Year |
Citation |
Score |
2023 |
Kuhle B, Chen Q, Schimmel P. tRNA renovatio: Rebirth through fragmentation. Molecular Cell. PMID 37802077 DOI: 10.1016/j.molcel.2023.09.016 |
0.344 |
|
2023 |
de Potter B, Vallee I, Camacho N, Filipe Costa Póvoas L, Bonsembiante A, Pons I Pons A, Eckhard U, Gomis-Rüth FX, Yang XL, Schimmel P, Kuhle B, Ribas de Pouplana L. Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase. Nucleic Acids Research. PMID 37638745 DOI: 10.1093/nar/gkad696 |
0.639 |
|
2023 |
Han L, Luo Z, Ju Y, Chen B, Zou T, Wang J, Xu J, Gu Q, Yang XL, Schimmel P, Zhou H. The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements. Science Advances. 9: eadf1027. PMID 36753552 DOI: 10.1126/sciadv.adf1027 |
0.372 |
|
2021 |
Ju Y, Han L, Chen B, Luo Z, Gu Q, Xu J, Yang XL, Schimmel P, Zhou H. X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications. Nucleic Acids Research. PMID 34390350 DOI: 10.1093/nar/gkab707 |
0.307 |
|
2021 |
Sun L, Wei N, Kuhle B, Blocquel D, Novick S, Matuszek Z, Zhou H, He W, Zhang J, Weber T, Horvath R, Latour P, Pan T, Schimmel P, Griffin PR, et al. CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33753480 DOI: 10.1073/pnas.2012898118 |
0.509 |
|
2020 |
Kuhle B, Chihade J, Schimmel P. Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs. Nature Communications. 11: 969. PMID 32080176 DOI: 10.1038/S41467-020-14725-Y |
0.773 |
|
2019 |
Blocquel D, Sun L, Matuszek Z, Li S, Weber T, Kuhle B, Kooi G, Wei N, Baets J, Pan T, Schimmel P, Yang XL. 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. PMID 31501329 DOI: 10.1073/Pnas.1908288116 |
0.552 |
|
2018 |
Naganuma M, Sekine SI, Chong YE, Guo M, Yang XL, Gamper H, Hou YM, Schimmel P, Yokoyama S. Author Correction: The selective tRNA aminoacylation mechanism based on a single G•U pair. Nature. PMID 30459470 DOI: 10.1038/S41586-018-0760-4 |
0.457 |
|
2018 |
Xu Z, Lo WS, Beck DB, Schuch LA, Oláhová M, Kopajtich R, Chong YE, Alston CL, Seidl E, Zhai L, Lau CF, Timchak D, LeDuc CA, Borczuk AC, Teich AF, ... ... Schimmel P, 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. 103: 100-114. PMID 29979980 DOI: 10.1016/J.Ajhg.2018.06.006 |
0.342 |
|
2018 |
Chong YE, Guo M, Yang XL, Kuhle B, Naganuma M, Sekine SI, 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. PMID 29967150 DOI: 10.1073/Pnas.1807109115 |
0.538 |
|
2018 |
Vo MN, Terrey M, Lee JW, Roy B, Moresco JJ, Sun L, Fu H, Liu Q, Weber TG, Yates JR, Fredrick K, Schimmel P, Ackerman SL. Publisher Correction: ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase. Nature. PMID 29925958 DOI: 10.1038/S41586-018-0271-3 |
0.5 |
|
2018 |
Vo MN, Terrey M, Lee JW, Roy B, Moresco JJ, Sun L, Fu H, Liu Q, Weber TG, Yates JR, Fredrick K, Schimmel P, Ackerman SL. ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase. Nature. PMID 29769718 DOI: 10.1038/S41586-018-0137-8 |
0.608 |
|
2018 |
Song Y, Zhou H, Vo MN, Shi Y, Nawaz MH, Vargas-Rodriguez O, Diedrich JK, Yates JR, Kishi S, Musier-Forsyth K, Schimmel P. Publisher Correction: Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid. Nature Communications. 9: 1113. PMID 29535387 DOI: 10.1038/S41467-018-03594-1 |
0.776 |
|
2017 |
Song Y, Zhou H, Vo MN, Shi Y, Nawaz MH, Vargas-Rodriguez O, Diedrich JK, Yates JR, Kishi S, Musier-Forsyth K, Schimmel P. Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid. Nature Communications. 8: 2281. PMID 29273753 DOI: 10.1038/S41467-017-02201-Z |
0.801 |
|
2017 |
Xu X, Zhou H, Zhou Q, Hong F, Vo MN, Niu W, Wang Z, Xiong X, Nakamura K, Wakasugi K, Schimmel P, Yang XL. An alternative conformation of human TrpRS suggests a role of zinc in activating non-enzymatic function. Rna Biology. 0. PMID 28910573 DOI: 10.1080/15476286.2017.1377868 |
0.323 |
|
2017 |
Schimmel P. The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis. Nature Reviews. Molecular Cell Biology. PMID 28875994 DOI: 10.1038/Nrm.2017.77 |
0.452 |
|
2017 |
Blocquel D, Li S, Wei N, Daub H, Sajish M, Erfurth ML, Kooi G, Zhou J, Bai G, Schimmel P, Jordanova A, Yang XL. Alternative stable conformation capable of protein misinteraction links tRNA synthetase to peripheral neuropathy. Nucleic Acids Research. PMID 28531329 DOI: 10.1093/Nar/Gkx455 |
0.378 |
|
2016 |
Sun L, Song Y, Blocquel D, Yang XL, 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. PMID 27911835 DOI: 10.1073/Pnas.1617316113 |
0.564 |
|
2016 |
Sun L, Gomes AC, He W, Zhou H, Wang X, Pan DW, Schimmel P, Pan T, Yang XL. Evolutionary gain of alanine mischarging to non-cognate tRNAs with a G4:U69 base pair. Journal of the American Chemical Society. PMID 27622773 DOI: 10.1021/Jacs.6B07121 |
0.63 |
|
2016 |
Song Y, Shi Y, Carland TM, Lian S, Sasaki T, Schork NJ, Head SR, 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. PMID 27402763 DOI: 10.1073/Pnas.1608139113 |
0.343 |
|
2016 |
Wei Z, Xu Z, Liu X, Lo WS, Ye F, Lau CF, Wang F, Zhou JJ, Nangle LA, Yang XL, Zhang M, Schimmel P. Alternative splicing creates two new architectures for human tyrosyl-tRNA synthetase. Nucleic Acids Research. PMID 26773056 DOI: 10.1093/Nar/Gkw002 |
0.407 |
|
2016 |
Kanaji S, Kanaji T, Vo M, Zarpellon A, Shapiro R, Belani R, Do M, Yang X, Ruggeri ZM, Schimmel P. Extracellular Tyrosyl-tRNA Synthetase Is a Potent Stimulator of Thrombocytopoiesis Blood. 128: 1476-1476. DOI: 10.1182/Blood.V128.22.1476.1476 |
0.318 |
|
2015 |
Sajish M, Schimmel P. A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. Nature. 519: 370-3. PMID 25533949 DOI: 10.1038/Nature14028 |
0.387 |
|
2014 |
Liu Y, Satz JS, Vo MN, Nangle LA, Schimmel P, Ackerman SL. Deficiencies in tRNA synthetase editing activity cause cardioproteinopathy. Proceedings of the National Academy of Sciences of the United States of America. 111: 17570-5. PMID 25422440 DOI: 10.1073/Pnas.1420196111 |
0.359 |
|
2014 |
Ishimura R, Nagy G, Dotu I, Zhou H, Yang XL, Schimmel P, Senju S, Nishimura Y, Chuang JH, Ackerman SL. RNA function. Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration. Science (New York, N.Y.). 345: 455-9. PMID 25061210 DOI: 10.1126/Science.1249749 |
0.394 |
|
2014 |
Lo WS, Gardiner E, Xu Z, Lau CF, Wang F, Zhou JJ, Mendlein JD, Nangle LA, Chiang KP, Yang XL, Au KF, Wong WH, Guo M, Zhang M, Schimmel P. Human tRNA synthetase catalytic nulls with diverse functions. Science (New York, N.Y.). 345: 328-32. PMID 25035493 DOI: 10.1126/Science.1252943 |
0.537 |
|
2014 |
Naganuma M, Sekine S, Chong YE, Guo M, Yang XL, Gamper H, Hou YM, Schimmel P, Yokoyama S. The selective tRNA aminoacylation mechanism based on a single G•U pair. Nature. 510: 507-11. PMID 24919148 DOI: 10.1038/Nature13440 |
0.584 |
|
2013 |
Wang F, Xu Z, Zhou J, Lo WS, Lau CF, Nangle LA, Yang XL, Zhang M, Schimmel P. Regulated capture by exosomes of mRNAs for cytoplasmic tRNA synthetases. The Journal of Biological Chemistry. 288: 29223-8. PMID 24003230 DOI: 10.1074/Jbc.C113.490599 |
0.343 |
|
2013 |
Guo M, Schimmel P. Essential nontranslational functions of tRNA synthetases. Nature Chemical Biology. 9: 145-53. PMID 23416400 DOI: 10.1038/Nchembio.1158 |
0.492 |
|
2013 |
Klipcan L, Safro M, Schimmel P. Anticodon G recognition by tRNA synthetases mimics the tRNA core. Trends in Biochemical Sciences. 38: 229-32. PMID 23266103 DOI: 10.1016/J.Tibs.2012.11.002 |
0.481 |
|
2013 |
Zhou H, Sun L, Yang XL, Schimmel P. ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. Nature. 494: 121-4. PMID 23263184 DOI: 10.1038/Nature11774 |
0.597 |
|
2013 |
Ofir-Birin Y, Fang P, Bennett SP, Zhang HM, Wang J, Rachmin I, Shapiro R, Song J, Dagan A, Pozo J, Kim S, Marshall AG, Schimmel P, Yang XL, Nechushtan H, et al. Structural switch of lysyl-tRNA synthetase between translation and transcription. Molecular Cell. 49: 30-42. PMID 23159739 DOI: 10.1016/J.Molcel.2012.10.010 |
0.709 |
|
2013 |
Schimmel P. 1 New biology from ancient enzymes Journal of Biomolecular Structure & Dynamics. 31: 1-1. DOI: 10.1080/07391102.2013.786317 |
0.414 |
|
2012 |
Xu Z, Wei Z, Zhou JJ, Ye F, Lo WS, Wang F, Lau CF, Wu J, Nangle LA, Chiang KP, Yang XL, Zhang M, Schimmel P. Internally deleted human tRNA synthetase suggests evolutionary pressure for repurposing. Structure (London, England : 1993). 20: 1470-7. PMID 22958643 DOI: 10.1016/J.Str.2012.08.001 |
0.322 |
|
2012 |
Guo M, Schimmel P. Homeostatic mechanisms by alternative forms of tRNA synthetases. Trends in Biochemical Sciences. 37: 401-3. PMID 22858252 DOI: 10.1016/J.Tibs.2012.07.003 |
0.477 |
|
2012 |
Lee PS, Zhang HM, Marshall AG, Yang XL, Schimmel P. Uncovering of a short internal peptide activates a tRNA synthetase procytokine. The Journal of Biological Chemistry. 287: 20504-8. PMID 22549774 DOI: 10.1074/Jbc.C112.369439 |
0.352 |
|
2012 |
Sajish M, Zhou Q, Kishi S, Valdez DM, Kapoor M, Guo M, Lee S, Kim S, Yang XL, Schimmel P. Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-γ and p53 signaling. Nature Chemical Biology. 8: 547-54. PMID 22504299 DOI: 10.1038/Nchembio.937 |
0.462 |
|
2012 |
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. 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. 109: E640-7. PMID 22345558 DOI: 10.1073/Pnas.1200194109 |
0.433 |
|
2012 |
Wang J, Fang P, Schimmel P, Guo M. Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor. The Journal of Physical Chemistry. B. 116: 6798-805. PMID 22329685 DOI: 10.1021/Jp212457W |
0.714 |
|
2012 |
Guo M, Schimmel P. Structural analyses clarify the complex control of mistranslation by tRNA synthetases. Current Opinion in Structural Biology. 22: 119-26. PMID 22155179 DOI: 10.1016/J.Sbi.2011.11.008 |
0.583 |
|
2011 |
Schimmel P. Mistranslation and its control by tRNA synthetases. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 366: 2965-71. PMID 21930589 DOI: 10.1098/Rstb.2011.0158 |
0.46 |
|
2011 |
Yang XL, Schimmel P. Functional expansion of the tRNA world under stress. Molecular Cell. 43: 500-2. PMID 21855789 DOI: 10.1016/J.Molcel.2011.08.004 |
0.309 |
|
2011 |
Fang P, Zhang HM, Shapiro R, Marshall AG, Schimmel P, Yang XL, 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. 108: 8239-44. PMID 21536907 DOI: 10.1073/Pnas.1100224108 |
0.69 |
|
2011 |
Vo MN, Yang XL, Schimmel P. Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase. The Journal of Biological Chemistry. 286: 11563-8. PMID 21310955 DOI: 10.1074/Jbc.C110.213876 |
0.383 |
|
2011 |
Schimmel P. The RNP bridge between two worlds. Nature Reviews. Molecular Cell Biology. 12: 135. PMID 21285979 DOI: 10.1038/Nrm3061 |
0.348 |
|
2011 |
Nawaz MH, Merriman E, Yang XL, Schimmel P. p23H 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. 108: 2723-8. PMID 21285375 DOI: 10.1073/Pnas.1019400108 |
0.321 |
|
2010 |
Guo M, Shapiro R, Morris GM, Yang XL, Schimmel P. Packaging HIV virion components through dynamic equilibria of a human tRNA synthetase. The Journal of Physical Chemistry. B. 114: 16273-9. PMID 21058683 DOI: 10.1021/Jp1082517 |
0.517 |
|
2010 |
Han GW, Yang XL, McMullan D, Chong YE, Krishna SS, Rife CL, Weekes D, Brittain SM, Abdubek P, Ambing E, Astakhova T, Axelrod HL, Carlton D, Caruthers J, Chiu HJ, ... ... Schimmel P, et al. Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66: 1326-34. PMID 20944229 DOI: 10.1107/S1744309110037619 |
0.301 |
|
2010 |
Guo M, Yang XL, Schimmel P. New functions of aminoacyl-tRNA synthetases beyond translation. Nature Reviews. Molecular Cell Biology. 11: 668-74. PMID 20700144 DOI: 10.1038/Nrm2956 |
0.519 |
|
2010 |
Guo M, Shapiro R, Schimmel P, Yang XL. Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase. Acta Crystallographica. Section D, Biological Crystallography. 66: 243-50. PMID 20179335 DOI: 10.1107/S0907444909055462 |
0.45 |
|
2010 |
Zhou Q, Kapoor M, Guo M, Belani R, Xu X, Kiosses WB, Hanan M, Park C, Armour E, Do MH, Nangle LA, Schimmel P, Yang XL. Orthogonal use of a human tRNA synthetase active site to achieve multifunctionality. Nature Structural & Molecular Biology. 17: 57-61. PMID 20010843 DOI: 10.1038/Nsmb.1706 |
0.55 |
|
2010 |
Guo M, Schimmel P, Yang XL. Functional expansion of human tRNA synthetases achieved by structural inventions. Febs Letters. 584: 434-42. PMID 19932696 DOI: 10.1016/J.Febslet.2009.11.064 |
0.552 |
|
2009 |
Guo M, Chong YE, Shapiro R, Beebe K, Yang XL, Schimmel P. Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. Nature. 462: 808-12. PMID 20010690 DOI: 10.1038/Nature08612 |
0.548 |
|
2009 |
Sankaran B, Bonnett SA, Shah K, Gabriel S, Reddy R, Schimmel P, Rodionov DA, de Crécy-Lagard V, Helmann JD, Iwata-Reuyl D, Swairjo MA. Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence for GTP cyclohydrolase IB. Journal of Bacteriology. 191: 6936-49. PMID 19767425 DOI: 10.1128/Jb.00287-09 |
0.608 |
|
2009 |
Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science (New York, N.Y.). 325: 744-7. PMID 19661429 DOI: 10.1126/Science.1174343 |
0.561 |
|
2009 |
Storkebaum E, Leitão-Gonçalves R, Godenschwege T, Nangle L, Mejia M, Bosmans I, Ooms T, Jacobs A, Van Dijck P, Yang XL, Schimmel P, Norga K, Timmerman V, Callaerts P, Jordanova A. 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. 106: 11782-7. PMID 19561293 DOI: 10.1073/Pnas.0905339106 |
0.317 |
|
2009 |
Schimmel P, Guo M. A tipping point for mistranslation and disease. Nature Structural & Molecular Biology. 16: 348-9. PMID 19343067 DOI: 10.1038/Nsmb0409-348 |
0.494 |
|
2009 |
El Yacoubi B, Lyons B, Cruz Y, Reddy R, Nordin B, Agnelli F, Williamson JR, Schimmel P, Swairjo MA, de Crécy-Lagard V. The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA. Nucleic Acids Research. 37: 2894-909. PMID 19287007 DOI: 10.1093/Nar/Gkp152 |
0.741 |
|
2009 |
Schimmel P, Guo M. Ancient tRNA synthetase meets modern structural biology. Structure (London, England : 1993). 17: 315-7. PMID 19278642 DOI: 10.1016/J.Str.2009.02.002 |
0.469 |
|
2008 |
Schimmel P. Development of tRNA synthetases and connection to genetic code and disease. Protein Science : a Publication of the Protein Society. 17: 1643-52. PMID 18765819 DOI: 10.1110/Ps.037242.108 |
0.433 |
|
2008 |
Chong YE, Yang XL, Schimmel P. Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. The Journal of Biological Chemistry. 283: 30073-8. PMID 18723508 DOI: 10.1074/Jbc.M805943200 |
0.457 |
|
2008 |
Park SG, 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. 105: 11043-9. PMID 18682559 DOI: 10.1073/Pnas.0802862105 |
0.398 |
|
2008 |
Guo M, Ignatov M, Musier-Forsyth K, Schimmel P, Yang XL. 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. 105: 2331-6. PMID 18272479 DOI: 10.1073/Pnas.0712072105 |
0.728 |
|
2008 |
Beebe K, Mock M, Merriman E, Schimmel P. Distinct domains of tRNA synthetase recognize the same base pair. Nature. 451: 90-3. PMID 18172502 DOI: 10.1038/Nature06454 |
0.524 |
|
2008 |
Kapoor M, Zhou Q, Otero F, Myers CA, Bates A, Belani R, Liu J, Luo JK, Tzima E, Zhang DE, Yang XL, Schimmel P. Evidence for annexin II-S100A10 complex and plasmin in mobilization of cytokine activity of human TrpRS. The Journal of Biological Chemistry. 283: 2070-7. PMID 17999956 DOI: 10.1074/Jbc.M706028200 |
0.366 |
|
2007 |
Yang XL, Kapoor M, Otero FJ, Slike BM, Tsuruta H, Frausto R, Bates A, Ewalt KL, Cheresh DA, Schimmel P. Gain-of-function mutational activation of human tRNA synthetase procytokine. Chemistry & Biology. 14: 1323-33. PMID 18096501 DOI: 10.1016/J.Chembiol.2007.10.016 |
0.354 |
|
2007 |
Waas WF, Schimmel P. Evidence that tRNA synthetase-directed proton transfer stops mistranslation. Biochemistry. 46: 12062-70. PMID 17924654 DOI: 10.1021/Bi7007454 |
0.459 |
|
2007 |
Zubieta C, Joseph R, Krishna SS, McMullan D, Kapoor M, Axelrod HL, Miller MD, Abdubek P, Acosta C, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, ... ... Schimmel P, et al. Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Proteins. 69: 234-43. PMID 17654547 DOI: 10.1002/Prot.21673 |
0.325 |
|
2007 |
Zubieta C, Krishna SS, Kapoor M, Kozbial P, McMullan D, Axelrod HL, Miller MD, Abdubek P, Ambing E, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, ... ... Schimmel P, et al. Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif. Proteins. 69: 223-33. PMID 17654545 DOI: 10.1002/Prot.21550 |
0.364 |
|
2007 |
Yang XL, Guo M, Kapoor M, Ewalt KL, Otero FJ, Skene RJ, McRee DE, Schimmel P. Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase. Structure (London, England : 1993). 15: 793-805. PMID 17637340 DOI: 10.1016/J.Str.2007.05.009 |
0.553 |
|
2007 |
Waas WF, Druzina Z, Hanan M, Schimmel P. Role of a tRNA base modification and its precursors in frameshifting in eukaryotes. The Journal of Biological Chemistry. 282: 26026-34. PMID 17623669 DOI: 10.1074/Jbc.M703391200 |
0.429 |
|
2007 |
Bacher JM, Waas WF, Metzgar D, de Crécy-Lagard V, Schimmel P. Genetic code ambiguity confers a selective advantage on Acinetobacter baylyi. Journal of Bacteriology. 189: 6494-6. PMID 17616603 DOI: 10.1128/Jb.00622-07 |
0.577 |
|
2007 |
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. 368: 111-21. PMID 17603003 DOI: 10.1016/J.Ab.2007.05.013 |
0.527 |
|
2007 |
Nangle LA, Zhang W, Xie W, Yang XL, Schimmel P. Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect. Proceedings of the National Academy of Sciences of the United States of America. 104: 11239-44. PMID 17595294 DOI: 10.1073/Pnas.0705055104 |
0.317 |
|
2007 |
Xie W, Nangle LA, Zhang W, Schimmel P, Yang XL. Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 104: 9976-81. PMID 17545306 DOI: 10.1073/Pnas.0703908104 |
0.353 |
|
2007 |
Bacher JM, Schimmel P. An editing-defective aminoacyl-tRNA synthetase is mutagenic in aging bacteria via the SOS response. Proceedings of the National Academy of Sciences of the United States of America. 104: 1907-12. PMID 17264207 DOI: 10.1073/Pnas.0610835104 |
0.343 |
|
2006 |
Schimmel P, Yang XL. Perfecting the genetic code with an RNP complex. Structure (London, England : 1993). 14: 1729-30. PMID 17161363 DOI: 10.1016/J.Str.2006.11.002 |
0.365 |
|
2006 |
Xie W, Schimmel P, Yang XL. Crystallization and preliminary X-ray analysis of a native human tRNA synthetase whose allelic variants are associated with Charcot-Marie-Tooth disease. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 1243-6. PMID 17142907 DOI: 10.1107/S1744309106046434 |
0.312 |
|
2006 |
Nangle LA, Motta CM, Schimmel P. Global effects of mistranslation from an editing defect in mammalian cells. Chemistry & Biology. 13: 1091-100. PMID 17052613 DOI: 10.1016/J.Chembiol.2006.08.011 |
0.365 |
|
2006 |
Seburn KL, Nangle LA, Cox GA, Schimmel P, Burgess RW. An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model. Neuron. 51: 715-26. PMID 16982418 DOI: 10.1016/J.Neuron.2006.08.027 |
0.304 |
|
2006 |
Lee JW, Beebe K, Nangle LA, Jang J, Longo-Guess CM, Cook SA, Davisson MT, Sundberg JP, Schimmel P, Ackerman SL. Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration. Nature. 443: 50-5. PMID 16906134 DOI: 10.1038/Nature05096 |
0.36 |
|
2006 |
Yang XL, Otero FJ, Ewalt KL, Liu J, Swairjo MA, Köhrer C, RajBhandary UL, Skene RJ, McRee DE, Schimmel P. Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis. The Embo Journal. 25: 2919-29. PMID 16724112 DOI: 10.1038/Sj.Emboj.7601154 |
0.42 |
|
2006 |
Schimmel P, Beebe K. 8 Aminoacyl tRNA Synthetases: From the RNA World to the Theater of Proteins Cold Spring Harbor Monograph Archive. 43: 227-255. DOI: 10.1101/087969739.43.227 |
0.467 |
|
2006 |
Marquéz V, Nierhaus KH, de Pouplana LR, Schimmel P. Trna and synthetases Protein Synthesis and Ribosome Structure. 145-184. DOI: 10.1002/3527603433.ch4 |
0.347 |
|
2005 |
Swairjo MA, Reddy RR, Lee B, Van Lanen SG, Brown S, de Crécy-Lagard V, Iwata-Reuyl D, Schimmel P. Crystallization and preliminary X-ray characterization of the nitrile reductase QueF: a queuosine-biosynthesis enzyme. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 61: 945-8. PMID 16511203 DOI: 10.1107/S1744309105029246 |
0.589 |
|
2005 |
Waas WF, de Crécy-Lagard V, Schimmel P. Discovery of a gene family critical to wyosine base formation in a subset of phenylalanine-specific transfer RNAs. The Journal of Biological Chemistry. 280: 37616-22. PMID 16162496 DOI: 10.1074/Jbc.M506939200 |
0.639 |
|
2005 |
Reader JS, Ordoukhanian PT, Kim JG, de Crécy-Lagard V, Hwang I, Farrand S, Schimmel P. Major biocontrol of plant tumors targets tRNA synthetase. Science (New York, N.Y.). 309: 1533. PMID 16141066 DOI: 10.1126/Science.1116841 |
0.545 |
|
2005 |
Ewalt KL, Yang XL, Otero FJ, Liu J, Slike B, Schimmel P. Variant of human enzyme sequesters reactive intermediate. Biochemistry. 44: 4216-21. PMID 15766249 DOI: 10.1021/Bi048116L |
0.428 |
|
2005 |
Swairjo MA, Schimmel PR. Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 102: 988-93. PMID 15657145 DOI: 10.1073/pnas.0409024102 |
0.319 |
|
2005 |
Bacher JM, de Crécy-Lagard V, Schimmel PR. Inhibited cell growth and protein functional changes from an editing-defective tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 102: 1697-701. PMID 15647356 DOI: 10.1073/pnas.0409064102 |
0.614 |
|
2004 |
Tamura K, Schimmel P. Non-enzymatic aminoacylation of an RNA minihelix with an aminoacyl phosphate oligonucleotide. Nucleic Acids Symposium Series (2004). 269-70. PMID 17150582 DOI: 10.1093/nass/48.1.269 |
0.33 |
|
2004 |
Metzgar D, Bacher JM, Pezo V, Reader J, Döring V, Schimmel P, Marlière P, de Crécy-Lagard V. Acinetobacter sp. ADP1: an ideal model organism for genetic analysis and genome engineering. Nucleic Acids Research. 32: 5780-90. PMID 15514111 DOI: 10.1093/Nar/Gkh881 |
0.561 |
|
2004 |
Schimmel P, Ewalt K. Translation silenced by fused pair of tRNA synthetases. Cell. 119: 147-8. PMID 15479630 DOI: 10.1016/J.Cell.2004.10.001 |
0.338 |
|
2004 |
Schimmel P, Beebe K. Molecular biology: genetic code seizes pyrrolysine. Nature. 431: 257-8. PMID 15372017 DOI: 10.1038/431257A |
0.366 |
|
2004 |
Tang HL, Yeh LS, Chen NK, Ripmaster T, Schimmel P, Wang CC. Translation of a yeast mitochondrial tRNA synthetase initiated at redundant non-AUG codons. The Journal of Biological Chemistry. 279: 49656-63. PMID 15358761 DOI: 10.1074/Jbc.M408081200 |
0.41 |
|
2004 |
Tamura K, Schimmel P. Chiral-selective aminoacylation of an RNA minihelix. Science (New York, N.Y.). 305: 1253. PMID 15333830 DOI: 10.1126/Science.1099141 |
0.388 |
|
2004 |
Schimmel P, Yang XL. Two classes give lessons about CCA. Nature Structural & Molecular Biology. 11: 807-8. PMID 15332079 DOI: 10.1038/Nsmb0904-807 |
0.411 |
|
2004 |
Hendrickson TL, de Crécy-Lagard V, Schimmel P. Incorporation of nonnatural amino acids into proteins. Annual Review of Biochemistry. 73: 147-76. PMID 15189139 DOI: 10.1146/Annurev.Biochem.73.012803.092429 |
0.643 |
|
2004 |
Pezo V, Metzgar D, Hendrickson TL, Waas WF, Hazebrouck S, Döring V, Marlière P, Schimmel P, De Crécy-Lagard V. Artificially ambiguous genetic code confers growth yield advantage. Proceedings of the National Academy of Sciences of the United States of America. 101: 8593-7. PMID 15163798 DOI: 10.1073/Pnas.0402893101 |
0.366 |
|
2004 |
Yang XL, Schimmel P, Ewalt KL. Relationship of two human tRNA synthetases used in cell signaling. Trends in Biochemical Sciences. 29: 250-6. PMID 15130561 DOI: 10.1016/J.Tibs.2004.03.002 |
0.384 |
|
2004 |
Beebe K, Merriman E, Ribas De Pouplana L, Schimmel P. A domain for editing by an archaebacterial tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 101: 5958-63. PMID 15079065 DOI: 10.1073/Pnas.0401530101 |
0.697 |
|
2004 |
Lovato MA, Swairjo MA, Schimmel P. Positional recognition of a tRNA determinant dependent on a peptide insertion. Molecular Cell. 13: 843-51. PMID 15053877 DOI: 10.1016/S1097-2765(04)00125-X |
0.807 |
|
2004 |
Swairjo MA, Otero FJ, Yang XL, Lovato MA, Skene RJ, McRee DE, Ribas de Pouplana L, Schimmel P. Alanyl-tRNA synthetase crystal structure and design for acceptor-stem recognition. Molecular Cell. 13: 829-41. PMID 15053876 DOI: 10.1016/S1097-2765(04)00126-1 |
0.817 |
|
2004 |
Reader JS, Metzgar D, Schimmel P, de Crécy-Lagard V. Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine. The Journal of Biological Chemistry. 279: 6280-5. PMID 14660578 DOI: 10.1074/Jbc.M310858200 |
0.573 |
|
2004 |
De Pereda JM, Waas WF, Jan Y, Ruoslahti E, Schimmel P, Pascual J. Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity. The Journal of Biological Chemistry. 279: 8111-5. PMID 14660562 DOI: 10.1074/Jbc.M311449200 |
0.395 |
|
2003 |
Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L. Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proceedings of the National Academy of Sciences of the United States of America. 100: 15376-80. PMID 14671330 DOI: 10.1073/Pnas.2136794100 |
0.695 |
|
2003 |
Nordin BE, Schimmel P. Transiently misacylated tRNA is a primer for editing of misactivated adenylates by class I aminoacyl-tRNA synthetases. Biochemistry. 42: 12989-97. PMID 14596614 DOI: 10.1021/Bi035052Q |
0.695 |
|
2003 |
Beebe K, Merriman E, Schimmel P. Structure-specific tRNA determinants for editing a mischarged amino acid. The Journal of Biological Chemistry. 278: 45056-61. PMID 12949076 DOI: 10.1074/Jbc.M307080200 |
0.46 |
|
2003 |
Tamura K, Schimmel P. Peptide synthesis with a template-like RNA guide and aminoacyl phosphate adaptors. Proceedings of the National Academy of Sciences of the United States of America. 100: 8666-9. PMID 12857953 DOI: 10.1073/Pnas.1432909100 |
0.425 |
|
2003 |
Frugier M, Giege R, Schimmel P. RNA recognition by designed peptide fusion creates "artificial" tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 100: 7471-5. PMID 12796515 DOI: 10.1073/Pnas.1332771100 |
0.468 |
|
2003 |
Schimmel P, Tamura K. tRNA structure goes from L to lambda. Cell. 113: 276-8. PMID 12732135 DOI: 10.1016/S0092-8674(03)00313-1 |
0.305 |
|
2003 |
Wang CC, Chang KJ, Tang HL, Hsieh CJ, Schimmel P. Mitochondrial form of a tRNA synthetase can be made bifunctional by manipulating its leader peptide. Biochemistry. 42: 1646-51. PMID 12578378 DOI: 10.1021/Bi025964C |
0.409 |
|
2003 |
Beebe K, Ribas De Pouplana L, Schimmel P. Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. The Embo Journal. 22: 668-75. PMID 12554667 DOI: 10.1093/Emboj/Cdg065 |
0.687 |
|
2003 |
Schimmel P. Incorporation of Non-natural Amino Acids Annual Review of Biochemistry. DOI: 10.1146/Annurev.Biochem.73.012803 |
0.315 |
|
2003 |
Yaug XL, Liu J, Skene RJ, McRee DE, Schimmel P. Crystal structure of an EMAP-II-like cytokine released from a human tRNA synthetase Helvetica Chimica Acta. 86: 1246-1257. DOI: 10.1002/Hlca.200390107 |
0.4 |
|
2002 |
Schimmel P. Introducing New Amino Acids into Proteins. The Scientific World Journal. 2: 47-48. PMID 29973798 DOI: 10.1100/Tsw.2002.24 |
0.446 |
|
2002 |
Kushiro T, Schimmel P. Trbp111 selectively binds a noncovalently assembled tRNA-like structure. Proceedings of the National Academy of Sciences of the United States of America. 99: 16631-5. PMID 12481025 DOI: 10.1073/Pnas.262667999 |
0.476 |
|
2002 |
Liu J, Yang XL, Ewalt KL, Schimmel P. Mutational switching of a yeast tRNA synthetase into a mammalian-like synthetase cytokine. Biochemistry. 41: 14232-7. PMID 12450387 DOI: 10.1021/Bi0205395 |
0.445 |
|
2002 |
Cen S, Javanbakht H, Kim S, Shiba K, Craven R, Rein A, Ewalt K, Schimmel P, Musier-Forsyth K, Kleiman L. Retrovirus-specific packaging of aminoacyl-tRNA synthetases with cognate primer tRNAs. Journal of Virology. 76: 13111-5. PMID 12438642 DOI: 10.1128/Jvi.76.24.13111-13115.2002 |
0.68 |
|
2002 |
Yang XL, Skene RJ, McRee DE, Schimmel P. Crystal structure of a human aminoacyl-tRNA synthetase cytokine. Proceedings of the National Academy of Sciences of the United States of America. 99: 15369-74. PMID 12427973 DOI: 10.1073/Pnas.242611799 |
0.433 |
|
2002 |
Ewalt KL, Schimmel P. Activation of angiogenic signaling pathways by two human tRNA synthetases Biochemistry. 41: 13344-13349. PMID 12416978 DOI: 10.1021/Bi020537K |
0.468 |
|
2002 |
Nangle LA, De Crécy Lagard V, Döring V, Schimmel P. Genetic code ambiguity: Cell viability related to severity of editing defects in mutant tRNA synthetases Journal of Biological Chemistry. 277: 45729-45733. PMID 12244062 DOI: 10.1074/Jbc.M208093200 |
0.412 |
|
2002 |
Tamura K, Schimmel P. Ribozyme programming extends the protein code. Nature Biotechnology. 20: 669-70. PMID 12089548 DOI: 10.1038/Nbt0702-669 |
0.368 |
|
2002 |
Bishop AC, Xu J, Johnson RC, Schimmel P, de Crécy-Lagard V. Identification of the tRNA-dihydrouridine synthase family. The Journal of Biological Chemistry. 277: 25090-5. PMID 11983710 DOI: 10.1074/Jbc.M203208200 |
0.595 |
|
2002 |
Wakasugi K, Slike BM, Hood J, Ewalt KL, Cheresh DA, Schimmel P. Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase. The Journal of Biological Chemistry. 277: 20124-6. PMID 11956181 DOI: 10.1074/Jbc.C200126200 |
0.367 |
|
2002 |
Nordin BE, Schimmel P. Plasticity of recognition of the 3'-end of mischarged tRNA by class I aminoacyl-tRNA synthetases. The Journal of Biological Chemistry. 277: 20510-7. PMID 11923317 DOI: 10.1074/Jbc.M202023200 |
0.694 |
|
2002 |
Hendrickson TL, Nomanbhoy TK, De Crécy-Lagard V, Fukai S, Nureki O, Yokoyama S, Schimmel P. Mutational separation of two pathways for editing by a class I tRNA synthetase Molecular Cell. 9: 353-362. PMID 11864608 DOI: 10.1016/S1097-2765(02)00449-5 |
0.666 |
|
2002 |
Bishop AC, Nomanbhoy TK, Schimmel P. Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 99: 585-90. PMID 11782529 DOI: 10.1073/Pnas.012611299 |
0.45 |
|
2002 |
Wakasugi K, Slike BM, Hood J, Otani A, Ewalt KL, Friedlander M, Cheresh DA, Schimmel P. A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. Proceedings of the National Academy of Sciences of the United States of America. 99: 173-7. PMID 11773626 DOI: 10.1073/Pnas.012602099 |
0.366 |
|
2001 |
Schimmel P, Ribas de Pouplana L. Formation of two classes of tRNA synthetases in relation to editing functions and genetic code. Cold Spring Harbor Symposia On Quantitative Biology. 66: 161-6. PMID 12762018 DOI: 10.1101/Sqb.2001.66.161 |
0.636 |
|
2001 |
Ribas de Pouplana L, Brown JR, Schimmel P. Structure-based phylogeny of class IIa tRNA synthetases in relation to an unusual biochemistry. Journal of Molecular Evolution. 53: 261-8. PMID 11675586 DOI: 10.1007/S002390010216 |
0.671 |
|
2001 |
Ribas de Pouplana L, Schimmel P. Aminoacyl-tRNA synthetases: potential markers of genetic code development. Trends in Biochemical Sciences. 26: 591-6. PMID 11590011 DOI: 10.1016/S0968-0004(01)01932-6 |
0.67 |
|
2001 |
Alexander RW, Schimmel P. Domain-domain communication in aminoacyl-tRNA synthetases Progress in Nucleic Acid Research and Molecular Biology. 69: 317-349. PMID 11550797 DOI: 10.1016/S0079-6603(01)69050-0 |
0.735 |
|
2001 |
Lovato MA, Chihade JW, Schimmel P. Translocation within the acceptor helix of a major tRNA identity determinant. The Embo Journal. 20: 4846-53. PMID 11532948 DOI: 10.1093/Emboj/20.17.4846 |
0.801 |
|
2001 |
Nomanbhoy TK, Schimmel P. Active site of an aminoacyl-tRNA synthetase dissected by energy-transfer-dependent fluorescence Bioorganic and Medicinal Chemistry Letters. 11: 1485-1491. PMID 11412966 DOI: 10.1016/S0960-894X(01)00127-5 |
0.481 |
|
2001 |
Fàbrega C, Farrow MA, Mukhopadhyay B, de Crécy-Lagard V, Ortiz AR, Schimmel P. An aminoacyl tRNA synthetase whose sequence fits into neither of the two known classes. Nature. 411: 110-4. PMID 11333988 DOI: 10.1038/35075121 |
0.502 |
|
2001 |
Döring V, Mootz HD, Nangle LA, Hendrickson TL, de Crécy-Lagard V, Schimmel P, Marlière P. Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway. Science (New York, N.Y.). 292: 501-4. PMID 11313495 DOI: 10.1126/Science.1057718 |
0.476 |
|
2001 |
Farrow MA, Schimmel P. Editing by a tRNA synthetase: DNA aptamer-induced translocation and hydrolysis of a misactivated amino acid. Biochemistry. 40: 4478-83. PMID 11284704 DOI: 10.1021/Bi0024052 |
0.434 |
|
2001 |
Nomanbhoy T, Morales AJ, Abraham AT, Vörtler CS, Giegé R, Schimmel P. Simultaneous binding of two proteins to opposite sides of a single transfer RNA. Nature Structural Biology. 8: 344-8. PMID 11276256 DOI: 10.1038/86228 |
0.453 |
|
2001 |
Ribas de Pouplana L, Schimmel P. Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem. Cell. 104: 191-3. PMID 11269237 DOI: 10.1016/S0092-8674(01)00204-5 |
0.599 |
|
2001 |
Ribas de Pouplana L, Schimmel P. Operational RNA code for amino acids in relation to genetic code in evolution. The Journal of Biological Chemistry. 276: 6881-4. PMID 11238440 DOI: 10.1074/Jbc.R000032200 |
0.653 |
|
2001 |
Kelley SO, Steinberg SV, Schimmel P. Fragile T-stem in Disease-associated Human Mitochondrial tRNA Sensitizes Structure to Local and Distant Mutations Journal of Biological Chemistry. 276: 10607-10611. PMID 11110797 DOI: 10.1074/Jbc.M008320200 |
0.388 |
|
2000 |
Sardesai NY, Stagg SM, Vanloock MS, Harvey SC, Schimmel P. RNA scaffolds for minihelix-based aminoacyl transfer: design of "transpeptizymes". Journal of Biomolecular Structure & Dynamics. 17: 29-37. PMID 22607404 DOI: 10.1080/07391102.2000.10506601 |
0.411 |
|
2000 |
Swairjo MA, Morales AJ, Wang CC, Ortiz AR, Schimmel P. Crystal structure of Trbp111: A structure-specific tRNA-binding protein Embo Journal. 19: 6287-6298. PMID 11101501 DOI: 10.1093/Emboj/19.23.6287 |
0.434 |
|
2000 |
Houman F, Rho SB, Zhang J, Shen X, Wang CC, Schimmel P, Martinis SA. A prokaryote and human tRNA synthetase provide an essential RNA splicing function in yeast mitochondria Proceedings of the National Academy of Sciences of the United States of America. 97: 13743-13748. PMID 11087829 DOI: 10.1073/Pnas.240465597 |
0.42 |
|
2000 |
Chihade JW, Brown JR, Schimmel PR, Ribas De Pouplana L. Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 97: 12153-7. PMID 11035802 DOI: 10.1073/Pnas.220388797 |
0.781 |
|
2000 |
Kelley SO, Steinberg SV, Schimmel P. Functional defects of pathogenic human mitochondrial tRNAs related to structural fragility Nature Structural Biology. 7: 862-865. PMID 11017193 DOI: 10.1038/79612 |
0.418 |
|
2000 |
Ribas de Pouplana L, Schimmel P. A view into the origin of life: aminoacyl-tRNA synthetases. Cellular and Molecular Life Sciences : Cmls. 57: 865-70. PMID 10950302 DOI: 10.1007/Pl00000729 |
0.609 |
|
2000 |
Hendrickson TL, Nomanbhoy TK, Schimmel P. Errors from selective disruption of the editing center in a tRNA synthetase Biochemistry. 39: 8180-8186. PMID 10889024 DOI: 10.1021/Bi0004798 |
0.455 |
|
2000 |
Turner RJ, Lovato M, Schimmel P. One of two genes encoding glycyl-tRNA synthetase in Saccharomyces cerevisiae provides mitochondrial and cytoplasmic functions Journal of Biological Chemistry. 275: 27681-27688. PMID 10874035 DOI: 10.1074/Jbc.M003416200 |
0.8 |
|
2000 |
Schimmel P, Ribas De Pouplana L. Footprints of aminoacyl-tRNA synthetases are everywhere. Trends in Biochemical Sciences. 25: 207-9. PMID 10782085 DOI: 10.1016/S0968-0004(00)01553-X |
0.693 |
|
2000 |
Wang CC, Morales AJ, Schimmel P. Functional redundancy in the nonspecific RNA binding domain of a class I tRNA synthetase Journal of Biological Chemistry. 275: 17180-17186. PMID 10747983 DOI: 10.1074/Jbc.M001057200 |
0.444 |
|
2000 |
Schimmel P, Kelley SO. Exiting an RNA world Nature Structural Biology. 7: 5-7. PMID 10625414 DOI: 10.1038/71194 |
0.393 |
|
1999 |
Farrow MA, Nordin BE, Schimmel P. Nucleotide determinants for tRNA-dependent amino acid discrimination by a class I tRNA synthetase. Biochemistry. 38: 16898-903. PMID 10606524 DOI: 10.1021/Bi9920782 |
0.683 |
|
1999 |
Alexander RW, Schimmel P. Evidence for breaking domain-domain functional communication in a synthetase-tRNA complex Biochemistry. 38: 16359-16365. PMID 10587461 DOI: 10.1021/Bi991948C |
0.728 |
|
1999 |
Steer BA, Schimmel P. Major anticodon-binding region missing from an archaebacterial tRNA synthetase Journal of Biological Chemistry. 274: 35601-35606. PMID 10585437 DOI: 10.1074/Jbc.274.50.35601 |
0.461 |
|
1999 |
Steer BA, Schimmel P. Domain-domain communication in a miniature archaebacterial tRNA synthetase Proceedings of the National Academy of Sciences of the United States of America. 96: 13644-13649. PMID 10570126 DOI: 10.1073/Pnas.96.24.13644 |
0.345 |
|
1999 |
Nomanbhoy TK, Hendrickson TL, Schimmel P. Transfer RNA-dependent translocation of misactivated amino acids to prevent errors in protein synthesis Molecular Cell. 4: 519-528. PMID 10549284 DOI: 10.1016/S1097-2765(00)80203-8 |
0.456 |
|
1999 |
Chihade JW, 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. 96: 12316-12321. PMID 10535919 DOI: 10.1073/Pnas.96.22.12316 |
0.806 |
|
1999 |
Sardesai NY, Green R, Schimmel P. Efficient 50S ribosome-catalyzed peptide bond synthesis with an aminoacyl minihelix Biochemistry. 38: 12080-12088. PMID 10508412 DOI: 10.1021/Bi991126F |
0.434 |
|
1999 |
Wakasugi K, Schimmel P. Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase Journal of Biological Chemistry. 274: 23155-23159. PMID 10438485 DOI: 10.1074/Jbc.274.33.23155 |
0.357 |
|
1999 |
Morales AJ, Swairjo MA, Schimmel P. Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus Embo Journal. 18: 3475-3483. PMID 10369686 DOI: 10.1093/Emboj/18.12.3475 |
0.471 |
|
1999 |
Wang CC, Schimmel P. Species barrier to RNA recognition overcome with nonspecific RNA binding domains Journal of Biological Chemistry. 274: 16508-16512. PMID 10347214 DOI: 10.1074/Jbc.274.23.16508 |
0.466 |
|
1999 |
Schimmel P, Wang CC. Getting tRNA synthetases into the nucleus Trends in Biochemical Sciences. 24: 127-128. PMID 10322413 DOI: 10.1016/S0968-0004(99)01369-9 |
0.327 |
|
1999 |
Steer BA, Schimmel P. Different adaptations of the same peptide motif for tRNA functional contacts by closely homologous tRNA synthetases Biochemistry. 38: 4965-4971. PMID 10213598 DOI: 10.1021/Bi990038S |
0.465 |
|
1999 |
Wakasugi K, Schimmel P. Two distinct cytokines released from a human aminoacyl-tRNA synthetase Science. 284: 147-151. PMID 10102815 DOI: 10.1126/Science.284.5411.147 |
0.422 |
|
1999 |
Nordin BE, Schimmel P. RNA determinants for translational editing. Mischarging a minihelix substrate by a tRNA synthetase. The Journal of Biological Chemistry. 274: 6835-8. PMID 10066735 DOI: 10.1074/Jbc.274.11.6835 |
0.711 |
|
1999 |
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. 96: 327-8. PMID 9892630 DOI: 10.1073/Pnas.96.2.327 |
0.6 |
|
1999 |
Musier-Forsyth K, Schimmel P. Atomic determinants for aminoacylation of RNA minihelices and relationship to genetic code Accounts of Chemical Research. 32: 368-375. DOI: 10.1021/Ar970148W |
0.677 |
|
1999 |
Schimmel P. Bringing RNA back to the future Trends in Biochemical Sciences. 24: 408-409. DOI: 10.1016/S0968-0004(99)01415-2 |
0.34 |
|
1998 |
Alexander RW, Nordin BE, Schimmel P. Activation of microhelix charging by localized helix destabilization. Proceedings of the National Academy of Sciences of the United States of America. 95: 12214-9. PMID 9770466 DOI: 10.1073/Pnas.95.21.12214 |
0.814 |
|
1998 |
Ribas de Pouplana L, Turner RJ, Steer BA, Schimmel P. Genetic code origins: tRNAs older than their synthetases? Proceedings of the National Academy of Sciences of the United States of America. 95: 11295-300. PMID 9736730 DOI: 10.1073/Pnas.95.19.11295 |
0.699 |
|
1998 |
Ribas de Pouplana L, Buechter D, Sardesai NY, Schimmel P. Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA-binding domains. The Embo Journal. 17: 5449-57. PMID 9736622 DOI: 10.1093/Emboj/17.18.5449 |
0.695 |
|
1998 |
Schimmel P, Alexander R. Diverse RNA substrates for aminoacylation: clues to origins? Proceedings of the National Academy of Sciences of the United States of America. 95: 10351-10353. PMID 9724705 DOI: 10.1073/Pnas.95.18.10351 |
0.741 |
|
1998 |
Schimmel P, Alexander R. All You Need Is RNA Science. 281: 658-659. PMID 9714675 DOI: 10.1126/Science.281.5377.658 |
0.695 |
|
1998 |
Chihade JW, Hayashibara K, Shiba K, Schimmel P. Strong Selective Pressure To Use G:U To Mark an RNA Acceptor Stem for Alanine† Biochemistry. 37: 9193-9202. PMID 9636067 DOI: 10.1021/Bi9804636 |
0.783 |
|
1998 |
Nureki O, Vassylyev DG, Tateno M, Shimada A, Nakama T, Fukai S, Konno M, Hendrickson TL, Schimmel P, Yokoyama S. Enzyme structure with two catalytic sites for double-sieve selection of substrate. Science (New York, N.Y.). 280: 578-82. PMID 9554847 DOI: 10.1126/Science.280.5363.578 |
0.403 |
|
1998 |
Wakasugi K, Quinn CL, Tao N, Schimmel P. Genetic code in evolution: Switching species-specific aminoacylation with a peptide transplant Embo Journal. 17: 297-305. PMID 9427763 DOI: 10.1093/Emboj/17.1.297 |
0.438 |
|
1998 |
Henderson BS, Beuning PJ, Shi JP, Bald R, Furste JP, Erdmann VA, Musier-Forsyth K, Schimmel P. Subtle functional interactions in the RNA minor groove at a nonessential base pair [21] Journal of the American Chemical Society. 120: 9110-9111. DOI: 10.1021/Ja9809152 |
0.686 |
|
1998 |
Sardesai NY, Schimmel P. Noncovalent Assembly Of Microhelix Recognition By A Class Ii Trna Synthetase Journal of the American Chemical Society. 120: 3269-3270. DOI: 10.1021/Ja9742287 |
0.3 |
|
1997 |
Ribas de Pouplana L, Schimmel P. Reconstruction of quaternary structures of class II tRNA synthetases by rational mutagenensis of a conserved domain. Biochemistry. 36: 15041-8. PMID 9398230 DOI: 10.1021/Bi971788+ |
0.655 |
|
1997 |
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. 94: 11291-11294. PMID 9326602 DOI: 10.1073/Pnas.94.21.11291 |
0.357 |
|
1997 |
Beuning PJ, 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. 94: 10150-10154. PMID 9294178 DOI: 10.1073/Pnas.94.19.10150 |
0.739 |
|
1997 |
Schimmel P, Söll D. When protein engineering confronts the tRNA world. Proceedings of the National Academy of Sciences of the United States of America. 94: 10007-10009. PMID 9294151 DOI: 10.1073/Pnas.94.19.10007 |
0.343 |
|
1997 |
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. 272: 22809-22816. PMID 9278442 DOI: 10.1074/Jbc.272.36.22809 |
0.75 |
|
1997 |
Henderson BS, Schimmel P. RNA-RNA interactions between oligonucleotide substrates for aminoacylation. Bioorganic & Medicinal Chemistry. 5: 1071-9. PMID 9222500 DOI: 10.1016/S0968-0896(97)00043-6 |
0.408 |
|
1997 |
Nair S, Ribas de Pouplana L, Houman F, Avruch A, Shen X, Schimmel P. Species-specific tRNA recognition in relation to tRNA synthetase contact residues. Journal of Molecular Biology. 269: 1-9. PMID 9192996 DOI: 10.1006/Jmbi.1997.1025 |
0.67 |
|
1997 |
Whelihan EF, Schimmel P. Rescuing an essential enzyme–RNA complex with a non‐essential appended domain The Embo Journal. 16: 2968-2974. PMID 9184240 DOI: 10.1093/Emboj/16.10.2968 |
0.409 |
|
1997 |
Glasfeld E, Schimmel P. Zinc-Dependent tRNA Binding by a Peptide Element within a tRNA Synthetase† Biochemistry. 36: 6739-6744. PMID 9184155 DOI: 10.1021/Bi970151N |
0.4 |
|
1997 |
Hale SP, Auld DS, Schmidt E, Schimmel P. Discrete determinants in transfer RNA for editing and aminoacylation. Science (New York, N.Y.). 276: 1250-2. PMID 9157882 DOI: 10.1126/Science.276.5316.1250 |
0.471 |
|
1997 |
Hale SP, Schimmel P. Dna Aptamer Targets Translational Editing Motif In A Trna Synthetase Tetrahedron. 53: 11985-11994. DOI: 10.1016/S0040-4020(97)00711-4 |
0.423 |
|
1996 |
Michaels JA, Schimmel P, Shiba K, Miller WT. Dominant negative inhibition by fragments of a monomeric enzyme Proceedings of the National Academy of Sciences of the United States of America. 93: 14452-14455. PMID 8962072 DOI: 10.1073/Pnas.93.25.14452 |
0.39 |
|
1996 |
Schimmel P, Musler-Forsyth K, Ibba M, Soll D. 'Distorted' RNA helix recognition [13] Nature. 384: 422. PMID 8945467 DOI: 10.1038/384422A0 |
0.362 |
|
1996 |
Gale AJ, Schimmel P. Affinity coelectrophoresis for dissecting protein-RNA domain-domain interactions in a tRNA synthetase system. Pharmaceutica Acta Helvetiae. 71: 45-50. PMID 8786999 DOI: 10.1016/0031-6865(95)00046-1 |
0.449 |
|
1996 |
Sassanfar M, Kranz JE, Gallant P, Schimmel P, Shiba K. A eubacterial Mycobacterium tuberculosis tRNA synthetase is eukaryote-like and resistant to a eubacterial-specific antisynthetase drug. Biochemistry. 35: 9995-10003. PMID 8756461 DOI: 10.1021/Bi9603027 |
0.349 |
|
1996 |
Ribas de Pouplana L, Auld DS, Kim S, Schimmel P. A mechanism for reducing entropic cost of induced fit in protein--RNA recognition. Biochemistry. 35: 8095-102. PMID 8679560 DOI: 10.1021/Bi960256A |
0.652 |
|
1996 |
Glasfeld E, Landro JA, Schimmel P. C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetase. Biochemistry. 35: 4139-4145. PMID 8672449 DOI: 10.1021/Bi9527810 |
0.455 |
|
1996 |
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. 93: 4521-4522. PMID 8643435 DOI: 10.1073/Pnas.93.10.4521 |
0.338 |
|
1996 |
Lin L, Schimmel P. Mutational analysis suggests the same design for editing activities of two tRNA synthetases. Biochemistry. 35: 5596-5601. PMID 8611551 DOI: 10.1021/Bi960011Y |
0.424 |
|
1996 |
Hale SP, Schimmel P. Protein synthesis editing by a DNA aptamer. Proceedings of the National Academy of Sciences of the United States of America. 93: 2755-2758. PMID 8610114 DOI: 10.1073/Pnas.93.7.2755 |
0.466 |
|
1996 |
Gale AJ, Shi J, Schimmel P. Evidence that Specificity of Microhelix Charging by a Class I tRNA Synthetase Occurs in the Transition State of Catalysis Biochemistry. 35: 608-615. PMID 8555234 DOI: 10.1021/Bi9520904 |
0.431 |
|
1996 |
Ribas de Pouplana L, Frugier M, Quinn CL, 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. 93: 166-70. PMID 8552597 DOI: 10.1073/Pnas.93.1.166 |
0.671 |
|
1995 |
Schimmel P, Schmidt E. Making connections: RNA-dependent amino acid recognition Trends in Biochemical Sciences. 20: 1-2. PMID 7878729 DOI: 10.1016/S0968-0004(00)88937-9 |
0.397 |
|
1995 |
Schimmel P. An operational RNA code for amino acids and variations in critical nucleotide sequences in evolution. Journal of Molecular Evolution. 40: 531-536. PMID 7783226 DOI: 10.1007/Bf00166621 |
0.481 |
|
1995 |
Ripmaster TL, 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. 92: 4932-4936. PMID 7761427 DOI: 10.1073/Pnas.92.11.4932 |
0.463 |
|
1995 |
Buechter DD, Schimmel P. Minor Groove Recognition Of The Critical Acceptor Helix Base Pair By An Appended Module Of A Class Ii Trna Synthetase Biochemistry. 34: 6014-6019. PMID 7742303 DOI: 10.1021/Bi00018A002 |
0.434 |
|
1995 |
Auld DS, Schimmel P. Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptide. Science (New York, N.Y.). 267: 1994-6. PMID 7701322 DOI: 10.1126/Science.7701322 |
0.425 |
|
1995 |
Schmidt E, Schimmel P. Residues in a class I tRNA synthetase which determine selectivity of amino acid recognition in the context of tRNA Biochemistry. 34: 11204-11210. PMID 7669778 DOI: 10.1021/Bi00035A028 |
0.416 |
|
1995 |
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. 34: 10340-10349. PMID 7654687 DOI: 10.1021/Bi00033A004 |
0.465 |
|
1995 |
Kirkpatrick CR, Schimmel P. Detection of leucine-independent DNA site occupancy of the yeast Leu3p transcriptional activator in vivo. Molecular and Cellular Biology. 15: 4021-4030. PMID 7623798 DOI: 10.1128/Mcb.15.8.4021 |
0.32 |
|
1995 |
Gale AJ, Schimmel P. Isolated RNA binding domain of a class I tRNA synthetase. Biochemistry. 34: 8896-8903. PMID 7612631 DOI: 10.1021/Bi00027A042 |
0.466 |
|
1995 |
Schimmel P, Ribas de Pouplana L. Transfer RNA: from minihelix to genetic code. Cell. 81: 983-6. PMID 7600584 DOI: 10.1016/S0092-8674(05)80002-9 |
0.642 |
|
1995 |
Quinn CL, Tao N, Schimmel P. Species-Specific Microhelix Aminoacylation By A Eukaryotic Pathogen Trna Synthetase Dependent On A Single Base Pair Biochemistry. 34: 12489-12495. PMID 7547995 DOI: 10.1021/Bi00039A001 |
0.44 |
|
1995 |
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. 92: 5550-5552. PMID 7539919 DOI: 10.1073/Pnas.92.12.5550 |
0.491 |
|
1995 |
Schimmel P, Ripmaster T. Modular design of components of the operational RNA code for alanine in evolution Trends in Biochemical Sciences. 20: 333-334. PMID 7482695 DOI: 10.1016/S0968-0004(00)89067-2 |
0.334 |
|
1995 |
Musier-Forsyth K, Shi J-, Henderson B, Bald R, Fuerste JP, Erdmann VA, Schimmel P. Base-analog-induced aminoacylation of an RNA helix by a tRNA synthetase Journal of the American Chemical Society. 117: 7253-7254. DOI: 10.1021/Ja00132A029 |
0.717 |
|
1995 |
Hipps D, Schimmel P. Cell growth inhibition by sequence-specific RNA minihelices. The Embo Journal. 14: 4050-4055. DOI: 10.1002/J.1460-2075.1995.Tb00076.X |
0.472 |
|
1994 |
Musier-Forsyth K, Schimmel P. Acceptor helix interactions in a class II tRNA synthetase: photoaffinity cross-linking of an RNA miniduplex substrate. Biochemistry. 33: 773-779. PMID 8292605 DOI: 10.1021/Bi00169A019 |
0.743 |
|
1994 |
Frugier M, Florentz C, Schimmel P, Giegé R. Triple aminoacylation specificity of a chimerized transfer RNA. Biochemistry. 32: 14053-61. PMID 8268184 DOI: 10.1021/Bi00213A039 |
0.441 |
|
1994 |
Shi J, 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. 33: 5312-5318. PMID 8172905 DOI: 10.1021/Bi00183A039 |
0.757 |
|
1994 |
Schmidt E, Schimmel P. Mutational isolation of a sieve for editing in a transfer RNA synthetase Science. 264: 265-267. PMID 8146659 DOI: 10.1126/Science.8146659 |
0.489 |
|
1994 |
Davis MW, Buechter DD, Schimmel P. Functional dissection of a predicted class-defining motif in a class II tRNA synthetase of unknown structure. Biochemistry. 33: 9904-9911. PMID 8060998 DOI: 10.1021/Bi00199A012 |
0.427 |
|
1994 |
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. 91: 7435-7439. PMID 8052601 DOI: 10.1073/Pnas.91.16.7435 |
0.457 |
|
1994 |
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. 91: 11283-11286. PMID 7972050 DOI: 10.1073/Pnas.91.24.11283 |
0.34 |
|
1994 |
Landro JA, Schmidt E, Schimmel P, Tierney DL, Penner-Hahn JE. Thiol ligation of two zinc atoms to a class I tRNA synthetase: evidence for unshared thiols and role in amino acid binding and utilization. Biochemistry. 33: 14213-20. PMID 7947832 DOI: 10.1021/Bi00251A033 |
0.45 |
|
1994 |
Kim S, Ribas de Pouplana L, Schimmel P. An RNA binding site in a tRNA synthetase with a reduced set of amino acids. Biochemistry. 33: 11040-5. PMID 7522052 DOI: 10.1021/Bi00202A025 |
0.707 |
|
1993 |
Buechter DD, Schimmel P. Dissection of a class II tRNA synthetase: determinants for minihelix recognition are tightly associated with domain for amino acid activation. Biochemistry. 32: 5267-5272. PMID 8494904 DOI: 10.1021/Bi00070A039 |
0.492 |
|
1993 |
Landro JA, 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. 90: 2261-2265. PMID 8460131 DOI: 10.1073/Pnas.90.6.2261 |
0.425 |
|
1993 |
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. 90: 6919-6923. PMID 8346197 DOI: 10.1073/Pnas.90.15.6919 |
0.411 |
|
1993 |
Ribas de Pouplana L, Buechter DD, Davis MW, Schimmel P. Idiographic representation of conserved domain of a class II tRNA synthetase of unknown structure. Protein Science : a Publication of the Protein Society. 2: 2259-62. PMID 8298469 DOI: 10.1002/Pro.5560021225 |
0.64 |
|
1993 |
Kim S, Landro JA, Gale AJ, Schimmel P. C-terminal peptide appendix in a class I tRNA synthetase needed for acceptor-helix contacts and microhelix aminoacylation. Biochemistry. 32: 13026-13031. PMID 8241156 DOI: 10.1021/Bi00211A011 |
0.45 |
|
1993 |
Wright DJ, Martinis SA, Jahn M, Söll D, Schimmel P. Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase Biochimie. 75: 1041-1049. PMID 8199240 DOI: 10.1016/0300-9084(93)90003-B |
0.394 |
|
1993 |
Schimmel P, Landro JA, Schmidt E. Evidence for distinct locations for metal binding sites in two closely related class i trna synthetases Journal of Biomolecular Structure and Dynamics. 11: 571-581. PMID 8129874 DOI: 10.1080/07391102.1993.10508016 |
0.419 |
|
1993 |
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. 90: 10046-50. PMID 7694278 DOI: 10.1073/Pnas.90.21.10046 |
0.703 |
|
1993 |
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. 90: 8763-8768. PMID 7692438 DOI: 10.1073/Pnas.90.19.8763 |
0.485 |
|
1993 |
Musier-Forsyth K, Schimmel P. Aminoacylation of RNA oligonucleotides: minimalist structures and origin of specificity. The Faseb Journal. 7: 282-289. PMID 7680012 DOI: 10.1096/Fasebj.7.2.7680012 |
0.733 |
|
1993 |
Landro JA, Schimmel P. Non-covalent protein assembly Current Opinion in Structural Biology. 3: 549-554. DOI: 10.1016/0959-440X(93)90082-V |
0.398 |
|
1992 |
Martinis SA, 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. 89: 65-69. PMID 1729719 DOI: 10.1073/Pnas.89.1.65 |
0.492 |
|
1992 |
Musier-Forsyth K, Schimmel P. Functional contacts of a transfer RNA synthetase with 2′-hydroxyl groups in the RNA minor groove Nature. 357: 513-515. PMID 1608452 DOI: 10.1038/357513A0 |
0.711 |
|
1992 |
Shi JP, Martinis SA, Schimmel P. RNA tetraloops as minimalist substrates for aminoacylation Biochemistry. 31: 4931-4936. PMID 1599917 DOI: 10.1021/Bi00136A002 |
0.485 |
|
1992 |
Hou YM, Schimmel P. Novel transfer RNAs that are active in Escherichia coli. Biochemistry. 31: 4157-4160. PMID 1567861 DOI: 10.1021/Bi00132A001 |
0.473 |
|
1992 |
Miller WT, 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. 89: 2032-2035. PMID 1549561 DOI: 10.1073/Pnas.89.6.2032 |
0.532 |
|
1992 |
Francklyn C, Shi J, Schimmel P. Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices Science. 255: 1121-1125. PMID 1546312 DOI: 10.1126/Science.1546312 |
0.482 |
|
1992 |
Shiba K, Schimmel P. Functional assembly of a randomly cleaved protein. Proceedings of the National Academy of Sciences of the United States of America. 89: 1880-1884. PMID 1542687 DOI: 10.1073/Pnas.89.5.1880 |
0.374 |
|
1992 |
Hou YM, Schimmel P. Functional compensation of a recognition-defective transfer RNA by a distal base pair substitution. Biochemistry. 31: 10310-10314. PMID 1420150 DOI: 10.1021/Bi00157A019 |
0.414 |
|
1992 |
Miller WT, Schimmel P. A metal-binding motif implicated in RNA recognition by an aminoacyl-tRNA synthetase and by a retroviral gene product. Molecular Microbiology. 6: 1259-1262. PMID 1379318 DOI: 10.1111/J.1365-2958.1992.Tb00846.X |
0.505 |
|
1992 |
Francklyn C, Musier-Forsyth K, Schimmel P. Small RNA helices as substrates for aminoacylation and their relationship to charging of transfer RNAs. Febs Journal. 206: 315-321. PMID 1375910 DOI: 10.1111/J.1432-1033.1992.Tb16929.X |
0.725 |
|
1992 |
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. 89: 9964-9968. PMID 1329109 DOI: 10.1073/Pnas.89.20.9964 |
0.501 |
|
1992 |
Burbaum JJ, Schimmel P. Amino acid binding by the Class I aminoacyl‐tRNA synthetases: Role for a conserved proline in the signature sequence Protein Science. 1: 575-581. PMID 1304356 DOI: 10.1002/Pro.5560010503 |
0.813 |
|
1992 |
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. 1: 1387-1391. PMID 1303756 DOI: 10.1002/Pro.5560011018 |
0.332 |
|
1991 |
Yi T, Walsh K, Schimmel P. Rabbit muscle creatine kinase: genomic cloning, sequencing, and analysis of upstream sequences important for expression in myocytes. Nucleic Acids Research. 19: 3027-3033. PMID 2057360 DOI: 10.1093/Nar/19.11.3027 |
0.317 |
|
1991 |
Schimmel P. Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code. Trends in Biochemical Sciences. 16: 1-3. PMID 2053131 DOI: 10.1016/0968-0004(91)90002-D |
0.343 |
|
1991 |
Schimmel P. RNA minihelices and the decoding of genetic information. The Faseb Journal. 5: 2180-2187. PMID 2022314 DOI: 10.1096/Fasebj.5.8.2022314 |
0.394 |
|
1991 |
Trézéguet 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. 11: 2744-2751. PMID 2017176 DOI: 10.1128/Mcb.11.5.2744 |
0.389 |
|
1991 |
Miller WT, Hou Y, Schimmel P. Mutant aminoacyl-tRNA synthetase that compensates for a mutation in the major identity determinant of its tRNA. Biochemistry. 30: 2635-2641. PMID 2001352 DOI: 10.1021/Bi00224A011 |
0.572 |
|
1991 |
Edwards H, Trézéguet 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. 88: 1153-1156. PMID 1996316 DOI: 10.1073/Pnas.88.4.1153 |
0.468 |
|
1991 |
Hou YM, 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. 88: 976-980. PMID 1992490 DOI: 10.1073/Pnas.88.3.976 |
0.45 |
|
1991 |
Burbaum JJ, Schimmel P. Assembly of a class I tRNA synthetase from products of an artificially split gene. Biochemistry. 30: 319-324. PMID 1988033 DOI: 10.1021/Bi00216A002 |
0.829 |
|
1991 |
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. 88: 209-213. PMID 1986368 DOI: 10.1073/Pnas.88.1.209 |
0.707 |
|
1991 |
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 (New York, N.Y.). 253: 784-6. PMID 1876835 DOI: 10.1126/Science.1876835 |
0.718 |
|
1991 |
Schimmel P, Burbaum JJ. [25] Transfer RNA with double identity for in Vitro kinetic modeling of transfer RNA identity in Vivo Methods in Enzymology. 203: 485-500. PMID 1762569 DOI: 10.1016/0076-6879(91)03027-E |
0.83 |
|
1991 |
Miller WT, Hill KA, Schimmel P. Evidence for a "cysteine-histidine box" metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase. Biochemistry. 30: 6970-6. PMID 1712632 DOI: 10.1021/Bi00242A023 |
0.563 |
|
1991 |
Schimmel P. Mutant enzymes and dissected tRNAs that elucidate motifs for protein-RNA recognition Current Opinion in Structural Biology. 1: 811-816. DOI: 10.1016/0959-440X(91)90183-T |
0.48 |
|
1990 |
Ch'ng JL, Mulligan RC, Schimmel P, Holmes EW. 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. 86: 10006-10. PMID 2481308 DOI: 10.1073/Pnas.86.24.10006 |
0.361 |
|
1990 |
Schimmel P. Alanine transfer RNA synthetase: structure-function relationships and molecular recognition of transfer RNA. Advances in Enzymology and Related Areas of Molecular Biology. 63: 233-270. PMID 2407064 DOI: 10.1002/9780470123096.Ch4 |
0.372 |
|
1990 |
Ch'ng JLC, Shoemaker DL, Schimmel P, Holmes EW. Reversal of creatine kinase translational repression by 3' untranslated sequences. Science. 248: 1003-1006. PMID 2343304 DOI: 10.1126/Science.2343304 |
0.319 |
|
1990 |
Park SJ, Miller WT, Schimmel P. Synthetic peptide model of an essential region of an aminoacyl-tRNA synthetase. Biochemistry. 29: 9212-9218. PMID 2271589 DOI: 10.1021/Bi00491A015 |
0.531 |
|
1990 |
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. 87: 8655-8659. PMID 2236077 DOI: 10.1073/Pnas.87.21.8655 |
0.431 |
|
1990 |
Hill K, Schimmel P. The dissection and engineering of sites that affect the activity of an enzyme of unknown structure. Biotechnology(Faisalabad). 14: 65-79. PMID 2183901 DOI: 10.1016/B978-0-409-90116-0.50012-1 |
0.322 |
|
1990 |
Burbaum JJ, Starzyk RM, Schimmel P. Understanding structural relationships proteins of unsolved three‐dimensional structure Proteins. 7: 99-111. PMID 2183216 DOI: 10.1002/Prot.340070202 |
0.796 |
|
1990 |
Shi JP, Francklyn C, Hill K, Schimmel P. A nucleotide that enhances the charging of RNA minihelix sequence variants with alanine. Biochemistry. 29: 3621-3626. PMID 1692733 DOI: 10.1021/Bi00467A005 |
0.438 |
|
1990 |
Edwards H, Schimmel P. A bacterial amber suppressor in Saccharomyces cerevisiae is selectively recognized by a bacterial aminoacyl-tRNA synthetase. Molecular and Cellular Biology. 10: 1633-1641. PMID 1690848 DOI: 10.1128/Mcb.10.4.1633 |
0.445 |
|
1990 |
Francklyn CS, Schimmel P. Synthetic RNA molecules as substrates for enzymes that act on tRNAs and tRNA-like molecules Chemical Reviews. 90: 1327-1342. DOI: 10.1021/Cr00105A013 |
0.401 |
|
1989 |
Francklyn C, Schimmel P. Aminoacylation of RNA minihelices with alanine Nature. 337: 478-481. PMID 2915692 DOI: 10.1038/337478A0 |
0.49 |
|
1989 |
Starzyk RM, Burbaum JJ, Schimmel P. Insertion of new sequences into the catalytic domain of an enzyme. Biochemistry. 28: 8479-8484. PMID 2690943 DOI: 10.1021/Bi00447A031 |
0.811 |
|
1989 |
Starzyk RM, Schimmel P. Construction of intra-domain chimeras of aminoacyl-tRNA synthetases. Journal of Biomolecular Structure & Dynamics. 7: 225-234. PMID 2690866 DOI: 10.1080/07391102.1989.10507767 |
0.398 |
|
1989 |
Hou YM, Schimmel P. Evidence that a major determinant for the identity of a transfer RNA is conserved in evolution Biochemistry. 28: 6800-6804. PMID 2684266 DOI: 10.1021/Bi00443A003 |
0.435 |
|
1989 |
Friden P, Reynolds C, Schimmel P. A large internal deletion converts yeast LEU3 to a constitutive transcriptional activator. Molecular and Cellular Biology. 9: 4056-4060. PMID 2674686 DOI: 10.1128/Mcb.9.9.4056 |
0.386 |
|
1989 |
Hou Y, Francklyn C, Schimmel P. Molecular dissection of a transfer RNA and the basis for its identity. Trends in Biochemical Sciences. 14: 233-237. PMID 2669241 DOI: 10.1016/0968-0004(89)90033-9 |
0.469 |
|
1989 |
Schimmel P. Parameters for the molecular recognition of transfer RNAs. Biochemistry. 28: 2747-2759. PMID 2663057 DOI: 10.1021/Bi00433A001 |
0.335 |
|
1989 |
Park SJ, Hou YM, Schimmel P. A single base pair affects binding and catalytic parameters in the molecular recognition of a transfer RNA. Biochemistry. 28: 2740-2746. PMID 2659081 DOI: 10.1021/Bi00432A056 |
0.407 |
|
1989 |
Hou YM, Schimmel P. Modeling with in vitro kinetic parameters for the elaboration of transfer RNA identity in vivo. Biochemistry. 28: 4942-4947. PMID 2548595 DOI: 10.1021/Bi00438A005 |
0.422 |
|
1989 |
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. 28: 2577-2586. PMID 2543446 DOI: 10.1021/Bi00432A035 |
0.46 |
|
1988 |
Hou Y, Schimmel P. A simple structural feature is a major determinant of the identity of a transfer RNA Nature. 333: 140-145. PMID 3285220 DOI: 10.1038/333140A0 |
0.438 |
|
1988 |
Clarke ND, Lien DC, Schimmel P. Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure Science. 240: 521-523. PMID 3282306 DOI: 10.1126/Science.3282306 |
0.432 |
|
1988 |
Regan L, Buxbaum L, Hill K, Schimmel P. Rationale for engineering an enzyme by introducing a mutation that compensates for a deletion. The Journal of Biological Chemistry. 263: 18598-600. PMID 3198590 |
0.528 |
|
1988 |
Profy AT, 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. 35: 1-26. PMID 3065821 DOI: 10.1016/S0079-6603(08)60608-X |
0.405 |
|
1988 |
Frederick CA, Wang AH, Rich A, Regan L, Schimmel P. Crystallization of a small fragment of an aminoacyl tRNA synthetase. Journal of Molecular Biology. 203: 521-2. PMID 3058989 DOI: 10.1016/0022-2836(88)90019-8 |
0.563 |
|
1988 |
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. 8: 2690-2697. PMID 3043190 DOI: 10.1128/Mcb.8.7.2690 |
0.385 |
|
1987 |
Edwards H, Schimmel P. An E. coli aminoacyl-tRNA synthetase can substitute for yeast mitochondrial enzyme function in vivo Cell. 51: 643-649. PMID 3315228 DOI: 10.1016/0092-8674(87)90133-4 |
0.382 |
|
1987 |
Starzyk RM, Webster TA, Schimmel P. Evidence for dispensable sequences inserted into a nucleotide fold Science. 237: 1614-1618. PMID 3306924 DOI: 10.1126/Science.3306924 |
0.467 |
|
1987 |
Schimmel P. Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annual Review of Biochemistry. 56: 125-158. PMID 3304131 DOI: 10.1146/Annurev.Bi.56.070187.001013 |
0.4 |
|
1987 |
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. 7: 2708-2717. PMID 2823102 DOI: 10.1128/Mcb.7.8.2708 |
0.435 |
|
1987 |
Regan L, Bowie J, Schimmel P. Polypeptide sequences essential for RNA recognition by an enzyme. Science (New York, N.Y.). 235: 1651-3. PMID 2435005 DOI: 10.1126/Science.2435005 |
0.668 |
|
1987 |
Schimmel P. Biological macromolecules and assemblies. Volume 3: Active sites of enzymes Cell. 51: 517-518. DOI: 10.1016/0092-8674(87)90119-X |
0.304 |
|
1986 |
Drain P, Schimmel P. Yeast LEU5 is a PET-like gene that is not essential for leucine biosynthesis. Molecular Genetics and Genomics. 204: 397-403. PMID 3020377 DOI: 10.1007/Bf00331015 |
0.339 |
|
1986 |
Regan L, Dignam JD, Schimmel P. A bacterial and silkworm aminoacyl-tRNA synthetase have a common epitope which maps to the catalytic domain of each. The Journal of Biological Chemistry. 261: 5241-4. PMID 2420799 |
0.546 |
|
1985 |
Ho C, Jasin M, Schimmel P. Amino acid replacements that compensate for a large polypeptide deletion in an enzyme. Science (New York, N.Y.). 229: 389-93. PMID 3892692 DOI: 10.1126/Science.3892692 |
0.645 |
|
1985 |
Jasin M, Regan L, Schimmel P. Two mutations in the dispensable part of alanine tRNA synthetase which affect the catalytic activity. The Journal of Biological Chemistry. 260: 2226-30. PMID 3882689 |
0.534 |
|
1985 |
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. 82: 339-42. PMID 3881761 DOI: 10.1073/Pnas.82.2.339 |
0.436 |
|
1985 |
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. 82: 2310-4. PMID 3857581 DOI: 10.1073/Pnas.82.8.2310 |
0.332 |
|
1985 |
Ludmerer SW, Schimmel P. Cloning of GLN4: an essential gene that encodes glutaminyl-tRNA synthetase in Saccharomyces cerevisiae. Journal of Bacteriology. 163: 763-768. PMID 2991203 DOI: 10.1128/Jb.163.2.763-768.1985 |
0.367 |
|
1984 |
Webster T, Tsai H, Kula M, Mackie GA, Schimmel P. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase Science. 226: 1315-1317. PMID 6390679 DOI: 10.1126/Science.6390679 |
0.487 |
|
1984 |
Schimmel P, Jasin M, Regan L. Size polymorphism and the structure of aminoacyl-tRNA synthetases. Federation Proceedings. 43: 2987-90. PMID 6389183 |
0.556 |
|
1984 |
Jasin M, Regan L, Schimmel P. Dispensable pieces of an aminoacyl tRNA synthetase which activate the catalytic site. Cell. 36: 1089-95. PMID 6200234 DOI: 10.1016/0092-8674(84)90059-X |
0.708 |
|
1984 |
Jasin M, Schimmel P. Deletion of an essential gene in Escherichia coli by site-specific recombination with linear DNA fragments. Journal of Bacteriology. 159: 783-6. PMID 6086588 DOI: 10.1128/Jb.159.2.783-786.1984 |
0.534 |
|
1983 |
Putney SD, Herlihy WC, Schimmel P. A New Troponin T and cDNA Clones for 13 Different Muscle Proteins, Found by Shotgun Sequencing Nature. 302: 718-721. PMID 6687628 DOI: 10.1038/302718A0 |
0.301 |
|
1983 |
Jasin M, Regan L, Schimmel P. Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase. Nature. 306: 441-7. PMID 6358898 DOI: 10.1038/306441A0 |
0.708 |
|
1983 |
Keng T, Schimmel P. Synthesis of two polypeptide subunits of an aminoacyl tRNA synthetase as a single polypeptide chain. Journal of Biomolecular Structure & Dynamics. 1: 225-229. PMID 6086058 DOI: 10.1080/07391102.1983.10507436 |
0.392 |
|
1982 |
Starzyk RM, Koontz SW, Schimmel P. A covalent adduct between the uracil ring and the active site of an aminoacyl tRNA synthetase Nature. 298: 136-140. PMID 7045689 DOI: 10.1038/298136A0 |
0.421 |
|
1982 |
Andreadis A, Hsu Y, Kohlhaw GB, Schimmel P. Nucleotide sequence of yeast LEU2 shows 5'-noncoding region has sequences cognate to leucine Cell. 31: 319-325. PMID 6297759 DOI: 10.1016/0092-8674(82)90125-8 |
0.402 |
|
1982 |
Schimmel P, Putney S, Starzyk R. RNA and DNA sequence recognition and structure-function of aminoacyl tRNA synthetases Trends in Biochemical Sciences. 7: 209-212. DOI: 10.1016/0968-0004(82)90092-5 |
0.442 |
|
1981 |
Putney SD, Royal NJ, Neuman de Vegvar H, Herlihy WC, Biemann K, Schimmel P. Primary structure of a large aminoacyl-tRNA synthetase. Science (New York, N.Y.). 213: 1497-501. PMID 7025207 DOI: 10.1126/Science.7025207 |
0.357 |
|
1981 |
Putney SD, Schimmel P. An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription Nature. 291: 632-635. PMID 6264314 DOI: 10.1038/291632A0 |
0.363 |
|
1979 |
Schimmel PR. Recent results on how aminoacyl transfer RNA synthetases recognize specific transfer RNAs. Molecular and Cellular Biochemistry. 25: 3-14. PMID 381892 DOI: 10.1007/BF00211137 |
0.423 |
|
1979 |
Söll D, Abelson J, Schimmel P. Preface/Front Matter Cold Spring Harbor Monograph Archive. DOI: 10.1101/087969128.9A.I |
0.445 |
|
1977 |
Rich A, Schimmel PR. Structural organization of complexes of transfer RNAs with aminoacyl transfer RNA synthetases. Nucleic Acids Research. 4: 1649-65. PMID 331261 DOI: 10.1093/nar/4.5.1649 |
0.337 |
|
1975 |
Eldred E, Schimmel P. Corrections - Investigation of the Transfer of Amino Acid from a Transfer Ribonucleic Acid Synthetase-Aminoacyl Adenylate Complex to Transfer Ribonucleic Acid Biochemistry. 14: 196-196. DOI: 10.1021/Bi00672A600 |
0.323 |
|
1968 |
Schimmel PR, Flory PJ. Conformational energies and configurational statistics of copolypeptides containing L-proline. Journal of Molecular Biology. 34: 105-20. PMID 5760450 DOI: 10.1016/0022-2836(68)90237-4 |
0.413 |
|
1967 |
Flory PJ, Schimmel PR. Dipole moments in relation to configuration of polypeptide chains. Journal of the American Chemical Society. 89: 6807-13. PMID 6064350 DOI: 10.1021/Ja01002A001 |
0.366 |
|
1967 |
Hammes GG, Schimmel PR. Relaxation spectra of enzymatic reactions. The Journal of Physical Chemistry. 71: 917-23. PMID 6045206 DOI: 10.1021/J100863A023 |
0.55 |
|
1967 |
Brant DA, Schimmel PR. Analysis of the skeletal configuration of crystalline hen egg-white lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 58: 428-35. PMID 5233451 DOI: 10.1073/pnas.58.2.428 |
0.535 |
|
1967 |
Schimmel PR, Flory PJ. Conformational energy and configurational statistics of poly-L-proline. Proceedings of the National Academy of Sciences of the United States of America. 58: 52-9. PMID 5231619 DOI: 10.1073/Pnas.58.1.52 |
0.353 |
|
1965 |
Fasella P, Hammes GG, Schimmel PR. A Sephadex dialysis method of determining small molecule-macromolecule binding constants. Biochimica Et Biophysica Acta. 103: 708-10. PMID 5859855 DOI: 10.1016/0005-2787(65)90094-8 |
0.57 |
|
1965 |
Hammes GG, Schimmel PR. Equilibrium measurements of the binding of cytidine 3'-phosphate to ribonuclease. Journal of the American Chemical Society. 87: 4665-9. PMID 5844451 DOI: 10.1021/Ja00949A001 |
0.584 |
|
1965 |
Cathou RE, Hammes GG, Schimmel PR. Optical rotatory dispersion of ribonuclease and ribonuclease--nucleotide complexes. Biochemistry. 4: 2687-90. PMID 4286548 DOI: 10.1021/Bi00888A018 |
0.568 |
|
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