Year |
Citation |
Score |
2020 |
Zuo Y, De S, Feng Y, Steitz TA. Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation. Iscience. 23: 101445. PMID 32829286 DOI: 10.1016/J.Isci.2020.101445 |
0.432 |
|
2020 |
Lomakin IB, De S, Wang J, Borkar AN, Steitz TA. Crystal structure of the C-terminal domain of DENR. Computational and Structural Biotechnology Journal. 18: 696-704. PMID 32257053 DOI: 10.1016/J.Csbj.2020.03.009 |
0.461 |
|
2020 |
Joseph NN, Roy RN, Steitz TA. Molecular dynamics analysis of Mg -dependent cleavage of a pistol ribozyme reveals a fail-safe secondary ion for catalysis. Journal of Computational Chemistry. PMID 32091136 DOI: 10.1002/Jcc.26179 |
0.782 |
|
2018 |
Lomakin IB, Dmitriev SE, Steitz TA. Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation. Proceedings of the National Academy of Sciences of the United States of America. PMID 30584092 DOI: 10.2210/Pdb6Ms4/Pdb |
0.473 |
|
2018 |
Lin J, Zhou D, Steitz TA, Polikanov YS, Gagnon MG. Ribosome-Targeting Antibiotics: Modes of Action, Mechanisms of Resistance, and Implications for Drug Design. Annual Review of Biochemistry. PMID 29570352 DOI: 10.1146/Annurev-Biochem-062917-011942 |
0.307 |
|
2017 |
Liu B, Hong C, Huang RK, Yu Z, Steitz TA. Structural basis of bacterial transcription activation. Science (New York, N.Y.). 358: 947-951. PMID 29146813 DOI: 10.1126/Science.Aao1923 |
0.479 |
|
2017 |
Vaidya AT, Lomakin IB, Joseph NN, Dmitriev SE, Steitz TA. Crystal Structure of the C-terminal Domain of Human eIF2D and its Implications on Eukaryotic Translation Initiation. Journal of Molecular Biology. PMID 28736176 DOI: 10.1016/J.Jmb.2017.07.015 |
0.409 |
|
2017 |
Lomakin IB, Stolboushkina EA, Vaidya AT, Zhao C, Garber MB, Dmitriev SE, Steitz TA. Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1. Cell Reports. 20: 521-528. PMID 28723557 DOI: 10.1016/J.Celrep.2017.06.025 |
0.475 |
|
2017 |
Nguyen LA, Wang J, Steitz TA. Crystal structure of Pistol, a class of self-cleaving ribozyme. Proceedings of the National Academy of Sciences of the United States of America. PMID 28096403 DOI: 10.1073/Pnas.1611191114 |
0.414 |
|
2016 |
Liu B, Steitz TA. Structural insights into NusG regulating transcription elongation. Nucleic Acids Research. PMID 27899640 DOI: 10.1093/Nar/Gkw1159 |
0.459 |
|
2016 |
Gagnon MG, Lin J, Steitz TA. Elongation factor 4 remodels the A-site tRNA on the ribosome. Proceedings of the National Academy of Sciences of the United States of America. PMID 27092003 DOI: 10.1073/Pnas.1522932113 |
0.468 |
|
2016 |
Melnikov SV, Söll D, Steitz TA, Polikanov YS. Insights into RNA binding by the anticancer drug cisplatin from the crystal structure of cisplatin-modified ribosome. Nucleic Acids Research. PMID 27079977 DOI: 10.1093/Nar/Gkw246 |
0.558 |
|
2016 |
Liu B, Zuo Y, Steitz TA. Structures of E. coli σS-transcription initiation complexes provide new insights into polymerase mechanism. Proceedings of the National Academy of Sciences of the United States of America. PMID 27035955 DOI: 10.1073/Pnas.1520555113 |
0.512 |
|
2016 |
Gagnon MG, Roy RN, Lomakin IB, Florin T, Mankin AS, Steitz TA. Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Research. PMID 26809677 DOI: 10.1093/Nar/Gkw018 |
0.8 |
|
2015 |
Lomakin IB, Gagnon MG, Steitz TA. Antimicrobial peptides targeting bacterial ribosome. Oncotarget. 6: 18744-5. PMID 26300053 DOI: 10.18632/Oncotarget.5114 |
0.408 |
|
2015 |
Polikanov YS, Starosta AL, Juette MF, Altman RB, Terry DS, Lu W, Burnett BJ, Dinos G, Reynolds KA, Blanchard SC, Steitz TA, Wilson DN. Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A. Molecular Cell. 58: 832-44. PMID 26028538 DOI: 10.1016/J.Molcel.2015.04.014 |
0.41 |
|
2015 |
Roy RN, Lomakin IB, Gagnon MG, Steitz TA. The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin. Nature Structural & Molecular Biology. 22: 466-9. PMID 25984972 DOI: 10.1038/Nsmb.3031 |
0.796 |
|
2015 |
Zuo Y, Steitz TA. Crystal Structures of the E. coli Transcription Initiation Complexes with a Complete Bubble. Molecular Cell. 58: 534-40. PMID 25866247 DOI: 10.1016/J.Molcel.2015.03.010 |
0.429 |
|
2015 |
Polikanov YS, Melnikov SV, Söll D, Steitz TA. Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly. Nature Structural & Molecular Biology. 22: 342-4. PMID 25775268 DOI: 10.1038/Nsmb.2992 |
0.575 |
|
2015 |
Bunick CG, Presland RB, Lawrence OT, Pearton DJ, Milstone LM, Steitz TA. Crystal Structure of Human Profilaggrin S100 Domain and Identification of Target Proteins Annexin II, Stratifin, and HSP27. The Journal of Investigative Dermatology. 135: 1801-9. PMID 25760235 DOI: 10.1038/Jid.2015.102 |
0.366 |
|
2015 |
Liu B, Zuo Y, Steitz TA. Structural basis for transcription reactivation by RapA. Proceedings of the National Academy of Sciences of the United States of America. 112: 2006-10. PMID 25646438 DOI: 10.1073/Pnas.1417152112 |
0.492 |
|
2015 |
Lin J, Gagnon MG, Bulkley D, Steitz TA. Conformational changes of elongation factor G on the ribosome during tRNA translocation. Cell. 160: 219-27. PMID 25594181 DOI: 10.1016/J.Cell.2014.11.049 |
0.736 |
|
2014 |
Guo LT, Wang YS, Nakamura A, Eiler D, Kavran JM, Wong M, Kiessling LL, Steitz TA, O'Donoghue P, Söll D. Polyspecific pyrrolysyl-tRNA synthetases from directed evolution. Proceedings of the National Academy of Sciences of the United States of America. 111: 16724-9. PMID 25385624 DOI: 10.1073/Pnas.1419737111 |
0.768 |
|
2014 |
Polikanov YS, Szal T, Jiang F, Gupta P, Matsuda R, Shiozuka M, Steitz TA, Vázquez-Laslop N, Mankin AS. Negamycin interferes with decoding and translocation by simultaneous interaction with rRNA and tRNA. Molecular Cell. 56: 541-50. PMID 25306922 DOI: 10.1016/J.Molcel.2014.09.021 |
0.411 |
|
2014 |
Polikanov YS, Osterman IA, Szal T, Tashlitsky VN, Serebryakova MV, Kusochek P, Bulkley D, Malanicheva IA, Efimenko TA, Efremenkova OV, Konevega AL, Shaw KJ, Bogdanov AA, Rodnina MV, Dontsova OA, ... ... Steitz TA, et al. Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Molecular Cell. 56: 531-40. PMID 25306919 DOI: 10.1016/J.Molcel.2014.09.020 |
0.752 |
|
2014 |
Eiler D, Wang J, Steitz TA. Structural basis for the fast self-cleavage reaction catalyzed by the twister ribozyme. Proceedings of the National Academy of Sciences of the United States of America. 111: 13028-33. PMID 25157168 DOI: 10.1073/Pnas.1414571111 |
0.457 |
|
2014 |
Gagnon MG, Lin J, Bulkley D, Steitz TA. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. Science (New York, N.Y.). 345: 684-7. PMID 25104389 DOI: 10.1126/Science.1253525 |
0.775 |
|
2014 |
Brown JA, Bulkley D, Wang J, Valenstein ML, Yario TA, Steitz TA, Steitz JA. Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nature Structural & Molecular Biology. 21: 633-40. PMID 24952594 DOI: 10.1038/Nsmb.2844 |
0.739 |
|
2014 |
Ritacco CJ, Steitz TA, Wang J. Exploiting large non-isomorphous differences for phase determination of a G-segment invertase-DNA complex. Acta Crystallographica. Section D, Biological Crystallography. 70: 685-93. PMID 24598738 DOI: 10.1107/S1399004713032392 |
0.407 |
|
2014 |
Ban N, Beckmann R, Cate JH, Dinman JD, Dragon F, Ellis SR, Lafontaine DL, Lindahl L, Liljas A, Lipton JM, McAlear MA, Moore PB, Noller HF, Ortega J, Panse VG, ... ... Steitz TA, et al. A new system for naming ribosomal proteins. Current Opinion in Structural Biology. 24: 165-9. PMID 24524803 DOI: 10.1016/J.Sbi.2014.01.002 |
0.527 |
|
2014 |
Bulkley D, Brandi L, Polikanov YS, Fabbretti A, O'Connor M, Gualerzi CO, Steitz TA. The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Reports. 6: 357-65. PMID 24412368 DOI: 10.1016/J.Celrep.2013.12.024 |
0.74 |
|
2014 |
Steitz T. How my Experiences at the MRC-LMB led to the Structure of the Ribosome Acta Crystallographica Section a Foundations and Advances. 70: C935-C935. DOI: 10.1107/S2053273314090640 |
0.439 |
|
2013 |
Liu B, Eliason WK, Steitz TA. Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly. Nature Communications. 4: 2495. PMID 24048025 DOI: 10.1038/Ncomms3495 |
0.52 |
|
2013 |
Eiler D, Lin J, Simonetti A, Klaholz BP, Steitz TA. Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases. Proceedings of the National Academy of Sciences of the United States of America. 110: 15662-7. PMID 24029018 DOI: 10.1073/Pnas.1309360110 |
0.425 |
|
2013 |
Simonetti A, Marzi S, Billas IM, Tsai A, Fabbretti A, Myasnikov AG, Roblin P, Vaiana AC, Hazemann I, Eiler D, Steitz TA, Puglisi JD, Gualerzi CO, Klaholz BP. Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor. Proceedings of the National Academy of Sciences of the United States of America. 110: 15656-61. PMID 24029017 DOI: 10.1073/Pnas.1309578110 |
0.328 |
|
2013 |
Lomakin IB, Steitz TA. The initiation of mammalian protein synthesis and mRNA scanning mechanism. Nature. 500: 307-11. PMID 23873042 DOI: 10.1038/Nature12355 |
0.423 |
|
2013 |
Zuo Y, Wang Y, Steitz TA. The mechanism of E. coli RNA polymerase regulation by ppGpp is suggested by the structure of their complex. Molecular Cell. 50: 430-6. PMID 23623685 DOI: 10.1016/J.Molcel.2013.03.020 |
0.472 |
|
2013 |
Liu B, Lin J, Steitz TA. Structure of the PolIIIα-τc-DNA complex suggests an atomic model of the replisome. Structure (London, England : 1993). 21: 658-64. PMID 23478062 DOI: 10.1016/J.Str.2013.02.002 |
0.5 |
|
2013 |
Ritacco CJ, Kamtekar S, Wang J, Steitz TA. Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase. Nucleic Acids Research. 41: 2673-82. PMID 23275567 DOI: 10.1093/Nar/Gks1303 |
0.462 |
|
2012 |
Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA. The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell. 151: 267-77. PMID 23022319 DOI: 10.1016/J.Cell.2012.09.014 |
0.661 |
|
2012 |
Blaha GM, Polikanov YS, Steitz TA. Elements of ribosomal drug resistance and specificity. Current Opinion in Structural Biology. 22: 750-8. PMID 22981944 DOI: 10.1016/J.Sbi.2012.07.016 |
0.367 |
|
2012 |
Polikanov YS, Blaha GM, Steitz TA. How hibernation factors RMF, HPF, and YfiA turn off protein synthesis. Science (New York, N.Y.). 336: 915-8. PMID 22605777 DOI: 10.1126/Science.1218538 |
0.437 |
|
2012 |
Gagnon MG, Seetharaman SV, Bulkley D, Steitz TA. Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science (New York, N.Y.). 335: 1370-2. PMID 22422986 DOI: 10.1126/Science.1217443 |
0.778 |
|
2012 |
Bulkley D, Johnson F, Steitz TA. The antibiotic thermorubin inhibits protein synthesis by binding to inter-subunit bridge B2a of the ribosome. Journal of Molecular Biology. 416: 571-8. PMID 22240456 DOI: 10.1016/J.Jmb.2011.12.055 |
0.766 |
|
2012 |
Steitz TA, Blaha G, Innis CA, Stanley RE, Bulkley D. Structural studies of the functional complexes of the 50s and 70s ribosome, a major antibiotic target Nato Science For Peace and Security Series a: Chemistry and Biology. 135-148. DOI: 10.1007/978-94-007-2530-0_13 |
0.781 |
|
2011 |
Wang M, Xia S, Blaha G, Steitz TA, Konigsberg WH, Wang J. Insights into base selectivity from the 1.8 Å resolution structure of an RB69 DNA polymerase ternary complex. Biochemistry. 50: 581-90. PMID 21158418 DOI: 10.1021/Bi101192F |
0.421 |
|
2011 |
Moore PB, Steitz TA. The roles of RNA in the synthesis of protein. Cold Spring Harbor Perspectives in Biology. 3: a003780. PMID 21068149 DOI: 10.1101/Cshperspect.A003780 |
0.394 |
|
2011 |
Steitz TA. From the structure and function of the ribosome to new antibiotics Acta Crystallographica Section a Foundations of Crystallography. 67: C2-C2. DOI: 10.1107/S0108767311099971 |
0.338 |
|
2010 |
Mitton-Fry RM, DeGregorio SJ, Wang J, Steitz TA, Steitz JA. Poly(A) tail recognition by a viral RNA element through assembly of a triple helix. Science (New York, N.Y.). 330: 1244-7. PMID 21109672 DOI: 10.1126/Science.1195858 |
0.367 |
|
2010 |
Pan B, Xiong Y, Steitz TA. How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA. Science (New York, N.Y.). 330: 937-40. PMID 21071662 DOI: 10.1126/Science.1194985 |
0.371 |
|
2010 |
Bulkley D, Innis CA, Blaha G, Steitz TA. Revisiting the structures of several antibiotics bound to the bacterial ribosome. Proceedings of the National Academy of Sciences of the United States of America. 107: 17158-63. PMID 20876130 DOI: 10.1073/Pnas.1008685107 |
0.75 |
|
2010 |
Steitz TA. From the structure and function of the ribosome to new antibiotics (Nobel Lecture). Angewandte Chemie (International Ed. in English). 49: 4381-98. PMID 20509130 DOI: 10.1002/Anie.201000708 |
0.338 |
|
2010 |
Gleick PH, Adams RM, Amasino RM, Anders E, Anderson DJ, Anderson WW, Anselin LE, Arroyo MK, Asfaw B, Ayala FJ, Bax A, Bebbington AJ, Bell G, Bennett MV, Bennetzen JL, ... ... Steitz TA, et al. Climate change and the integrity of science. Science (New York, N.Y.). 328: 689-90. PMID 20448167 DOI: 10.1126/Science.328.5979.689 |
0.71 |
|
2010 |
Stanley RE, Blaha G, Grodzicki RL, Strickler MD, Steitz TA. The structures of the anti-tuberculosis antibiotics viomycin and capreomycin bound to the 70S ribosome. Nature Structural & Molecular Biology. 17: 289-93. PMID 20154709 DOI: 10.1038/Nsmb.1755 |
0.7 |
|
2010 |
Steitz TA, Goldman A, Engelman DM. Quantitative application of the helical hairpin hypothesis to membrane proteins. Biophysical Journal. 37: 124-5. PMID 19431438 DOI: 10.1016/S0006-3495(82)84633-X |
0.554 |
|
2009 |
Seidelt B, Innis CA, Wilson DN, Gartmann M, Armache JP, Villa E, Trabuco LG, Becker T, Mielke T, Schulten K, Steitz TA, Beckmann R. Structural insight into nascent polypeptide chain-mediated translational stalling. Science (New York, N.Y.). 326: 1412-5. PMID 19933110 DOI: 10.1126/Science.1177662 |
0.387 |
|
2009 |
Steitz TA. The structural changes of T7 RNA polymerase from transcription initiation to elongation. Current Opinion in Structural Biology. 19: 683-90. PMID 19811903 DOI: 10.1016/J.Sbi.2009.09.001 |
0.447 |
|
2009 |
Sharma H, Yu S, Kong J, Wang J, Steitz TA. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proceedings of the National Academy of Sciences of the United States of America. 106: 16604-9. PMID 19805344 DOI: 10.1073/Pnas.0908380106 |
0.641 |
|
2009 |
Gürel G, Blaha G, Steitz TA, Moore PB. Structures of triacetyloleandomycin and mycalamide A bind to the large ribosomal subunit of Haloarcula marismortui. Antimicrobial Agents and Chemotherapy. 53: 5010-4. PMID 19738021 DOI: 10.1128/Aac.00817-09 |
0.445 |
|
2009 |
Blaha G, Stanley RE, Steitz TA. Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Science (New York, N.Y.). 325: 966-70. PMID 19696344 DOI: 10.1126/Science.1175800 |
0.694 |
|
2009 |
Palioura S, Sherrer RL, Steitz TA, Söll D, Simonovic M. The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science (New York, N.Y.). 325: 321-5. PMID 19608919 DOI: 10.1126/Science.1173755 |
0.586 |
|
2009 |
Simonovi? M, Steitz TA. A structural view on the mechanism of the ribosome-catalyzed peptide bond formation. Biochimica Et Biophysica Acta. 1789: 612-23. PMID 19595805 DOI: 10.1016/J.Bbagrm.2009.06.006 |
0.385 |
|
2009 |
Yin FF, Bailey S, Innis CA, Ciubotaru M, Kamtekar S, Steitz TA, Schatz DG. Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nature Structural & Molecular Biology. 16: 499-508. PMID 19396172 DOI: 10.1038/Nsmb.1593 |
0.447 |
|
2009 |
Gürel G, Blaha G, Moore PB, Steitz TA. U2504 determines the species specificity of the A-site cleft antibiotics: the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome. Journal of Molecular Biology. 389: 146-56. PMID 19362093 DOI: 10.1016/J.Jmb.2009.04.005 |
0.468 |
|
2009 |
Steitz TA. Retrospective. Frederic M. Richards (1925-2009). Science (New York, N.Y.). 323: 1181. PMID 19251620 DOI: 10.1126/Science.1171157 |
0.349 |
|
2009 |
Stabach PR, Simonovi? I, Ranieri MA, Aboodi MS, Steitz TA, Simonovi? M, Morrow JS. The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties. Blood. 113: 5377-84. PMID 19168783 DOI: 10.1182/Blood-2008-10-184291 |
0.438 |
|
2008 |
Durniak KJ, Bailey S, Steitz TA. The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation. Science (New York, N.Y.). 322: 553-7. PMID 18948533 DOI: 10.1126/Science.1163433 |
0.818 |
|
2008 |
Simonovi? M, Steitz TA. Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNA. Rna (New York, N.Y.). 14: 2372-8. PMID 18818369 DOI: 10.1261/Rna.1118908 |
0.406 |
|
2008 |
Wing RA, Bailey S, Steitz TA. Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit. Journal of Molecular Biology. 382: 859-69. PMID 18691598 DOI: 10.1016/J.Jmb.2008.07.058 |
0.65 |
|
2008 |
Ippolito JA, Kanyo ZF, Wang D, Franceschi FJ, Moore PB, Steitz TA, Duffy EM. Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit. Journal of Medicinal Chemistry. 51: 3353-6. PMID 18494460 DOI: 10.1021/Jm800379D |
0.459 |
|
2008 |
Blaha G, Gürel G, Schroeder SJ, Moore PB, Steitz TA. Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. Journal of Molecular Biology. 379: 505-19. PMID 18455733 DOI: 10.1016/J.Jmb.2008.03.075 |
0.369 |
|
2008 |
Steitz TA. Structural insights into the functions of the large ribosomal subunit, a major antibiotic target. The Keio Journal of Medicine. 57: 1-14. PMID 18382121 DOI: 10.2302/Kjm.57.1 |
0.359 |
|
2008 |
Evans RN, Blaha G, Bailey S, Steitz TA. The structure of LepA, the ribosomal back translocase. Proceedings of the National Academy of Sciences of the United States of America. 105: 4673-8. PMID 18362332 DOI: 10.1073/Pnas.0801308105 |
0.436 |
|
2008 |
Steitz TA. A structural understanding of the dynamic ribosome machine. Nature Reviews. Molecular Cell Biology. 9: 242-53. PMID 18292779 DOI: 10.1038/Nrm2352 |
0.427 |
|
2008 |
Simonovi? M, Steitz TA. Cross-crystal averaging reveals that the structure of the peptidyl-transferase center is the same in the 70S ribosome and the 50S subunit. Proceedings of the National Academy of Sciences of the United States of America. 105: 500-5. PMID 18187576 DOI: 10.1073/Pnas.0711076105 |
0.435 |
|
2007 |
Steitz TA. Collecting butterflies and the protein structure initiative: the right questions? Structure (London, England : 1993). 15: 1523-4. PMID 18073100 DOI: 10.1016/J.Str.2007.11.005 |
0.442 |
|
2007 |
Bailey S, Eliason WK, Steitz TA. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science (New York, N.Y.). 318: 459-63. PMID 17947583 DOI: 10.1126/Science.1147353 |
0.496 |
|
2007 |
Berman AJ, Kamtekar S, Goodman JL, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TA. Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases. The Embo Journal. 26: 3494-505. PMID 17611604 DOI: 10.1038/Sj.Emboj.7601780 |
0.695 |
|
2007 |
Bailey S, Eliason WK, Steitz TA. The crystal structure of the Thermus aquaticus DnaB helicase monomer. Nucleic Acids Research. 35: 4728-36. PMID 17606462 DOI: 10.1093/Nar/Gkm507 |
0.445 |
|
2007 |
Kavran JM, Steitz TA. Structure of the base of the L7/L12 stalk of the Haloarcula marismortui large ribosomal subunit: analysis of L11 movements. Journal of Molecular Biology. 371: 1047-59. PMID 17599351 DOI: 10.1016/J.Jmb.2007.05.091 |
0.731 |
|
2007 |
Kavran JM, Gundllapalli S, O'Donoghue P, Englert M, Söll D, Steitz TA. Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation. Proceedings of the National Academy of Sciences of the United States of America. 104: 11268-73. PMID 17592110 DOI: 10.1073/Pnas.0704769104 |
0.796 |
|
2007 |
Lomakin IB, Xiong Y, Steitz TA. The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell. 129: 319-32. PMID 17448991 DOI: 10.1016/J.Cell.2007.03.013 |
0.407 |
|
2007 |
Schroeder SJ, Blaha G, Tirado-Rives J, Steitz TA, Moore PB. The structures of antibiotics bound to the E site region of the 50 S ribosomal subunit of Haloarcula marismortui: 13-deoxytedanolide and girodazole. Journal of Molecular Biology. 367: 1471-9. PMID 17321546 DOI: 10.1016/J.Jmb.2007.01.081 |
0.423 |
|
2007 |
Kamtekar S, Hohn MJ, Park HS, Schnitzbauer M, Sauerwald A, Söll D, Steitz TA. Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 104: 2620-5. PMID 17301225 DOI: 10.1073/Pnas.0611504104 |
0.614 |
|
2006 |
Bailey S, Wing RA, Steitz TA. The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell. 126: 893-904. PMID 16959569 DOI: 10.1016/J.Cell.2006.07.027 |
0.668 |
|
2006 |
Simonovic M, Zhang Z, Cianci CD, Steitz TA, Morrow JS. Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. The Journal of Biological Chemistry. 281: 34333-40. PMID 16945920 DOI: 10.1074/Jbc.M604613200 |
0.436 |
|
2006 |
Steitz TA. Visualizing polynucleotide polymerase machines at work. The Embo Journal. 25: 3458-68. PMID 16900098 DOI: 10.1038/Sj.Emboj.7601211 |
0.455 |
|
2006 |
Kamtekar S, Ho RS, Cocco MJ, Li W, Wenwieser SV, Boocock MR, Grindley ND, Steitz TA. Implications of structures of synaptic tetramers of gamma delta resolvase for the mechanism of recombination. Proceedings of the National Academy of Sciences of the United States of America. 103: 10642-7. PMID 16807292 DOI: 10.1073/Pnas.0604062103 |
0.813 |
|
2006 |
Voss NR, Gerstein M, Steitz TA, Moore PB. The geometry of the ribosomal polypeptide exit tunnel. Journal of Molecular Biology. 360: 893-906. PMID 16784753 DOI: 10.1016/J.Jmb.2006.05.023 |
0.371 |
|
2006 |
Kamtekar S, Berman AJ, Wang J, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TA. The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition. The Embo Journal. 25: 1335-43. PMID 16511564 DOI: 10.1038/Sj.Emboj.7601027 |
0.707 |
|
2006 |
Xiong Y, Steitz TA. A story with a good ending: tRNA 3'-end maturation by CCA-adding enzymes. Current Opinion in Structural Biology. 16: 12-7. PMID 16364630 DOI: 10.1016/J.Sbi.2005.12.001 |
0.352 |
|
2006 |
Moore PB, Steitz TA. 9 The Roles of RNA in the Synthesis of Protein Cold Spring Harbor Monograph Archive. 43: 257-285. DOI: 10.1101/087969739.43.257 |
0.383 |
|
2005 |
Schmeing TM, Huang KS, Strobel SA, Steitz TA. An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature. 438: 520-4. PMID 16306996 DOI: 10.1038/Nature04152 |
0.632 |
|
2005 |
Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA. Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction. Molecular Cell. 20: 437-48. PMID 16285925 DOI: 10.1016/J.Molcel.2005.09.006 |
0.614 |
|
2005 |
Li W, Kamtekar S, Xiong Y, Sarkis GJ, Grindley ND, Steitz TA. Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs. Science (New York, N.Y.). 309: 1210-5. PMID 15994378 DOI: 10.2210/Pdb1Zr2/Pdb |
0.796 |
|
2005 |
Tu D, Blaha G, Moore PB, Steitz TA. Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted. Extremophiles : Life Under Extreme Conditions. 9: 427-35. PMID 15970993 DOI: 10.1007/S00792-005-0459-Y |
0.554 |
|
2005 |
Moore PB, Steitz TA. The ribosome revealed. Trends in Biochemical Sciences. 30: 281-3. PMID 15950868 DOI: 10.1016/J.Tibs.2005.04.006 |
0.335 |
|
2005 |
Tu D, Blaha G, Moore PB, Steitz TA. Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell. 121: 257-70. PMID 15851032 DOI: 10.1016/J.Cell.2005.02.005 |
0.622 |
|
2005 |
RodrÃguez I, Lázaro JM, Blanco L, Kamtekar S, Berman AJ, Wang J, Steitz TA, Salas M, de Vega M. A specific subdomain in phi29 DNA polymerase confers both processivity and strand-displacement capacity. Proceedings of the National Academy of Sciences of the United States of America. 102: 6407-12. PMID 15845765 DOI: 10.1073/Pnas.0500597102 |
0.681 |
|
2005 |
Steitz TA. On the structural basis of peptide-bond formation and antibiotic resistance from atomic structures of the large ribosomal subunit. Febs Letters. 579: 955-8. PMID 15680981 DOI: 10.1016/J.Febslet.2004.11.053 |
0.446 |
|
2005 |
Wang J, Kamtekar S, Berman AJ, Steitz TA. Correction of X-ray intensities from single crystals containing lattice-translocation defects. Acta Crystallographica. Section D, Biological Crystallography. 61: 67-74. PMID 15608377 DOI: 10.1107/S0907444904026721 |
0.672 |
|
2004 |
Kamtekar S, Berman AJ, Wang J, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TA. Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage phi29. Molecular Cell. 16: 609-18. PMID 15546620 DOI: 10.1016/J.Molcel.2004.10.019 |
0.704 |
|
2004 |
Klein DJ, Moore PB, Steitz TA. The contribution of metal ions to the structural stability of the large ribosomal subunit. Rna (New York, N.Y.). 10: 1366-79. PMID 15317974 DOI: 10.1261/Rna.7390804 |
0.546 |
|
2004 |
Xiong Y, Steitz TA. Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template. Nature. 430: 640-5. PMID 15295590 DOI: 10.1038/Nature02711 |
0.447 |
|
2004 |
Pata JD, Stirtan WG, Goldstein SW, Steitz TA. Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors. Proceedings of the National Academy of Sciences of the United States of America. 101: 10548-53. PMID 15249669 DOI: 10.1073/Pnas.0404151101 |
0.404 |
|
2004 |
Klein DJ, Moore PB, Steitz TA. The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. Journal of Molecular Biology. 340: 141-77. PMID 15184028 DOI: 10.1016/J.Jmb.2004.03.076 |
0.594 |
|
2004 |
Steitz TA. The structural basis of the transition from initiation to elongation phases of transcription, as well as translocation and strand separation, by T7 RNA polymerase. Current Opinion in Structural Biology. 14: 4-9. PMID 15102443 DOI: 10.1016/J.Sbi.2004.01.006 |
0.449 |
|
2004 |
Steitz TA, Yin YW. Accuracy, lesion bypass, strand displacement and translocation by DNA polymerases. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 359: 17-23. PMID 15065652 DOI: 10.1098/Rstb.2003.1374 |
0.443 |
|
2004 |
Yin YW, Steitz TA. The structural mechanism of translocation and helicase activity in T7 RNA polymerase. Cell. 116: 393-404. PMID 15016374 DOI: 10.1016/S0092-8674(04)00120-5 |
0.446 |
|
2003 |
Xiong Y, Li F, Wang J, Weiner AM, Steitz TA. Crystal structures of an archaeal class I CCA-adding enzyme and its nucleotide complexes. Molecular Cell. 12: 1165-72. PMID 14636575 DOI: 10.1016/S1097-2765(03)00440-4 |
0.489 |
|
2003 |
Schmeing TM, Moore PB, Steitz TA. Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. Rna (New York, N.Y.). 9: 1345-52. PMID 14561884 DOI: 10.1261/Rna.5120503 |
0.635 |
|
2003 |
Moore PB, Steitz TA. The structural basis of large ribosomal subunit function. Annual Review of Biochemistry. 72: 813-50. PMID 14527328 DOI: 10.1146/Annurev.Biochem.72.110601.135450 |
0.446 |
|
2003 |
Li F, Steitz TA. A novel method of determining the number of macromolecules per asymmetric unit from accurate crystal-volume measurements. Acta Crystallographica. Section D, Biological Crystallography. 59: 1793-6. PMID 14501119 DOI: 10.1107/S0907444903016858 |
0.402 |
|
2003 |
Steitz TA, Moore PB. RNA, the first macromolecular catalyst: the ribosome is a ribozyme. Trends in Biochemical Sciences. 28: 411-8. PMID 12932729 DOI: 10.1016/S0968-0004(03)00169-5 |
0.41 |
|
2003 |
Hansen JL, Moore PB, Steitz TA. Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. Journal of Molecular Biology. 330: 1061-75. PMID 12860128 DOI: 10.1016/S0022-2836(03)00668-5 |
0.749 |
|
2003 |
Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Söll D, Steitz TA. The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases. Proceedings of the National Academy of Sciences of the United States of America. 100: 1673-8. PMID 12578991 DOI: 10.1073/Pnas.0437911100 |
0.59 |
|
2003 |
Moore PB, Steitz TA. After the ribosome structures: how does peptidyl transferase work? Rna (New York, N.Y.). 9: 155-9. PMID 12554855 DOI: 10.1261/Rna.2127103 |
0.423 |
|
2002 |
Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA. Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP. Cell. 111: 815-24. PMID 12526808 DOI: 10.1016/S0092-8674(02)01115-7 |
0.511 |
|
2002 |
Pata JD, King BR, Steitz TA. Assembly, purification and crystallization of an active HIV-1 reverse transcriptase initiation complex. Nucleic Acids Research. 30: 4855-63. PMID 12433988 DOI: 10.1093/Nar/Gkf620 |
0.353 |
|
2002 |
Yin YW, Steitz TA. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science (New York, N.Y.). 298: 1387-95. PMID 12242451 DOI: 10.1126/Science.1077464 |
0.438 |
|
2002 |
Hansen JL, Schmeing TM, Moore PB, Steitz TA. Structural insights into peptide bond formation. Proceedings of the National Academy of Sciences of the United States of America. 99: 11670-5. PMID 12185246 DOI: 10.1073/pnas.172404099 |
0.78 |
|
2002 |
Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB, Steitz TA. The structures of four macrolide antibiotics bound to the large ribosomal subunit. Molecular Cell. 10: 117-28. PMID 12150912 DOI: 10.1016/S1097-2765(02)00570-1 |
0.758 |
|
2002 |
Moore PB, Steitz TA. The involvement of RNA in ribosome function. Nature. 418: 229-35. PMID 12110899 DOI: 10.1038/418229A |
0.347 |
|
2002 |
Mitra K, Steitz TA, Engelman DM. Rational design of 'water-soluble' bacteriorhodopsin variants. Protein Engineering. 15: 485-92. PMID 12082167 DOI: 10.1093/Protein/15.6.485 |
0.589 |
|
2002 |
Schmeing TM, Seila AC, Hansen JL, Freeborn B, Soukup JK, Scaringe SA, Strobel SA, Moore PB, Steitz TA. A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits. Nature Structural Biology. 9: 225-30. PMID 11828326 DOI: 10.1038/Nsb758 |
0.798 |
|
2001 |
Hansen JL, Schmeing TM, Klein DJ, Ippolito JA, Ban N, Nissen P, Freeborn B, Moore PB, Steitz TA. Progress toward an understanding of the structure and enzymatic mechanism of the large ribosomal subunit. Cold Spring Harbor Symposia On Quantitative Biology. 66: 33-42. PMID 12762006 DOI: 10.1101/Sqb.2001.66.33 |
0.807 |
|
2001 |
Zhou BL, Pata JD, Steitz TA. Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Molecular Cell. 8: 427-37. PMID 11545744 DOI: 10.1016/S1097-2765(01)00310-0 |
0.662 |
|
2001 |
Klein DJ, Schmeing TM, Moore PB, Steitz TA. The kink-turn: a new RNA secondary structure motif. The Embo Journal. 20: 4214-21. PMID 11483524 DOI: 10.1093/Emboj/20.15.4214 |
0.683 |
|
2001 |
Franklin MC, Wang J, Steitz TA. Structure of the replicating complex of a pol alpha family DNA polymerase. Cell. 105: 657-67. PMID 11389835 DOI: 10.1016/S0092-8674(01)00367-1 |
0.675 |
|
2001 |
Li H, Cocco MJ, Steitz TA, Engelman DM. Conversion of phospholamban into a soluble pentameric helical bundle. Biochemistry. 40: 6636-45. PMID 11380258 DOI: 10.1021/Bi0026573 |
0.579 |
|
2001 |
Nissen P, Ippolito JA, Ban N, Moore PB, Steitz TA. RNA tertiary interactions in the large ribosomal subunit: the A-minor motif. Proceedings of the National Academy of Sciences of the United States of America. 98: 4899-903. PMID 11296253 DOI: 10.1073/Pnas.081082398 |
0.453 |
|
2001 |
Dandekar T, Nissen P, Hansen J, Ban N, Moore PB, Steitz TA. The structural basis of ribosome activity in peptide bond synthesis Chemtracts. 14: 746-750. |
0.689 |
|
2000 |
Passner JM, Schultz SC, Steitz TA. Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution. Journal of Molecular Biology. 304: 847-59. PMID 11124031 DOI: 10.1006/Jmbi.2000.4231 |
0.825 |
|
2000 |
Li F, Wang J, Steitz TA. Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: A scrunching-shuttling model of CCA specificity. Journal of Molecular Biology. 304: 483-92. PMID 11090289 DOI: 10.1006/Jmbi.2000.4189 |
0.466 |
|
2000 |
Nissen P, Hansen J, Ban N, Moore PB, Steitz TA. The structural basis of ribosome activity in peptide bond synthesis. Science (New York, N.Y.). 289: 920-30. PMID 10937990 DOI: 10.1126/Science.289.5481.920 |
0.737 |
|
2000 |
Ban N, Nissen P, Hansen J, Moore PB, Steitz TA. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science (New York, N.Y.). 289: 905-20. PMID 10937989 DOI: 10.1126/Science.289.5481.905 |
0.779 |
|
2000 |
Lu M, Steitz TA. Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 97: 2023-8. PMID 10696113 DOI: 10.1073/Pnas.97.5.2023 |
0.553 |
|
2000 |
Cheetham GM, Steitz TA. Insights into transcription: structure and function of single-subunit DNA-dependent RNA polymerases. Current Opinion in Structural Biology. 10: 117-23. PMID 10679468 DOI: 10.1016/S0959-440X(99)00058-5 |
0.417 |
|
2000 |
Ippolito JA, Steitz TA. The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution. Journal of Molecular Biology. 295: 711-7. PMID 10656783 DOI: 10.1006/Jmbi.1999.3405 |
0.44 |
|
2000 |
Nissen P, Ban N, Hansen J, Moore P, Steitz T. 2SB5 The complete atomic structure of the large ribosomal subunit from Haloarcula marismortui Seibutsu Butsuri. 40: S105. DOI: 10.2142/Biophys.40.S105_3 |
0.721 |
|
2000 |
Nissen P, Ban N, Hansen J, Moore PB, Steitz TA. The structure of the 50S ribosomal subunit at 2.7 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 56: s80-s80. DOI: 10.1107/S0108767300022364 |
0.747 |
|
2000 |
Nissen P, Ban N, Hansen J, Moore PB, Steitz TA. The complete structure of the 50S ribosomal subunit and a substrate complex Biochemical Society Transactions. 28: A103-A103. DOI: 10.1042/Bst028A103C |
0.746 |
|
1999 |
Brautigam CA, Aschheim K, Steitz TA. Structural elucidation of the binding and inhibitory properties of lanthanide (III) ions at the 3'-5' exonucleolytic active site of the Klenow fragment. Chemistry & Biology. 6: 901-8. PMID 10631518 DOI: 10.1016/S1074-5521(00)80009-5 |
0.642 |
|
1999 |
Cheetham GM, Steitz TA. Structure of a transcribing T7 RNA polymerase initiation complex. Science (New York, N.Y.). 286: 2305-9. PMID 10600732 DOI: 10.1126/Science.286.5448.2305 |
0.419 |
|
1999 |
Klosterman PS, Shah SA, Steitz TA. Crystal structures of two plasmid copy control related RNA duplexes: An 18 base pair duplex at 1.20 A resolution and a 19 base pair duplex at 1.55 A resolution. Biochemistry. 38: 14784-92. PMID 10555960 DOI: 10.1021/Bi9912793 |
0.443 |
|
1999 |
Shamoo Y, Steitz TA. Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Cell. 99: 155-66. PMID 10535734 DOI: 10.1016/S0092-8674(00)81647-5 |
0.47 |
|
1999 |
Ban N, Nissen P, Hansen J, Capel M, Moore PB, Steitz TA. Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit. Nature. 400: 841-7. PMID 10476961 DOI: 10.1038/23641 |
0.752 |
|
1999 |
Silvian LF, Wang J, Steitz TA. Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. Science (New York, N.Y.). 285: 1074-7. PMID 10446055 DOI: 10.2210/Pdb1Ffy/Pdb |
0.388 |
|
1999 |
Steitz TA. DNA polymerases: structural diversity and common mechanisms. The Journal of Biological Chemistry. 274: 17395-8. PMID 10364165 DOI: 10.1074/Jbc.274.25.17395 |
0.398 |
|
1999 |
Cheetham GM, Jeruzalmi D, Steitz TA. Structural basis for initiation of transcription from an RNA polymerase-promoter complex. Nature. 399: 80-3. PMID 10331394 DOI: 10.1038/19999 |
0.762 |
|
1999 |
Kaplan DL, Steitz TA. DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence. The Journal of Biological Chemistry. 274: 6889-97. PMID 10066742 DOI: 10.1074/Jbc.274.11.6889 |
0.588 |
|
1999 |
Brautigam CA, Sun S, Piccirilli JA, Steitz TA. Structures of normal single-stranded DNA and deoxyribo-3'-S-phosphorothiolates bound to the 3'-5' exonucleolytic active site of DNA polymerase I from Escherichia coli. Biochemistry. 38: 696-704. PMID 9888810 DOI: 10.1021/Bi981537G |
0.628 |
|
1999 |
Rife JP, Stallings SC, Correll CC, Dallas A, Steitz TA, Moore PB. Comparison of the crystal and solution structures of two RNA oligonucleotides. Biophysical Journal. 76: 65-75. PMID 9876123 DOI: 10.1016/S0006-3495(99)77178-X |
0.392 |
|
1999 |
Ban N, Moore PB, Steitz TA. APPENDIX 5: The Large Ribosomal Subunit from H. marismortui at 9 Å Resolution Cold Spring Harbor Monograph Archive. 37: 695-696. DOI: 10.1101/087969589.37.695 |
0.338 |
|
1999 |
Cheetham GMT, Jeruzalmi D, Steitz TA. Correction: Structural basis for initiation of transcription from an RNA polymerase–promoter complex Nature. 400: 89-89. DOI: 10.1038/21929 |
0.712 |
|
1998 |
Cheetham GM, Jeruzalmi D, Steitz TA. Transcription regulation, initiation, and "DNA scrunching" by T7 RNA polymerase. Cold Spring Harbor Symposia On Quantitative Biology. 63: 263-7. PMID 10384290 DOI: 10.1101/Sqb.1998.63.263 |
0.704 |
|
1998 |
Correll CC, Munishkin A, Chan YL, Ren Z, Wool IG, Steitz TA. Crystal structure of the ribosomal RNA domain essential for binding elongation factors. Proceedings of the National Academy of Sciences of the United States of America. 95: 13436-41. PMID 9811818 DOI: 10.1073/Pnas.95.23.13436 |
0.452 |
|
1998 |
Ippolito JA, Steitz TA. A 1.3-A resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation. Proceedings of the National Academy of Sciences of the United States of America. 95: 9819-24. PMID 9707559 DOI: 10.1073/Pnas.95.17.9819 |
0.399 |
|
1998 |
Jaeger J, Restle T, Steitz TA. The structure of HIV-1 reverse transcriptase complexed with an RNA pseudoknot inhibitor. The Embo Journal. 17: 4535-42. PMID 9687519 DOI: 10.1093/Emboj/17.15.4535 |
0.453 |
|
1998 |
Jeruzalmi D, Steitz TA. Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. The Embo Journal. 17: 4101-13. PMID 9670025 DOI: 10.1093/Emboj/17.14.4101 |
0.738 |
|
1998 |
Ban N, Freeborn B, Nissen P, Penczek P, Grassucci RA, Sweet R, Frank J, Moore PB, Steitz TA. A 9 A resolution X-ray crystallographic map of the large ribosomal subunit. Cell. 93: 1105-15. PMID 9657144 DOI: 10.1016/S0092-8674(00)81455-5 |
0.337 |
|
1998 |
Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA. How glutaminyl-tRNA synthetase selects glutamine. Structure (London, England : 1993). 6: 439-49. PMID 9562563 DOI: 10.1016/S0969-2126(98)00046-X |
0.41 |
|
1998 |
Brautigam CA, Steitz TA. Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Current Opinion in Structural Biology. 8: 54-63. PMID 9519297 DOI: 10.1016/S0959-440X(98)80010-9 |
0.672 |
|
1998 |
Richmond TJ, Steitz TA. Protein-nucleic acid interactions. Current Opinion in Structural Biology. 8: 11-3. PMID 9519290 DOI: 10.1016/S0959-440X(98)80003-1 |
0.602 |
|
1998 |
Brautigam CA, Steitz TA. Structural principles for the inhibition of the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates. Journal of Molecular Biology. 277: 363-77. PMID 9514742 DOI: 10.1006/Jmbi.1997.1586 |
0.669 |
|
1998 |
Steitz TA. A mechanism for all polymerases. Nature. 391: 231-2. PMID 9440683 DOI: 10.1038/34542 |
0.402 |
|
1997 |
Jeruzalmi D, Steitz TA. Use of organic cosmotropic solutes to crystallize flexible proteins: application to T7 RNA polymerase and its complex with the inhibitor T7 lysozyme. Journal of Molecular Biology. 274: 748-56. PMID 9405156 DOI: 10.1006/Jmbi.1997.1366 |
0.719 |
|
1997 |
Correll CC, Freeborn B, Moore PB, Steitz TA. Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain. Cell. 91: 705-12. PMID 9393863 DOI: 10.1016/S0092-8674(00)80457-2 |
0.423 |
|
1997 |
Bellon SF, Rodgers KK, Schatz DG, Coleman JE, Steitz TA. Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nature Structural Biology. 4: 586-91. PMID 9228952 DOI: 10.1038/Nsb0797-586 |
0.401 |
|
1997 |
Wang J, Sattar AK, Wang CC, Karam JD, Konigsberg WH, Steitz TA. Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69. Cell. 89: 1087-99. PMID 9215631 DOI: 10.1016/S0092-8674(00)80296-2 |
0.458 |
|
1997 |
Shamoo Y, Krueger U, Rice LM, Williams KR, Steitz TA. Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 A resolution. Nature Structural Biology. 4: 215-22. PMID 9164463 DOI: 10.1038/Nsb0397-215 |
0.38 |
|
1997 |
Passner JM, Steitz TA. The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proceedings of the National Academy of Sciences of the United States of America. 94: 2843-7. PMID 9096308 DOI: 10.1073/pnas.94.7.2843 |
0.376 |
|
1997 |
Coleman JE, Rodgers KK, Junker M, Gardner KH, Bellon SF, Steitz TA. Zinc as a structural and folding element of proteins which interact with DNA Journal of Inorganic Biochemistry. 67: 342. DOI: 10.1016/S0162-0134(97)80209-7 |
0.392 |
|
1996 |
Arnez JG, Steitz TA. Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP Biochemistry. 35: 14725-14733. PMID 8942633 DOI: 10.1021/Bi961532O |
0.405 |
|
1996 |
Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, Steitz TA. Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose Embo Journal. 15: 5739-5751. PMID 8918451 DOI: 10.1002/J.1460-2075.1996.Tb00960.X |
0.429 |
|
1996 |
Eom SH, Wang J, Steitz TA. Structure of Taq polymerase with DNA at the polymerase active site. Nature. 382: 278-81. PMID 8717047 DOI: 10.1038/382278A0 |
0.649 |
|
1996 |
Wang J, Yu P, Lin TC, Konigsberg WH, Steitz TA. Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions. Biochemistry. 35: 8110-9. PMID 8679562 DOI: 10.1021/Bi960178R |
0.482 |
|
1995 |
Eom SH, Song HK, Suh SW, Kim Y, Steitz TA, Park JH, Kim JS, Kwon ST, Lee DS. Crystallization and preliminary X-ray crystallographic analysis of DNA polymerase from Thermus aquaticus. Acta Crystallographica. Section D, Biological Crystallography. 51: 1086-8. PMID 15299782 DOI: 10.1107/S0907444995003386 |
0.658 |
|
1995 |
Friedman AM, Fischmann TO, Steitz TA. Crystal structure of lac repressor core tetramer and its implications for DNA looping Science. 268: 1721-1727. PMID 7792597 DOI: 10.1126/Science.7792597 |
0.485 |
|
1995 |
Yang W, Steitz TA. Recombining the structures of HIV integrase, RuvC and RNase H. Structure (London, England : 1993). 3: 131-4. PMID 7735828 DOI: 10.1016/S0969-2126(01)00142-3 |
0.416 |
|
1995 |
Landès C, Perona JJ, Brunie S, Rould MA, Zelwer C, Steitz TA, Risler JL. A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases Biochimie. 77: 194-203. PMID 7647112 DOI: 10.1016/0300-9084(96)88125-9 |
0.655 |
|
1995 |
Kim Y, Eom SH, Wang J, Lee DS, Suh SW, Steitz TA. Crystal structure of Thermus aquaticus DNA polymerase. Nature. 376: 612-6. PMID 7637814 DOI: 10.1038/376612A0 |
0.723 |
|
1995 |
Shamoo Y, Friedman AM, Parsons MR, Konigsberg WH, Steitz TA. Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA. Nature. 376: 362-6. PMID 7630406 DOI: 10.1038/376362A0 |
0.346 |
|
1995 |
Yang W, Steitz TA. Crystal structure of the site-specific recombinase gamma delta resolvase complexed with a 34 bp cleavage site. Cell. 82: 193-207. PMID 7628011 DOI: 10.1016/0092-8674(95)90307-0 |
0.523 |
|
1995 |
Shamoo Y, Friedman AM, Parsons MR, Konigsberg WH, Steitz TA. ERRATUM: Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA Nature. 376: 616-616. DOI: 10.1038/376616a0 |
0.331 |
|
1994 |
Rice PA, Steitz TA. Model for a DNA-mediated synaptic complex suggested by crystal packing of gamma delta resolvase subunits. The Embo Journal. 13: 1514-24. PMID 8156989 DOI: 10.2210/Pdb1Gdr/Pdb |
0.657 |
|
1994 |
Rice PA, Steitz TA. Refinement of gamma delta resolvase reveals a strikingly flexible molecule. Structure (London, England : 1993). 2: 371-84. PMID 8081753 DOI: 10.2210/Pdb2Rsl/Pdb |
0.681 |
|
1994 |
Czworkowski J, Wang J, Steitz TA, Moore PB. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution Embo Journal. 13: 3661-3668. PMID 8070396 DOI: 10.1002/J.1460-2075.1994.Tb06675.X |
0.382 |
|
1994 |
Arnez JG, Steitz TA. Crystal structure of unmodified tRNA(Gln) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure. Biochemistry. 33: 7560-7. PMID 8011621 DOI: 10.1021/Bi00190A008 |
0.462 |
|
1994 |
Jäger J, Smerdon SJ, Wang J, Boisvert DC, Steitz TA. Comparison of three different crystal forms shows HIV-1 reverse transcriptase displays an internal swivel motion Structure. 2: 869-876. PMID 7529124 DOI: 10.1016/S0969-2126(94)00087-5 |
0.457 |
|
1994 |
Steitz TA, Smerdon SJ, Jager J, Joyce CM. A unified polymerase mechanism for nonhomologous DNA and RNA polymerases Science. 266: 2022-2025. PMID 7528445 DOI: 10.1126/Science.7528445 |
0.355 |
|
1994 |
Joyce CM, Steitz TA. Function and structure relationships in DNA polymerases Annual Review of Biochemistry. 63: 777-822. PMID 7526780 DOI: 10.1146/Annurev.Bi.63.070194.004021 |
0.38 |
|
1994 |
Wang J, Smerdon SJ, Jäger J, Kohlstaedt LA, Rice PA, Friedman JM, Steitz TA. Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer. Proceedings of the National Academy of Sciences of the United States of America. 91: 7242-6. PMID 7518928 DOI: 10.1073/Pnas.91.15.7242 |
0.589 |
|
1994 |
Smerdon SJ, Jäger J, Wang J, Kohlstaedt LA, Chirino AJ, Friedman JM, Rice PA, Steitz TA. Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1. Proceedings of the National Academy of Sciences of the United States of America. 91: 3911-5. PMID 7513427 DOI: 10.1073/Pnas.91.9.3911 |
0.564 |
|
1993 |
DiGabriele AD, Steitz TA. A DNA dodecamer containing an adenine tract crystallizes in a unique lattice and exhibits a new bend Journal of Molecular Biology. 231: 1024-1039. PMID 8515463 DOI: 10.1006/Jmbi.1993.1349 |
0.425 |
|
1993 |
Beese LS, Derbyshire V, Steitz TA. Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science (New York, N.Y.). 260: 352-5. PMID 8469987 DOI: 10.1126/Science.8469987 |
0.706 |
|
1993 |
Story RM, Bishop DK, Kleckner N, Steitz TA. Structural relationship of bacterial RecA proteins to recombination proteins from bacteriophage T4 and yeast Science. 259: 1892-1896. PMID 8456313 DOI: 10.1126/Science.8456313 |
0.383 |
|
1993 |
Hughes RE, Rice PA, Steitz TA, Grindley ND. Protein-protein interactions directing resolvase site-specific recombination: a structure-function analysis. The Embo Journal. 12: 1447-58. PMID 8385604 DOI: 10.1002/J.1460-2075.1993.Tb05788.X |
0.751 |
|
1993 |
Perona JJ, Rould MA, Steitz TA. Structural basis for transfer RNA aminoacylation by escherichia coli glutaminyl-tRNA synthetase Biochemistry. 32: 8758-8771. PMID 8364025 DOI: 10.1021/Bi00085A006 |
0.7 |
|
1993 |
Steitz TA, Steitz JA. A general two-metal-ion mechanism for catalytic RNA Proceedings of the National Academy of Sciences of the United States of America. 90: 6498-6502. PMID 8341661 DOI: 10.1073/Pnas.90.14.6498 |
0.344 |
|
1993 |
Beese LS, Friedman JM, Steitz TA. Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Biochemistry. 32: 14095-101. PMID 8260491 DOI: 10.1021/Bi00214A004 |
0.711 |
|
1993 |
Steitz TA, Smerdon S, Jäger J, Wang J, Kohlstaedt LA, Friedman JM, Beese LS, Rice PA. Two DNA polymerases: HIV reverse transcriptase and the Klenow fragment of Escherichia coli DNA polymerase I. Cold Spring Harbor Symposia On Quantitative Biology. 58: 495-504. PMID 7525146 DOI: 10.1101/Sqb.1993.058.01.056 |
0.724 |
|
1993 |
Steitz TA, Kohlstaedt LA, Wang J, Friedman JM, Rice PA. Addendum: Crystal Structure at 3.5 overset{circ}{mathrm A} Resolution of HIV-1 Reverse Transcriptase Complexed with an Inhibitor Science. 259: 295. DOI: 10.1126/Science.259.5093.295 |
0.575 |
|
1993 |
Wang J, Smerdon SJ, Kohlstaedt LA, Jacger J, Rice PA, Friedman JM, Steitz TA. Structure of HIV reverse transcriptase Acta Crystallographica Section a Foundations of Crystallography. 49: c154-c154. DOI: 10.1107/S0108767378095598 |
0.527 |
|
1993 |
Kohlstaedt LA, Wang J, Rice PA, Friedman JM, Steitz TA. 12 The Structure of HIV-1 Reverse Transcriptase Cold Spring Harbor Monograph Archive. 23: 223-249. DOI: 10.1101/087969382.23.223 |
0.526 |
|
1993 |
Steitz TA. 10 Similarities and Differences between RNA and DNA Recognition by Proteins Cold Spring Harbor Monograph Archive. 24: 219-237. DOI: 10.1101/087969380.24.219 |
0.462 |
|
1993 |
Steitz TA. DNA- and RNA-dependent DNA polymerases Current Opinion in Structural Biology. 3: 31-38. DOI: 10.1016/0959-440X(93)90198-T |
0.419 |
|
1992 |
Story RM, Steitz TA. Structure of the recA protein-ADP complex Nature. 355: 374-376. PMID 1731253 DOI: 10.1038/355374A0 |
0.447 |
|
1992 |
Story RM, Weber IT, Steitz TA. The structure of the E. coli recA protein monomer and polymer Nature. 355: 318-325. PMID 1731246 DOI: 10.1038/355318A0 |
0.454 |
|
1992 |
Rould MA, Perona JJ, Steitz TA. Improving multiple isomorphous replacement phasing by heavy-atom refinement using solvent-flattened phases Acta Crystallographica Section a: Foundations of Crystallography. 48: Pt 5/-. PMID 1445683 DOI: 10.1107/S0108767392003404 |
0.536 |
|
1992 |
Kohlstaedt LA, Steitz TA. Reverse transcriptase of human immunodeficiency virus can use either human tRNALys 3 or Escherichia coli tRNAGln 2 as a primer in an in vitro primer-utilization assay Proceedings of the National Academy of Sciences of the United States of America. 89: 9652-9656. PMID 1384059 DOI: 10.1073/Pnas.89.20.9652 |
0.389 |
|
1992 |
Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science (New York, N.Y.). 256: 1783-90. PMID 1377403 DOI: 10.1126/Science.1377403 |
0.677 |
|
1992 |
Kriwacki RW, Schultz SC, Steitz TA, Caradonna JP. Sequence-specific recognition of DNA by zinc-finger peptides derived from the transcription factor Sp1. Proceedings of the National Academy of Sciences of the United States of America. 89: 9759-63. PMID 1329106 DOI: 10.1073/Pnas.89.20.9759 |
0.801 |
|
1992 |
Crothers DM, Steitz TA. 19 Transcriptional Activation by Escherichia coli CAP Protein Cold Spring Harbor Monograph Archive. 501-534. DOI: 10.1101/087969425.22A.501 |
0.439 |
|
1991 |
Perona JJ, Rould MA, Steitz TA, Risler JL, Zelwer C, Brunie S. Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding. Proceedings of the National Academy of Sciences of the United States of America. 88: 2903-7. PMID 2011598 DOI: 10.1073/Pnas.88.7.2903 |
0.693 |
|
1991 |
Beese LS, Steitz TA. Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. The Embo Journal. 10: 25-33. PMID 1989886 DOI: 10.1002/J.1460-2075.1991.Tb07917.X |
0.707 |
|
1991 |
Rould MA, Perona JJ, Steitz TA. Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase Nature. 352: 213-218. PMID 1857417 DOI: 10.1038/352213A0 |
0.71 |
|
1991 |
Schultz SC, Shields GC, Steitz TA. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees. Science (New York, N.Y.). 253: 1001-7. PMID 1653449 DOI: 10.1126/Science.1653449 |
0.813 |
|
1991 |
Steitz TA. Aminoacyl-tRNA synthetases: structural aspects of evolution and tRNA recognition Current Opinion in Structural Biology. 1: 139-143. DOI: 10.1016/0959-440X(91)90022-L |
0.385 |
|
1990 |
Perona JJ, Swanson RN, Rould MA, Steitz TA, Söll D. Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes. Science (New York, N.Y.). 246: 1152-4. PMID 2686030 DOI: 10.1126/Science.2686030 |
0.738 |
|
1990 |
Rould MA, Perona JJ, Söll D, Steitz TA. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution. Science (New York, N.Y.). 246: 1135-42. PMID 2479982 DOI: 10.1126/Science.2479982 |
0.739 |
|
1990 |
Weeks KM, Ampe C, Schultz SC, Steitz TA, Crothers DM. Fragments of the HIV-1 Tat protein specifically bind TAR RNA. Science (New York, N.Y.). 249: 1281-5. PMID 2205002 DOI: 10.1126/Science.2205002 |
0.802 |
|
1990 |
Gartenberg MR, Ampe C, Steitz TA, Crothers DM. Molecular characterization of the GCN4-DNA complex. Proceedings of the National Academy of Sciences of the United States of America. 87: 6034-8. PMID 2201019 DOI: 10.1073/Pnas.87.16.6034 |
0.439 |
|
1990 |
Steitz TA, Rould MA, Perona JJ. Structural basis of tRNA discrimination as derived from the high resolution crystal structure of glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP. Molecular Biology Reports. 14: 213-4. PMID 2194108 DOI: 10.1007/Bf00360479 |
0.682 |
|
1990 |
Hughes RE, Hatfull GF, Rice P, Steitz TA, Grindley ND. Cooperativity mutants of the gamma delta resolvase identify an essential interdimer interaction. Cell. 63: 1331-8. PMID 2175679 DOI: 10.1016/0092-8674(90)90428-H |
0.747 |
|
1990 |
Sanderson MR, Freemont PS, Rice PA, Goldman A, Hatfull GF, Grindley ND, Steitz TA. The crystal structure of the catalytic domain of the site-specific recombination enzyme gamma delta resolvase at 2.7 A resolution. Cell. 63: 1323-9. PMID 2175678 DOI: 10.1016/0092-8674(90)90427-G |
0.814 |
|
1990 |
Schultz SC, Shields GC, Steitz TA. Crystallization of Escherichia coli catabolite gene activator protein with its DNA binding site. The use of modular DNA. Journal of Molecular Biology. 213: 159-66. PMID 2160019 DOI: 10.1016/S0022-2836(05)80128-7 |
0.816 |
|
1990 |
Rice PA, Goldman A, Steitz TA. A helix-turn-strand structural motif common in alpha-beta proteins. Proteins. 8: 334-40. PMID 1708883 DOI: 10.1002/Prot.340080407 |
0.55 |
|
1989 |
DiGabriele AD, Sanderson MR, Steitz TA. Crystal lattice packing is important in determining the bend of a DNA dodecamer containing an adenine tract. Proceedings of the National Academy of Sciences of the United States of America. 86: 1816-20. PMID 2928304 DOI: 10.1073/Pnas.86.6.1816 |
0.431 |
|
1989 |
Rice PA, Steitz TA. Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins. Nucleic Acids Research. 17: 3757-62. PMID 2660100 DOI: 10.1093/Nar/17.10.3757 |
0.598 |
|
1989 |
Hatfull GF, Sanderson MR, Freemont PS, Raccuia PR, Grindley ND, Steitz TA. Preparation of heavy-atom derivatives using site-directed mutagenesis. Introduction of cysteine residues into gamma delta resolvase. Journal of Molecular Biology. 208: 661-7. PMID 2553982 DOI: 10.1016/0022-2836(89)90156-3 |
0.675 |
|
1988 |
Freemont PS, Friedman JM, Beese LS, Sanderson MR, Steitz TA. Cocrystal structure of an editing complex of Klenow fragment with DNA. Proceedings of the National Academy of Sciences of the United States of America. 85: 8924-8. PMID 3194400 DOI: 10.1073/Pnas.85.23.8924 |
0.726 |
|
1988 |
Warwicker J, Engelman BP, Steitz TA. Electrostatic calculations and model-building suggest that DNA bound to CAP is sharply bent. Proteins. 2: 283-9. PMID 2834718 DOI: 10.1002/Prot.340020404 |
0.403 |
|
1988 |
Derbyshire V, Freemont PS, Sanderson MR, Beese L, Friedman JM, Joyce CM, Steitz TA. Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Science (New York, N.Y.). 240: 199-201. PMID 2832946 DOI: 10.1126/Science.2832946 |
0.695 |
|
1988 |
Weber IT, Steitz TA. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution. Journal of Molecular Biology. 198: 311-26. PMID 2828639 DOI: 10.1016/0022-2836(87)90315-9 |
0.427 |
|
1988 |
Perona JJ, Swanson R, Steitz TA, Söll D. Overproduction and purification of Escherichia coli tRNA(2Gln) and its use in crystallization of the glutaminyl-tRNA synthetase-tRNA(Gln) complex. Journal of Molecular Biology. 202: 121-6. PMID 2459391 DOI: 10.1016/0022-2836(88)90524-4 |
0.701 |
|
1987 |
Goldman A, Ollis DL, Steitz TA. Crystal structure of muconate lactonizing enzyme at 3 A resolution. Journal of Molecular Biology. 194: 143-53. PMID 3612800 DOI: 10.1016/0022-2836(87)90723-6 |
0.566 |
|
1987 |
Steitz TA, Beese L, Freemont PS, Friedman JM, Sanderson MR. Structural studies of Klenow fragment: an enzyme with two active sites. Cold Spring Harbor Symposia On Quantitative Biology. 52: 465-71. PMID 3331343 DOI: 10.1101/Sqb.1987.052.01.053 |
0.672 |
|
1987 |
Weber IT, Steitz TA, Bubis J, Taylor SS. Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase. Biochemistry. 26: 343-51. PMID 3030405 DOI: 10.1021/Bi00376A003 |
0.422 |
|
1987 |
Bruist MF, Horvath SJ, Hood LE, Steitz TA, Simon MI. Synthesis of a site-specific DNA-binding peptide. Science (New York, N.Y.). 235: 777-80. PMID 3027895 DOI: 10.1126/Science.3027895 |
0.431 |
|
1987 |
Joyce CM, Steitz TA. DNA polymerase I: from crystal structure to function via genetics Trends in Biochemical Sciences. 12: 288-292. DOI: 10.1016/0968-0004(87)90143-5 |
0.448 |
|
1986 |
Weber IT, Steitz TA. Crystallization of recA protein from Proteus mirabilis. Journal of Molecular Biology. 188: 109-10. PMID 3519980 DOI: 10.1016/0022-2836(86)90486-9 |
0.35 |
|
1986 |
Steitz TA, Freemont PS, Ollis DL, Joyce CM, Grindley JM. Functional implications of the Klenow fragment structure Biochemical Society Transactions. 14: 205-207. PMID 3519313 DOI: 10.1042/Bst0140205 |
0.344 |
|
1986 |
Freemont PS, Ollis DL, Steitz TA, Joyce CM. A domain of the Klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity Proteins: Structure, Function and Genetics. 1: 66-73. PMID 3329725 DOI: 10.1002/Prot.340010111 |
0.441 |
|
1985 |
Weber IT, Steitz TA. A model for the non-specific binding of catabolite gene activator protein to DNA. Nucleic Acids Research. 12: 8475-87. PMID 6390343 DOI: 10.1093/Nar/12.22.8475 |
0.429 |
|
1985 |
Goldman A, Ollis D, Ngai KL, Steitz TA. Crystal structure of muconate lactonizing enzyme at 6.5 A resolution. Journal of Molecular Biology. 182: 353-5. PMID 3999146 DOI: 10.1016/0022-2836(85)90352-3 |
0.583 |
|
1985 |
Warwicker J, Ollis D, Richards FM, Steitz TA. Electrostatic field of the large fragment of Escherichia coli DNA polymerase I. Journal of Molecular Biology. 186: 645-9. PMID 3912509 DOI: 10.1016/0022-2836(85)90136-6 |
0.604 |
|
1985 |
Ollis DL, Kline C, Steitz TA. Domain of E. coli DNA polymerase I showing sequence homology to T7 DNA polymerase. Nature. 313: 818-9. PMID 3883196 DOI: 10.1038/313818A0 |
0.418 |
|
1985 |
Ollis DL, Brick P, Hamlin R, Xuong NG, Steitz TA. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature. 313: 762-6. PMID 3883192 DOI: 10.1038/313762A0 |
0.686 |
|
1984 |
Weber IT, Steitz TA. Model of specific complex between catabolite gene activator protein and B-DNA suggested by electrostatic complementarity. Proceedings of the National Academy of Sciences of the United States of America. 81: 3973-7. PMID 6377305 DOI: 10.1073/Pnas.81.13.3973 |
0.432 |
|
1984 |
Abdel-Meguid SS, Grindley ND, Templeton NS, Steitz TA. Cleavage of the site-specific recombination protein gamma delta resolvase: the smaller of two fragments binds DNA specifically. Proceedings of the National Academy of Sciences of the United States of America. 81: 2001-5. PMID 6326096 DOI: 10.1073/Pnas.81.7.2001 |
0.697 |
|
1984 |
Abdel-Meguid SS, Moore PB, Steitz TA. Crystallization of a ribonuclease-resistant fragment of Escherichia coli 5 S ribosomal RNA and its complex with protein L25. Journal of Molecular Biology. 171: 207-15. PMID 6197527 DOI: 10.1016/S0022-2836(83)80353-2 |
0.389 |
|
1984 |
Ollis D, Brick P, Hamlin R, Xuong NG, Steitz TA. Structure of the large fragment ofE. coliDNA polymerase I complexed with dCMP Acta Crystallographica Section a Foundations of Crystallography. 40: C47-C47. DOI: 10.1107/S0108767384098330 |
0.643 |
|
1983 |
Ollis D, Brick P, Abdel-Meguid SS, Murthy K, Chase JW, Steitz TA. Crystals of Escherichia coli single-strand DNA-binding protein show that the tetramer has D2 symmetry. Journal of Molecular Biology. 170: 797-800. PMID 6355488 DOI: 10.1016/S0022-2836(83)80134-X |
0.649 |
|
1983 |
Brick P, Ollis D, Steitz TA. Crystallization and 7 A resolution electron density map of the large fragment of Escherichia coli DNA polymerase I. Journal of Molecular Biology. 166: 453-6. PMID 6343618 DOI: 10.1016/S0022-2836(83)80095-3 |
0.66 |
|
1983 |
Steitz TA, Weber IT, Ollis D, Brick P. Crystallographic studies of protein-nucleic acid interaction: catabolite gene activator protein and the large fragment of DNA polymerase I. Journal of Biomolecular Structure & Dynamics. 1: 1023-37. PMID 6101086 DOI: 10.1080/07391102.1983.10507500 |
0.658 |
|
1982 |
McKay DB, Pickover CA, Steitz TA. Escherichia coli lac repressor is elongated with its operator DNA binding domains located at both ends. Journal of Molecular Biology. 156: 175-83. PMID 7047750 DOI: 10.1016/0022-2836(82)90465-X |
0.61 |
|
1982 |
Weber IT, McKay DB, Steitz TA. Two helix DNA binding motif of CAP found in lac repressor and gal repressor. Nucleic Acids Research. 10: 5085-102. PMID 6897114 DOI: 10.1093/nar/10.16.5085 |
0.582 |
|
1982 |
Shoham M, Steitz TA. The 6-hydroxymethyl group of a hexose is essential for the substrate-induced closure of the cleft in hexokinase. Biochimica Et Biophysica Acta. 705: 380-4. PMID 6751401 DOI: 10.1016/0167-4838(82)90260-6 |
0.379 |
|
1982 |
Weber PC, Ollis DL, Bebrin WR, Abdel-Meguid SS, Steitz TA. Crystallization of resolvase, a repressor that also catalyzes site-specific DNA recombination. Journal of Molecular Biology. 157: 689-90. PMID 6288965 DOI: 10.1016/0022-2836(82)90508-3 |
0.396 |
|
1982 |
McKay DB, Weber IT, Steitz TA. Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP. The Journal of Biological Chemistry. 257: 9518-24. PMID 6286624 |
0.616 |
|
1982 |
Steitz TA, Ohlendorf DH, McKay DB, Anderson WF, Matthews BW. Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins. Proceedings of the National Academy of Sciences of the United States of America. 79: 3097-100. PMID 6212926 DOI: 10.1073/Pnas.79.10.3097 |
0.718 |
|
1981 |
Bennett WS, Steitz TA. Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer. Journal of Molecular Biology. 140: 211-30. PMID 7001032 DOI: 10.1016/0022-2836(80)90103-5 |
0.434 |
|
1981 |
Bennett WS, Steitz TA. Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5 A resolution. Journal of Molecular Biology. 140: 183-209. PMID 7001031 DOI: 10.1016/0022-2836(80)90102-3 |
0.346 |
|
1981 |
McKay DB, Steitz TA. Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA. Nature. 290: 744-9. PMID 6261152 DOI: 10.1107/S0108767381098942 |
0.667 |
|
1981 |
Steitz TA, Shoham M, Bennett WS. Structural dynamics of yeast hexokinase during catalysis. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 293: 43-52. PMID 6115422 DOI: 10.1098/Rstb.1981.0058 |
0.428 |
|
1980 |
Shoham M, Steitz TA. Crystallographic studies and model building of ATP at the active site of hexokinase. Journal of Molecular Biology. 140: 1-14. PMID 7411639 DOI: 10.1016/0022-2836(80)90353-8 |
0.385 |
|
1980 |
McKay DB, Steitz TA, Weber IT, West SC, Howard-Flanders P. Crystallization of monomeric recA protein. The Journal of Biological Chemistry. 255: 6662. PMID 6446560 |
0.518 |
|
1979 |
Klug A, Jack A, Viswamitra MA, Kennard O, Shakked Z, Steitz TA. A hypothesis on a specific sequence-dependent conformation of DNA and its relation to the binding of the lac-repressor protein. Journal of Molecular Biology. 131: 669-80. PMID 513130 DOI: 10.1016/0022-2836(79)90196-7 |
0.615 |
|
1979 |
Pickover CA, McKay DB, Engelman DM, Steitz TA. Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. The Journal of Biological Chemistry. 254: 11323-9. PMID 387770 |
0.515 |
|
1979 |
Bennett WS, Steitz TA. Glucose-induced conformational change in yeast hexokinase. Proceedings of the National Academy of Sciences of the United States of America. 75: 4848-52. PMID 283394 DOI: 10.1073/Pnas.75.10.4848 |
0.326 |
|
1978 |
Anderson CM, Stenkamp RE, McDonald RC, Steitz TA. A refined model of the sugar binding site of yeast hexokinase B Journal of Molecular Biology. 123: 207-219. PMID 355645 DOI: 10.1016/0022-2836(78)90321-2 |
0.365 |
|
1978 |
Anderson CM, Stenkamp RE, Steitz TA. Sequencing a protein by x-ray crystallography. II. Refinement of yeast hexokinase B co-ordinates and sequence at 2.1 A resolution. Journal of Molecular Biology. 123: 15-33. PMID 355643 DOI: 10.1016/0022-2836(78)90374-1 |
0.308 |
|
1978 |
Anderson CM, McDonald RC, Steitz TA. Sequencing a protein by X-ray crystallography. I. Interpretation of yeast hexokinase B at 2.5 Å resolution by model building Journal of Molecular Biology. 123: 1-13. PMID 355642 DOI: 10.1016/0022-2836(78)90373-X |
0.352 |
|
1977 |
Steitz TA, Anderson C, Bennett W, McDonald R, Stenkamp R. Protomer structure of oligomeric enzymes: symmetry and allosteric interactions in yeast hexokinase. Biochemical Society Transactions. 5: 620-3. PMID 332556 DOI: 10.1042/Bst0050620 |
0.369 |
|
1977 |
Steitz TA, Anderson WF, Fletterick RJ, Anderson CM. High resolution crystal structures of yeast hexokinase complexes with substrates, activators, and inhibitors. Evidence for an allosteric control site. The Journal of Biological Chemistry. 252: 4494-500. PMID 326777 |
0.554 |
|
1976 |
Steitz TA, Fletterick RJ, Anderson WF, Anderson CM. High resolution x-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits. Journal of Molecular Biology. 104: 197-22. PMID 785010 DOI: 10.1016/0022-2836(76)90009-7 |
0.639 |
|
1976 |
Richmond TJ, Steitz TA. Protein-DNA interaction investigated by binding Escherichia coli lac repressor protein to poly(d(A-U-HgX)). Journal of Molecular Biology. 103: 25-38. PMID 785008 DOI: 10.1016/0022-2836(76)90050-4 |
0.677 |
|
1976 |
Fletterick RJ, Steitz TA. The combination of independent phase information obtained from separate protein structure determinations of yeast hexokinase Acta Crystallographica Section A. 32: 125-132. DOI: 10.1107/S0567739476000235 |
0.473 |
|
1975 |
Anderson WF, Steitz TA. Structure of yeast hexokinase. IV. Low-resoultion structure of enzyme-substrate complexes revealing negative co-operativity and allosteric interactions. Journal of Molecular Biology. 92: 279-87. PMID 1095755 DOI: 10.1016/0022-2836(75)90227-2 |
0.428 |
|
1975 |
Fletterick RJ, Bates DJ, Steitz TA. The structure of a yeast hexokinase monomer and its complexes with substrates at 2.7-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 72: 38-42. PMID 164023 DOI: 10.1073/Pnas.72.1.38 |
0.63 |
|
1974 |
Steitz TA, Richmond TJ, Wise D, Engelman D. The lac repressor protein: molecular shape, subunit structure, and proposed model for operator interaction based on structural studies of microcrystals. Proceedings of the National Academy of Sciences of the United States of America. 71: 593-7. PMID 4595565 DOI: 10.1073/Pnas.71.3.593 |
0.686 |
|
1974 |
Anderson WF, Fletterick RJ, Steitz TA. Structure of yeast hexokinase. 3. Low resolution structure of a second crystal form showing a different quaternary structure, heterologous interaction of subunits and substrate binding. Journal of Molecular Biology. 86: 261-9. PMID 4370398 DOI: 10.1016/0022-2836(74)90017-5 |
0.633 |
|
1974 |
STEITZ TA, FLETTERICK RJ, ANDERSON WF, BATES DJ. The Structure of Yeast Hexokinase and its Complexes with Substrates Biochemical Society Transactions. 2: 52-54. DOI: 10.1042/Bst0020052C |
0.581 |
|
1973 |
Steitz TA, Fletterick RJ, Hwang KJ. Structure of yeast hexokinase. II. A 6 angstrom resolution electron density map showing molecular shape and heterologous interaction of subunits. Journal of Molecular Biology. 78: 551-61. PMID 4585329 DOI: 10.1016/0022-2836(73)90475-0 |
0.554 |
|
1970 |
Blow DM, Steitz TA. X-ray diffraction studies of enzymes. Annual Review of Biochemistry. 39: 63-100. PMID 5479039 DOI: 10.1146/annurev.bi.39.070170.000431 |
0.522 |
|
1970 |
Birktoft JJ, Blow DM, Henderson R, Steitz TA. I. Serine proteinases. The structure of alpha-chymotrypsin. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 257: 67-76. PMID 4399050 DOI: 10.1098/Rstb.1970.0009 |
0.686 |
|
1969 |
Steitz TA, Henderson R, Blow DM. Structure of crystalline alpha-chymotrypsin. 3. Crystallographic studies of substrates and inhibitors bound to the active site of alpha-chymotrypsin. Journal of Molecular Biology. 46: 337-48. PMID 5360043 DOI: 10.1016/0022-2836(69)90426-4 |
0.655 |
|
1968 |
Lipscomb WN, Hartsuck JA, Reeke GN, Quiocho FA, Bethge PH, Ludwig ML, Steitz TA, Muirhead H, Coppola JC. The structure of carboxypeptidase A. VII. The 2.0-angstrom resolution studies of the enzyme and of its complex with glycyltyrosine, and mechanistic deductions. Brookhaven Symposia in Biology. 21: 24-90. PMID 5719196 |
0.7 |
|
1967 |
Reeke GN, Hartsuck JA, Ludwig ML, Quiocho FA, Steitz TA, Lipscomb WN. The structure of carboxypeptidase a, vi. Some results at 2.0-a resolution, and the complex with glycyl-tyrosine at 2.8-a resolution. Proceedings of the National Academy of Sciences of the United States of America. 58: 2220-6. PMID 16591584 DOI: 10.1073/Pnas.58.6.2220 |
0.743 |
|
1967 |
Steitz TA, Ludwig ML, Quiocho FA, Lipscomb WN. The structure of carboxypepidase A. V. Studies of enzyme-substrate and enzyme-inhibitor complexes at 6 A resolution. The Journal of Biological Chemistry. 242: 4662-8. PMID 6061411 |
0.677 |
|
1967 |
Steitz TA, Wiley DC, Lipscomb WN. The structure of aspartate transcarbamylase, I. A molecular twofold axis in the complex with cytidine triphosphate. Proceedings of the National Academy of Sciences of the United States of America. 58: 1859-61. PMID 5237487 DOI: 10.1073/Pnas.58.5.1859 |
0.657 |
|
1967 |
Ludwig ML, Hartsuck JA, Steitz TA, Muirhead H, Coppola JC, Reeke GN, Lipscomb WN. Symposium on Three-Dimensional Structure of Macromolecules of Biological Origin. by Invitation of the Committee on Arrangements for the Autumn Meeting. Presented before the Academy on October 19, 1966. Chairman, Walter Kauzmann: THE STRUCTURE OF CARBOXYPEPTIDASE A, IV. PRELIMINARY RESULTS AT 2.8 Å RESOLUTION, AND A SUBSTRATE COMPLEX AT 6 Å RESOLUTION Proceedings of the National Academy of Sciences of the United States of America. 57: 511-514. DOI: 10.1073/Pnas.57.3.511 |
0.696 |
|
1966 |
Lipscomb W, Coppola J, Hartsuck J, Ludwig M, Muirhead H, Searl J, Steitz T. The structure of carboxypeptidase A Journal of Molecular Biology. 19: 423-IN3. DOI: 10.1016/S0022-2836(66)80014-1 |
0.68 |
|
1965 |
Hartsuck JA, Ludwig ML, Muirhead H, Steitz TA, Lipscomb WN. CARBOXYPEPTIDASE A, II. THE THREE-DIMENSIONAL ELECTRON DENSITY MAP AT 6 A RESOLUTION. Proceedings of the National Academy of Sciences of the United States of America. 53: 396-403. PMID 16591261 DOI: 10.1073/Pnas.53.2.396 |
0.609 |
|
1965 |
Steitz TA, Lipscomb WN. Molecular Structure of Methyl Ethylene Phosphate Journal of the American Chemical Society. 87: 2488-2489. DOI: 10.1021/Ja01089A031 |
0.478 |
|
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