schimmel, P. A large internal deletion converts yeast LEU3 to a constitutive transcriptional activator Molecular and Cellular Biology  1989 9:4056-4060  PMID:2674686  PMCID:PMC362471
    • Hou, Y. M., Schimmel, P. Evidence that a major determinant for the identity of a transfer RNA is conserved in evolution Biochemistry  1989 28:6800-6804  DOI:10.1021/bi00443a003  PMID:2684266
    • Schimmel, P. RNA pseudoknots that interact with components of the translation apparatus Cell  1989 58:9-12  DOI:10.1016/0092-8674(89)90395-4  PMID:2473840
    • Schimmel, P. Hazards of deducing enzyme structure-activity relationships on the basis of chemical applications of molecular biology Accounts of Chemical Research  1989 22:232-233  DOI:10.1021/ar00163a001
    • Hou, Y. M., Francklyn, C., Schimmel, P. Molecular dissection of a transfer RNA and the basis for its identity Trends in Biochemical Sciences  1989 14:233-237  DOI:10.1016/0968-0004(89)90033-9  PMID:2669241
    • Schimmel, P. Parameters for the molecular recognition of transfer RNAs Biochemistry  1989 28:2747-2759  DOI:10.1021/bi00433a001  PMID:2663057
    • Park, S. J., Hou, Y. M., Schimmel, P. A single base pair affects binding and catalytic parameters in the molecular recognition of a transfer RNA Biochemistry  1989 28:2740-2746  DOI:10.1021/bi00432a056  PMID:2659081
    • Hill, K., Schimmel, P. Evidence that the 3' end of a tRNA binds to a site in the adenylate synthesis domain of an aminoacyl-tRNA synthetase Biochemistry  1989 28:2577-2586  DOI:10.1021/bi00432a035  PMID:2543446
    • Francklyn, C., Schimmel, P. Aminoacylation of RNA minihelices with alanine Nature  1989 337:478-481  DOI:10.1038/337478a0  PMID:2915692
    • Hou, Y. M., Schimmel, P. Modeling with in vitro kinetic parameters for the elaboration of transfer RNA identity in vivo Biochemistry  1989 28:4942-4947  DOI:10.1021/bi00438a005  PMID:2548595
    • Regan, L., Buxbaum, L., Hill, K., Schimmel, P. Rationale for engineering an enzyme by introducing a mutation that compensates for a deletion Journal of Biological Chemistry  1988 263:18598-18600  PMID:3198590
    • Park, S. J., Schimmel, P. Evidence for interaction of an aminoacyl transfer RNA synthetase with a region important for the identity of its cognate transfer RNA Journal of Biological Chemistry  1988 263:16527-16530  PMID:3053691
    • Frederick, C. A., Wang, A. H. J., Rich, A., Regan, L., Schimmel, P. Crystallization of a small fragment of an aminoacyl tRNA synthetase Journal of Molecular Biology  1988 203:521-522  DOI:10.1016/0022-2836(88)90019-8  PMID:3058989
    • Schimmel, P. Who will watch the watchdogs? Cell  1988 54:596  DOI:10.1016/s0092-8674(88)80002-3  PMID:3409318
    • Friden, P., Schimmel, P. LEU3 of Saccharomyces cerevisiae activates multiple genes for branched-chain amino acid biosynthesis by binding to a common decanucleotide core sequence Molecular and Cellular Biology  1988 8:2690-2697  PMID:3043190  PMCID:PMC363479
    • Toth, M. J., Murgola, E. J., Schimmel, P. Evidence for a unique first position codon-anticodon mismatch in vivo Journal of Molecular Biology  1988 201:451-454  DOI:10.1016/0022-2836(88)90152-0  PMID:3262166
    • Hou, Y. M., Schimmel, P. A simple structural feature is a major determinant of the identity of a transfer RNA Nature  1988 333:140-145  DOI:10.1038/333140a0  PMID:3285220
    • Drain, P., Schimmel, P. Multiple new genes that determine activity for the first step of leucine biosynthesis in Saccharomyces cerevisiae Genetics  1988 119:13-20  PMID:3294097  PMCID:PMC1203331
    • Clarke, N. D., Lien, D. C., Schimmel, P. Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure Science  1988 240:521-523  DOI:10.1126/science.3282306  PMID:3282306
    • Walsh, K., Schimmel, P. DNA-binding site for two skeletal actin promoter factors is important for expression in muscle cells Molecular and Cellular Biology  1988 8:1800-1802  PMID:3380098  PMCID:PMC363341
    • Daouk, G. H., Kaddarah-Daouk, R., Putney, S., Kingston, R., Schimmel, P. Isolation of a functional human gene for brain creatine kinase Journal of Biological Chemistry  1988 263:2442-2446  PMID:2828370
    • Profy, A. T., Schimmel, P. Complementary use of chemical modification and site-directed mutagenesis to probe structure activity relationships in enzymes Progress in Nucleic Acid Research and Molecular Biology  1988 35:1-26  DOI:10.1016/s0079-6603(08)60608-x  PMID:3065821
    • Schimmel, P. Evolution and future of biotechnology ACS Symposium Series  1988 362:30-35  DOI:10.1021/bk-1988-0362.ch003
    • Schimmel, P. Third thoughts on second code Science News  1988 133:387
    • Edwards, H., Schimmel, P. An E. coli aminoacyl-tRNA synthetase can substitute for yeast mitochondrial enzyme function in vivo Cell  1987 51:643-649  DOI:10.1016/0092-8674(87)90133-4  PMID:3315228
    • Starzyk, R. M., Webster, T. A., Schimmel, P. Evidence for dispensable sequences inserted into a nucleotide fold Science  1987 237:1614-1618  DOI:10.1126/science.3306924  PMID:3306924
    • Friden, P., Schimmel, P. LEU3 of Saccharomyces cerevisiae encodes a factor for control of RNA levels of a group of leucine-specific genes Molecular and Cellular Biology  1987 7:2708-2717  PMID:2823102  PMCID:PMC367887
    • Walsh, K., Schimmel, P. Two nuclear factors compete for the skeletal muscle actin promoter Journal of Biological Chemistry  1987 262:9429-9432  PMID:3036859
    • Regan, L., Bowie, J., Schimmel, P. Polypeptide sequences essential for RNA recognition by an enzyme Science  1987 235:1651-1653  DOI:10.1126/science.2435005  PMID:2435005
    • Schimmel, P. Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs Annual Review of Biochemistry  1987 56:125-158  DOI:10.1146/annurev.biochem.56.1.125  PMID:3304131
    • Ludmerer, S. W., Schimmel, P. Construction and analysis of deletions in the amino-terminal extension of glutamine tRNA synthetase of Saccharomyces cerevisiae Journal of Biological Chemistry  1987 262:10807-10813  PMID:3301842
    • Ludmerer, S. W., Schimmel, P. Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetases Journal of Biological Chemistry  1987 262:10801-10806  PMID:3301841
    • Profy, A. T., Schimmel, P. A sulfhydryl presumed essential is not required for catalysis by an aminoacyl-tRNA synthetase Journal of Biological Chemistry  1986 261:15474-15479  PMID:3536904
    • Toth, M. J., Schimmel, P. Internal structural features of E. coli glycyl-tRNA synthetase examined by subunit polypeptide chain fusions Journal of Biological Chemistry  1986 261:6643-6646  PMID:3009467
    • Regan, L., Dignam, J. D., Schimmel, P. A bacterial and silkworm aminoacyl-tRNA synthetase have a common epitope which maps to the catalytic domain of each Journal of Biological Chemistry  1986 261:5241-5244  PMID:2420799
    • Drain, P., Schimmel, P. Yeast LEU5 is a PET-like gene that is not essential for leucine biosynthesis Molecular and General Genetics  1986 204:397-403  DOI:10.1007/bf00331015  PMID:3020377
    • Ho, C., Jasin, M., Schimmel, P. Amino-acid replacements that compensate for a large polypeptide deletion in an enzyme Science  1985 229:389-393  DOI:10.1126/science.3892692  PMID:3892692
    • Ludmerer, S. W., Schimmel, P. Cloning of GLN4: an essential gene that encodes glutaminyl-tRNA synthetase in Saccharomyces cerevisiae Journal of Bacteriology  1985 163:763-768  PMID:2991203  PMCID:PMC219187
    • Starzyk, R., Schoemaker, H., Schimmel, P. Covalent enzyme-RNA complex: a tRNA modification that prevents a covalent enzyme interaction also prevents aminoacylation Proceedings of the National Academy of Sciences of the United States of America  1985 82:339-342  DOI:10.1073/pnas.82.2.339  PMID:3881761  PMCID:PMC397033
    • Schimmel, P. High priority scores Science  1985 229:706  DOI:10.1126/science.229.4715.706  PMID:17841480
    • Schimmel, P. In biology, neither smaller nor larger is necessarily better Cell  1985 42:1  DOI:10.1016/s0092-8674(85)80090-8  PMID:4016951
    • Freedman, R., Gibson, B., Donovan, D., Biemann, K., Eisenbeis, S., Parker, J., Schimmel, P. Primary structure of histidine-tRNA synthetase and characterization of hisS transcripts Journal of Biological Chemistry  1985 260:10063-10068  PMID:2991272
    • Middleton, T., Herlihy, W. C., Schimmel, P. R., Munro, H. N. Synthesis and purification of oligoribonucleotides using T4 RNA ligase and reverse-phase chromatography Analytical Biochemistry  1985 144:110-117  DOI:10.1016/0003-2697(85)90091-0  PMID:3985307
    • Jasin, M., Regan, L., Schimmel, P. Two mutations in the dispensable part of alanine tRNA synthetase which affect the catalytic activity Journal of Biological Chemistry  1985 260:2226-2230  PMID:3882689
    • Pickering, L., Pang, H., Biemann, K., Munro, H., Schimmel, P. Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences Proceedings of the National Academy of Sciences of the United States of America  1985 82:2310-2314  DOI:10.1073/pnas.82.8.2310  PMID:3857581  PMCID:PMC397547
    • Jasin, M., Schimmel, P. Deletion of an essential gene in Escherichia coli by site-specific recombination with linear DNA fragments Journal of Bacteriology  1984 159:783-786  PMID:6086588  PMCID:PMC215717
    • Jasin, M., Regan, L., Schimmel, P. Dispensable pieces of an aminoacyl tRNA synthetase which activate the catalytic site Cell  1984 36:1089-1095  DOI:10.1016/0092-8674(84)90059-x  PMID:6200234
    • Putney, S., Herlihy, W., Royal, N., Pang, H., Aposhian, H. V., Pickering, L., Belagaje, R., Biemann, K., Page, D., Kuby, S., Schimmel, P. Rabbit muscle creatine phosphokinase. CDNA cloning, primary structure and detection of human homologues Journal of Biological Chemistry  1984 259:14317-14320  PMID:6094551
    • Schimmel, P., Jasin, M., Regan, L. Size polymorphism and the structure of aminoacyl-tRNA synthetases Federation Proceedings  1984 43:2987-2990  PMID:6389183
    • Webster, T., Tsai, H., Kula, M., Mackie, G. A., Schimmel, P. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase Science  1984 226:1315-1317  DOI:10.1126/science.6390679  PMID:6390679
    • Hsu, Y. P., Schimmel, P. Yeast LEU1. Repression of mRNA levels by leucine and relationship of 5'-noncoding region to that of LEU2 Journal of Biological Chemistry  1984 259:3714-3719  PMID:6323436
    • Andreadis, A., Hsu, Y. P., Hermodson, M., Kohlhaw, G., Schimmel, P. Yeast LEU2. Repression of mRNA levels by leucine and primary structure of the gene product Journal of Biological Chemistry  1984 259:8059-8062  PMID:6330094
    • Putney, S. D., Herlihy, W. C., Schimmel, P. A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing Nature  1983 302:718-721  DOI:10.1038/302718a0  PMID:6687628
    • Schimmel, P. R. Book review: Fundamentals of Enzymology by N. C. Price and L. Stevens American Scientist  1983 71:316-317
    • Jasin, M., Regan, L., Schimmel, P. Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase Nature  1983 306:441-447  DOI:10.1038/306441a0  PMID:6358898
    • Webster, T. A., Gibson, B. W., Keng, T., Biemann, K., Schimmel, P. Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase Journal of Biological Chemistry  1983 258:637-641  PMID:6309809
    • Keng, T., Schimmel, P. Synthesis of two polypeptide subunits of an aminoacyl tRNA synthetase as a single polypeptide chain Journal of Biomolecular Structure & Dynamics  1983 1:225-229  DOI:10.1080/07391102.1983.10507436  PMID:6086058
    • Starzyk, R. M., Koontz, S. W., Schimmel, P. A covalent adduct between the uracil ring and the active site of an aminoacyl tRNA synthetase Nature  1982 298:136-140  DOI:10.1038/298136a0  PMID:7045689
    • Keng, T., Webster, T. A., Sauer, R. T., Schimmel, P. Gene for Escherichia coli glycyl-tRNA synthetase has tandem subunit coding regions in the same reading frame Journal of Biological Chemistry  1982 257:12503-12508  PMID:6290471
    • Schimmel, P., Keng, T., Putney, S. Genes for two E. coli aminoacyl tRNA synthetases Developments in Biochemistry  1982 24:49-56
    • Andreadis, A., Hsu, Y. P., Kohlhaw, G. B., Schimmel, P. Nucleotide sequence of yeast LEU2 shows 5'-noncoding region has sequences cognate to leucine Cell  1982 31:319-325  DOI:10.1016/0092-8674(82)90125-8  PMID:6297759
    • Schimmel, P., Putney, S., Starzyk, R. RNA and DNA sequence recognition and structure: function of aminoacyl tRNA synthetases Trends in Biochemical Sciences  1982 7:209-212  DOI:10.1016/0968-0004(82)90092-5
    • Putney, S. D., Benkovic, S. J., Schimmel, P. R. 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 Proceedings of the National Academy of Sciences of the United States of America-Biological Sciences  1981 78:7350-7354  DOI:10.1073/pnas.78.12.7350  PMID:6278470  PMCID:PMC349264
    • Putney, S. D., Schimmel, P. An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription Nature  1981 291:632-635  DOI:10.1038/291632a0  PMID:6264314
    • Putney, S. D., Melendez, D. L., Schimmel, P. R. Cloning, partial sequencing, and in vitro transcription of the gene for alanine tRNA synthetase Journal of Biological Chemistry  1981 256:205-211  PMID:6256345
    • Freedman, R., Schimmel, P. In vitro transcription of the histidine operon. Identification of the his promoter and leader and readthrough transcripts Journal of Biological Chemistry  1981 256:10747-10750  PMID:6270128
    • Putney, S. D., Royal, N. J., Devegvar, H. N., Herlihy, W. C., Biemann, K., Schimmel, P. Primary structure of a large aminoacyl-tRNA synthetase Science  1981 213:1497-1501  DOI:10.1126/science.7025207  PMID:7025207
    • Putney, S. D., Sauer, R. T., Schimmel, P. R. Purification and properties of alanine tRNA synthetase from Escherichia coli. A tetramer of identical subunits Journal of Biological Chemistry  1981 256:198-204  PMID:7005211
    • Schimmel, P. R. Five specific protein-transfer RNA interactions CRC Critical Reviews in Biochemistry  1980 9:207-251  DOI:10.3109/10409238009105435  PMID:6160952
    • Herlihy, W. C., Royal, N. J., Biemann, K., Putney, S. D., Schimmel, P. R. 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 Proceedings of the National Academy of Sciences of the United States of America-Biological Sciences  1980 77:6531-6535  DOI:10.1073/pnas.77.11.6531  PMID:7005898  PMCID:PMC350319
    • Schimmel, P. R., Melendez, D. L., Putney, S. D. Molecular dissection of an enzyme that recognizes transfer RNA Macromolecules  1980 13:716-721  DOI:10.1021/ma60075a044
    • Schimmel, P. R., Redfield, A. G. Transfer RNA in solution: selected topics Annual Review of Biophysics and Bioengineering  1980 9:181-221  DOI:10.1146/annurev.bb.09.060180.001145  PMID:6994589
    • Koontz, S. W., Schimmel, P. R. Aminoacyl-tRNA synthetase-catalyzed cleavage of the glycosidic bond of 5-halogenated uridines Journal of Biological Chemistry  1979 254:12277-12280  PMID:40993
    • Schimmel, P. R., Soll, D. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs Annual Review of Biochemistry  1979 48:601-648  DOI:10.1146/annurev.bi.48.070179.003125  PMID:382994
    • Schimmel, P. R., Schoemaker, H. J. Mapping the structure of specific protein-transfer RNA complexes by a tritium labeling method Methods in Enzymology  1979 59:332-350  DOI:10.1016/0076-6879(79)59095-8  PMID:440081
    • Schimmel, P. R. Recent results on how aminoacyl transfer RNA synthetases recognize specific transfer RNAs Molecular and Cellular Biochemistry  1979 25:3-14  PMID:381892
    • Schimmel, P. R. Understanding the recognition of transfer RNAs by aminoacyl transfer RNA synthetases Advances in Enzymology and Related Areas of Molecular Biology  1979 49:187-222  DOI:10.1002/9780470122945.ch5  PMID:400854
    • Cole, F. X., Schimmel, P. R. Dynamics of tautomerization of formycin Journal of the American Chemical Society  1978 100:3957-3958  DOI:10.1021/ja00480a066
    • Gamble, R. C., Schimmel, P. R. Nanosecond relaxation processes of phospholipid bilayers in transition zone Proceedings of the National Academy of Sciences of the United States of America  1978 75:3011-3014  DOI:10.1073/pnas.75.7.3011  PMID:277906  PMCID:PMC392701
    • Schimmel, P. R. Approaches to understanding the mechanism of specific protein-transfer RNA interactions Accounts of Chemical Research  1977 10:411-418  DOI:10.1021/ar50119a005
    • Yue, V. T., Schimmel, P. R. Direct and specific photochemical cross-linking of adenosine 5'-triphosphate to an aminoacyl-tRNA synthetase Biochemistry  1977 16:4678-4684  DOI:10.1021/bi00640a023  PMID:334247
    • Schoemaker, H. J. P., Schimmel, P. R. Effect of aminoacyl transfer RNA synthetases on H-5 exchange of specific pyrimidines in transfer RNAs Biochemistry  1977 16:5454-5460  DOI:10.1021/bi00644a009  PMID:411506
    • Schoemaker, H. J. P., Schimmel, P. R. Inhibition of an aminoacyl transfer RNA synthetase by a specific trinucleotide derived from the sequence of its cognate transfer RNA Biochemistry  1977 16:5461-5464  DOI:10.1021/bi00644a010  PMID:336087
    • Rich, A., Schimmel, P. R. Introduction to transfer RNA Accounts of Chemical Research  1977 10:385-387  DOI:10.1021/ar50119a001
    • Jekowsky, E., Schimmel, P. R., Miller, D. L. Isolation, characterization and structural implications of a nuclease-digested complex of aminoacyl transfer RNA and Escherichia coli elongation factor Tu Journal of Molecular Biology  1977 114:451-458  DOI:10.1016/0022-2836(77)90262-5  PMID:333117
    • Schimmel, P. R., Budzik, G. P. Photo-cross-linking of protein-nucleic acid complexes Methods in Enzymology  1977 46:168-180  DOI:10.1016/S0076-6879(77)46018-X  PMID:333226
    • Rich, A., Schimmel, P. R. Structural organization of complexes of transfer RNAs with aminoacyl transfer RNA synthetases Nucleic Acids Research  1977 4:1649-1665  DOI:10.1093/nar/4.5.1649  PMID:331261  PMCID:PMC343779
    • Schoemaker, H. J. P., Gamble, R. C., Budzik, G. P., Schimmel, P. R. Comparison of isotope labeling patterns of purines in three specific transfer RNAs Biochemistry  1976 15:2800-2803  DOI:10.1021/bi00658a015  PMID:779830
    • Schimmel, P. R. Equilibrium and kinetic investigations of cooperative interaction of cations with transfer RNA Journal of Polymer Science Part C-Polymer Symposium  1976 387-401
    • Schoemaker, H. J. P., Schimmel, P. R. Isotope labeling of free and aminoacyl transfer RNA synthetase-bound transfer RNA Journal of Biological Chemistry  1976 251:6823-6830  PMID:789377
    • Gamble, R. C., Schoemaker, H. J. P., Jekowsky, E., Schimmel, P. R. Rate of tritium labeling of specific purines in relation to nucleic acid and particularly transfer RNA conformation Biochemistry  1976 15:2791-2799  DOI:10.1021/bi00658a014  PMID:949477
    • Lam, S. S. M., Schimmel, P. R. Equilibrium measurements of cognate and noncognate interactions between aminoacyl transfer RNA synthetases and transfer RNA Biochemistry  1975 14:2775-2780  DOI:10.1021/bi00683a034  PMID:238575
    • Schreier, A. A., Schimmel, P. R. Interaction of polyamines with fragments and whole molecules of yeast phenylalanine-specific transfer RNA Journal of Molecular Biology  1975 93:323-329  DOI:10.1016/0022-2836(75)90136-9  PMID:1097707
    • Dickson, L. A., Schimmel, P. R. Structure of transfer RNA-aminoacyl transfer RNA synthetase complexes investigated by nuclease digestion Archives of Biochemistry and Biophysics  1975 167:638-645  DOI:10.1016/0003-9861(75)90507-x  PMID:1092269
    • Schoemaker, H. J. P., Budzik, G. P., Giege, R., Schimmel, P. R. Three photo-cross-linked complexes of yeast phenylalanine specific transfer ribonucleic acid with aminoacyl transfer ribonucleic acid synthetases Journal of Biological Chemistry  1975 250:4440-4444  PMID:237899
    • Budzik, G. P., Lam, S. S. M., Schoemaker, H. J. P., Schimmel, P. R. Two photo-cross-linked complexes of isoleucine specific transfer ribonucleic acid with aminoacyl transfer ribonucleic acid synthetases Journal of Biological Chemistry  1975 250:4433-4439  PMID:1095570
    • Lynch, D. C., Schimmel, P. R. Cooperative binding of magnesium to transfer ribonucleic acid studied by a fluorescent probe Biochemistry  1974 13:1841-1852  DOI:10.1021/bi00706a012  PMID:4601164
    • Lynch, D. C., Schimmel, P. R. Effects of abnormal base ionizations on Mg(++) binding to transfer ribonucleic acid as studied by a fluorescent probe Biochemistry  1974 13:1852-1861  DOI:10.1021/bi00706a013  PMID:4209166
    • Schreier, A. A., Schimmel, P. R. Interaction of manganese with fragments, complementary fragment recombinations, and whole molecules of yeast phenylalanine specific transfer RNA Journal of Molecular Biology  1974 86:601-620  DOI:10.1016/0022-2836(74)90183-1  PMID:4604622
    • Rhodes, L. M., Schimmel, P. R. Intermolecular proton-transfer reaction between base and phosphate moieties of mononucleotides in solution Journal of the American Chemical Society  1974 96:2609-2611  DOI:10.1021/ja00815a048  PMID:4833713
    • Schoemaker, H. J. P., Schimmel, P. R. Photo-induced joining of a transfer RNA with its cognate aminoacyl-transfer RNA synthetase Journal of Molecular Biology  1974 84:503-513  DOI:10.1016/0022-2836(74)90112-0  PMID:4840999
    • Schwartz, A. M., Schimmel, P. R. Relaxation spectra of the iron spin transition in methemoglobin Journal of Molecular Biology  1974 89:505-510  DOI:10.1016/0022-2836(74)90479-3  PMID:4374554
    • Gamble, R. C., Schimmel, P. R. Transfer RNA conformation in solution investigated by isotope labeling Proceedings of the National Academy of Sciences of the United States of America  1974 71:1356-1360  PMID:4598301  PMCID:PMC388227
    • Schimmel, P. R., Lynch, D. C. Interactions and conformational transitions of a transfer RNA monitored by a covalently attached fluorescent probe Polymer Preprints  1973 14:143-148
    • Schimmel, P. R. Mechanism of an aminoacyl transfer ribonucleic acid synthetase Accounts of Chemical Research  1973 6:299-305  DOI:10.1021/ar50069a003
    • Eldred, E. W., Schimmel, P. R. Release of aminoacyl transfer ribonucleic acid from transfer ribonucleic acid synthetase studied by rapid molecular sieve chromatography Analytical Biochemistry  1973 51:229-239  DOI:10.1016/0003-2697(73)90470-3  PMID:4347232
    • Schimmel, P. R., Uhlenbeck, O. C., Lewis, J. B., Dickson, L. A., Eldred, E. W., Schreier, A. A. Binding of complementary oligonucleotides to free and aminoacyl transfer ribonucleic acid synthetase bound transfer ribonucleic acid Biochemistry  1972 11:642-646  DOI:10.1021/bi00754a028  PMID:4334910
    • Lo, H. H., Schimmel, P. R. Effect of 2-3-diphosphoglycerate and ATP on ethyl isocyanide binding to human hemoglobin Biochimica et Biophysica Acta  1972 263:304-308  DOI:10.1016/0005-2795(72)90083-9  PMID:5031159
    • McNeil, M. R., Schimmel, P. R. 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 Archives of Biochemistry and Biophysics  1972 152:175-179  DOI:10.1016/0003-9861(72)90205-6  PMID:4342105
    • Eldred, E. W., Schimmel, P. R. Investigation of the transfer of amino acid from a transfer ribonucleic acid synthetase-aminoacyl adenylate complex to transfer ribonucleic acid Biochemistry  1972 11:17-23  DOI:10.1021/bi00751a004  PMID:4550554
    • Eldred, E. W., Schimmel, P. R. Rapid deacylation by isoleucyl transfer ribonucleic acid synthetase of isoleucine-specific transfer ribonucleic acid aminoacylated with valine Journal of Biological Chemistry  1972 247:2961-2964  PMID:4554364
    • Schreier, A. A., Schimmel, P. R. Transfer ribonucleic acid synthetase catalyzed deacylation of aminoacyl transfer ribonucleic acid in the absence of adenosine monophosphate and pyrophosphate Biochemistry  1972 11:1582-1589  DOI:10.1021/bi00759a006  PMID:4337554
    • Rhodes, L. M., Schimmel, P. R. Nanosecond relaxation processes in aqueous mononucleoside solutions Biochemistry  1971 10:4423-4433  PMID:5316837
    • Schimmel, P. R. On the calculation of chemical relaxation amplitudes Journal of Chemical Physics  1971 54:4136-4137  DOI:10.1063/1.1675487
    • Schimmel, P. R., Leung, J. G. M. Dipole moments of nonzwitterionic polypeptide chains Macromolecules  1970 3:704-705  DOI:10.1021/ma60017a617
    • Cole, F. X., Schimmel, P. R. Isoleucyl transfer ribonucleic acid synthetase. The role of magnesium in amino acid activation Biochemistry  1970 9:3143-3148  DOI:10.1021/bi00818a005  PMID:4321368
    • Cole, F. X., Schimmel, P. R. On the rate law and mechanism of the adenosine triphosphate-pyrophosphate isotope exchange reaction of amino acyl transfer ribonucleic acid synthetases Biochemistry  1970 9:480-489  DOI:10.1021/bi00805a005  PMID:4313472
    • Lo, H. H., Schimmel, P. R. Interaction of human hemoglobin with adenine nucleotides Journal of Biological Chemistry  1969 244:5084-5086  PMID:5824580
    • Kowalski, C. J., Schimmel, P. R. Interaction of lysozyme with alpha-N-acetyl-D-glucosamine Journal of Biological Chemistry  1969 244:3643-3646  PMID:5815830
    • Schimmel, P. R., Flory, P. J. Conformational energies and configurational statistics of copolypeptides containing L-proline Journal of Molecular Biology  1968 34:105-120  DOI:10.1016/0022-2836(68)90237-4  PMID:5760450
    • Chipman, D. M., Schimmel, P. R. Dynamics of lysozyme-saccharide interactions Journal of Biological Chemistry  1968 243:3771-3774  PMID:5658551
    • Hammes, G. G., Schimmel, P. R. An investigation of water-urea and water-urea-polyethylene glycol interactions Journal of the American Chemical Society  1967 89:442-446  DOI:10.1021/ja00978a050
    • Brant, D. A., Schimmel, P. R. Analysis of the skeletal configuration of crystalline hen egg-white lysozyme Proceedings of the National Academy of Sciences of the United States of America  1967 58:428-435  DOI:10.1073/pnas.58.2.428  PMID:5233451  PMCID:PMC335652
    • Schimmel, P. R., Flory, P. J. Conformational energy and configurational statistics of poly-L-proline Proceedings of the National Academy of Sciences of the United States of America  1967 58:52-59  DOI:10.1073/pnas.58.1.52  PMID:5231619  PMCID:PMC335595
    • Flory, P. J., Schimmel, P. R. Dipole moments in relation to configuration of polypeptide chains Journal of the American Chemical Society  1967 89:6807-6813  DOI:10.1021/ja01002a001  PMID:6064350
    • Hammes, G. G., Schimmel, P. R. Relaxation spectra of enzymatic reactions Journal of Physical Chemistry  1967 71:917-923  DOI:10.1021/j100863a023  PMID:6045206
    • Hammes, G. G., Schimmel, P. R. Chemical relaxation spectra: calculation of relaxation times for complex mechanisms Journal of Physical Chemistry  1966 70:2319-2324  DOI:10.1021/j100879a039
    • Fasella, P., Hammes, G. G., Schimmel, P. R. A Sephadex dialysis method of determining small molecule-macromolecule binding constants Biochimica et Biophysica Acta  1965 103:708-710  DOI:10.1016/0005-2787(65)90094-8  PMID:5859855
    • Hammes, G. G., Schimmel, P. R. Equilibrium measurements of the binding of cytidine 3'-phosphate to ribonuclease Journal of the American Chemical Society  1965 87:4665-4669  DOI:10.1021/ja00949a001  PMID:5844451
    • Cathou, R. E., Hammes, G. G., Schimmel, P. R. Optical rotatory dispersion of ribonuclease and ribonuclease-nucleotide complexes Biochemistry  1965 4:2687-2690  DOI:10.1021/bi00888a018  PMID:4286548

featured in

  • Inside the Second Genetic Code: An Interview with Paul Schimmel  Newsletter
  • The Scripps Research Institute Recruits Prominent Scientists to Join its Ranks  News Release
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Research

research overview

  • Decoding Genetic Information In Translation

    The genetic code was established over two billion years ago and became universally adopted by all living organisms. The rules of the code--which relate specific nucleotide triplets to specific amino acids--are established by aminoacylation reactions catalyzed by aminoacyl tRNA synthetases. In these reactions, an amino acid is associated with a specific nucleotide triplet of the genetic code, by virtue of being linked to a specific tRNA that harbors the anticodon triplet cognate to the amino acid. Because of their central role in establishing the rules of the code, the tRNAs are thought to have arisen quite early, perhaps in the context of an RNA world. The synthetases may have been amongst the earliest proteins to appear, perhaps replacing ribozymes that catalyzed the aminoacylation of primordial tRNAs. The Schimmel laboratory is interested in understanding all aspects of these systems.

    The cloverleaf structure of tRNA is folded into two domains--one contains the anticodon with the template reading head of the genetic code, and the other (called the minihelix domain) contains the amino acid attachment site. The minihelix domain itself is a substrate for aminoacylation, for at least ten of the synthetases. Even smaller pieces than the minihelix are active as substrates (see figure). Because these pieces lack the anticodon trinucleotides, the relationship between the sequences/structures of these active pieces (with as few as four base pairs) and the specific amino acid is distinct from the genetic code. The relationship between sequences and structures in tRNA acceptor stems and specific amino acids is referred to as an operational RNA code for amino acids. The operational RNA code is thought to have predated the genetic code.

    Our recent studies have expanded upon these concepts to elucidate a role for the tRNA in amino acid fine structure recognition. That is, the ability to distinguish between two closely similar amino acids is greatly enhanced by an effector function of the tRNA, that causes the rejection of amino acids that are not exactly matched with the synthetase and its cognate tRNA. This RNA-dependent fine structure recognition may have first developed in an RNA world, and later was incorporated into the synthetase system as a critical part of maintaining the accuracy of the genetic code.
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Teaching

advisees

  • graduate advising relationship

    • Song, Youngzee, Ph.D.  candidate, 2014 - 2017
    • Lee, Peter S., Ph.D.  candidate, 2010 - 2014
    • Song, Youngzee, Ph.D.  candidate, 2009 - 2014
    • He, Weiwei, Ph.D.  candidate, 2008 - 2013
    • Chong, Yeeting, Ph.D.  candidate, 2006 - 2011
    • Nangle, Leslie, Ph.D.  candidate, 2002 - 2006
    • Lovato-Tse, Martha , Ph.D.  candidate, 1999 - 2003
    • Nordin, Brian, Ph.D.  candidate, 1998 - 2002
  • postdoc or fellow advising relationship

    • Chong, Yeeting, Ph.D.  candidate, 2011 - 2012
    • Nordin, Brian, 2003 - 2005
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Background

education and training

  • Ph.D. in Biology, Massachusetts Institute of Technology 1966

awards and honors

  • Member (National Academy of Sciences), conferred by National Academy of Sciences, 1990
  • Fellow of the American Academy of Arts and Sciences, conferred by American Academy of Arts & Sciences, 1985
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Contact

full name

  • Paul R. Schimmel

geographic location

  • Scripps California 

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