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Seth A. Darst, Ph.D. - Publications

Affiliations: 
Molecular biophysics Rockefeller University, New York, NY, United States 
Website:
http://www.rockefeller.edu/research/faculty/labheads/SethDarst/

171 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Delbeau M, Omollo EO, Froom R, Koh S, Mooney RA, Lilic M, Brewer JJ, Rock J, Darst SA, Campbell EA, Landick R. Structural and functional basis of the universal transcription factor NusG pro-pausing activity in Mycobacterium tuberculosis. Molecular Cell. PMID 37116494 DOI: 10.1016/j.molcel.2023.04.007  0.357
2023 Mueller AU, Chen J, Wu M, Chiu C, Nixon BT, Campbell EA, Darst SA. A general mechanism for transcription bubble nucleation in bacteria. Proceedings of the National Academy of Sciences of the United States of America. 120: e2220874120. PMID 36972428 DOI: 10.1073/pnas.2220874120  0.346
2023 Kang JY, Mishanina TV, Bao Y, Chen J, Llewellyn E, Liu J, Darst SA, Landick R. An ensemble of interconverting conformations of the elemental paused transcription complex creates regulatory options. Proceedings of the National Academy of Sciences of the United States of America. 120: e2215945120. PMID 36795753 DOI: 10.1073/pnas.2215945120  0.391
2023 Malone BF, Perry JK, Olinares PDB, Lee HW, Chen J, Appleby TC, Feng JY, Bilello JP, Ng H, Sotiris J, Ebrahim M, Chua EYD, Mendez JH, Eng ET, Landick R, ... ... Darst SA, et al. Structural basis for substrate selection by the SARS-CoV-2 replicase. Nature. PMID 36725929 DOI: 10.1038/s41586-022-05664-3  0.362
2022 Chen J, Wang Q, Malone B, Llewellyn E, Pechersky Y, Maruthi K, Eng ET, Perry JK, Campbell EA, Shaw DE, Darst SA. Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex. Nature Structural & Molecular Biology. 29: 250-260. PMID 35260847 DOI: 10.1038/s41594-022-00734-6  0.392
2021 Malone B, Campbell EA, Darst SA. CoV-er all the bases: Structural perspectives of SARS-CoV-2 RNA synthesis. The Enzymes. 49: 1-37. PMID 34696829 DOI: 10.1016/bs.enz.2021.06.004  0.319
2021 Saecker RM, Chen J, Chiu CE, Malone B, Sotiris J, Ebrahim M, Yen LY, Eng ET, Darst SA. Structural origins of RNA polymerase open promoter complex stability. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34599106 DOI: 10.1073/pnas.2112877118  0.377
2021 Lilic M, Darst SA, Campbell EA. Structural basis of transcriptional activation by the Mycobacterium tuberculosis intrinsic antibiotic-resistance transcription factor WhiB7. Molecular Cell. PMID 34171296 DOI: 10.1016/j.molcel.2021.05.017  0.329
2021 Malone B, Chen J, Wang Q, Llewellyn E, Choi YJ, Olinares PDB, Cao X, Hernandez C, Eng ET, Chait BT, Shaw DE, Landick R, Darst SA, Campbell EA. Structural basis for backtracking by the SARS-CoV-2 replication-transcription complex. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33883267 DOI: 10.1073/pnas.2102516118  0.379
2021 Malone B, Chen J, Wang Q, Llewellyn E, Choi YJ, Olinares PDB, Cao X, Hernandez C, Eng ET, Chait BT, Shaw DE, Landick R, Darst SA, Campbell EA. Structural basis for backtracking by the SARS-CoV-2 replication-transcription complex. Biorxiv : the Preprint Server For Biology. PMID 33758867 DOI: 10.1101/2021.03.13.435256  0.388
2021 Kang JY, Llewellyn E, Chen J, Olinares PDB, Brewer J, Chait BT, Campbell EA, Darst SA. Structural basis for transcription complex disruption by the Mfd translocase. Elife. 10. PMID 33480355 DOI: 10.7554/eLife.62117  0.321
2020 Lilic M, Chen J, Boyaci H, Braffman N, Hubin EA, Herrmann J, Müller R, Mooney R, Landick R, Darst SA, Campbell EA. The antibiotic sorangicin A inhibits promoter DNA unwinding in a rifampicin-resistant RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. PMID 33199626 DOI: 10.1073/pnas.2013706117  0.301
2020 Chen J, Malone B, Llewellyn E, Grasso M, Shelton PMM, Olinares PDB, Maruthi K, Eng ET, Vatandaslar H, Chait BT, Kapoor TM, Darst SA, Campbell EA. Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex. Cell. PMID 32783916 DOI: 10.1016/J.Cell.2020.07.033  0.47
2020 Chen J, Malone B, Llewellyn E, Grasso M, Shelton PMM, Olinares PDB, Maruthi K, Eng ET, Vatandaslar H, Chait B, Kapoor T, Darst SA, Campbell EA. Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex. Biorxiv : the Preprint Server For Biology. PMID 32676607 DOI: 10.1101/2020.07.08.194084  0.371
2020 Chen J, Chiu C, Gopalkrishnan S, Chen AY, Olinares PDB, Saecker RM, Winkelman JT, Maloney MF, Chait BT, Ross W, Gourse RL, Campbell EA, Darst SA. Stepwise Promoter Melting by Bacterial RNA Polymerase. Molecular Cell. PMID 32160514 DOI: 10.1016/J.Molcel.2020.02.017  0.505
2019 Chen J, Noble AJ, Kang JY, Darst SA. Eliminating effects of particle adsorption to the air/water interface in single-particle cryo-electron microscopy: Bacterial RNA polymerase and CHAPSO. Journal of Structural Biology: X. 1. PMID 32285040 DOI: 10.1016/J.Yjsbx.2019.100005  0.34
2019 Chen J, Gopalkrishnan S, Chiu C, Chen AY, Campbell EA, Gourse RL, Ross W, Darst SA. TraR allosterically regulates transcription initiation by altering RNA polymerase conformation. Elife. 8. PMID 31841111 DOI: 10.7554/Elife.49375  0.495
2019 Cartagena AJ, Banta AB, Sathyan N, Ross W, Gourse RL, Campbell EA, Darst SA. Structural basis for transcription activation by Crl through tethering of σ and RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. PMID 31484766 DOI: 10.1073/Pnas.1910827116  0.414
2019 Kang JY, Mishanina TV, Landick R, Darst SA. Mechanisms of Transcriptional Pausing in Bacteria. Journal of Molecular Biology. PMID 31310765 DOI: 10.1016/J.Jmb.2019.07.017  0.466
2019 Cheung-Lee WL, Parry ME, Jaramillo Cartagena A, Darst SA, Link AJ. Discovery and structure of the antimicrobial lasso peptide citrocin. The Journal of Biological Chemistry. PMID 30846564 DOI: 10.1074/Jbc.Ra118.006494  0.337
2019 Boyaci H, Chen J, Jansen R, Darst SA, Campbell EA. Structures of an RNA polymerase promoter melting intermediate elucidate DNA unwinding. Nature. 565: 382-385. PMID 30626968 DOI: 10.1038/S41586-018-0840-5  0.469
2019 Braffman NR, Piscotta FJ, Hauver J, Campbell EA, Link AJ, Darst SA. Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin. Proceedings of the National Academy of Sciences of the United States of America. 116: 1273-1278. PMID 30626643 DOI: 10.1073/pnas.1817352116  0.379
2019 Chen J, Gopalkrishnan S, Chiu C, Chen AY, Campbell EA, Gourse RL, Ross W, Darst SA. Author response: E. coli TraR allosterically regulates transcription initiation by altering RNA polymerase conformation Elife. DOI: 10.7554/Elife.49375.Sa2  0.448
2018 Peek J, Lilic M, Montiel D, Milshteyn A, Woodworth I, Biggins JB, Ternei MA, Calle PY, Danziger M, Warrier T, Saito K, Braffman N, Fay A, Glickman MS, Darst SA, et al. Rifamycin congeners kanglemycins are active against rifampicin-resistant bacteria via a distinct mechanism. Nature Communications. 9: 4147. PMID 30297823 DOI: 10.1038/S41467-018-06587-2  0.302
2018 Kang JY, Mooney RA, Nedialkov Y, Saba J, Mishanina TV, Artsimovitch I, Landick R, Darst SA. Structural Basis for Transcript Elongation Control by NusG Family Universal Regulators. Cell. PMID 29887376 DOI: 10.1016/J.Cell.2018.05.017  0.493
2018 Kang JY, Mishanina TV, Bellecourt MJ, Mooney RA, Darst SA, Landick R. RNA Polymerase Accommodates a Pause RNA Hairpin by Global Conformational Rearrangements that Prolong Pausing. Molecular Cell. 69: 802-815.e1. PMID 29499135 DOI: 10.1016/J.Molcel.2018.01.018  0.506
2018 Boyaci H, Chen J, Lilic M, Palka M, Mooney RA, Landick R, Darst SA, Campbell EA. Fidaxomicin jamsRNA polymerase motions needed for initiation via RbpA contacts. Elife. 7. PMID 29480804 DOI: 10.7554/eLife.34823  0.361
2018 Boyaci H, Chen J, Lilic M, Palka M, Mooney RA, Landick R, Darst SA, Campbell EA. Author response: Fidaxomicin jams Mycobacterium tuberculosis RNA polymerase motions needed for initiation via RbpA contacts Elife. DOI: 10.7554/Elife.34823.030  0.351
2018 Kang JY, Mooney RA, Artsimovitch I, Landick R, Darst SA. Molecular mechanism of transcription pause inhibition by elongation factor NusG and RfaH Cell. DOI: 10.2210/Pdb6C6T/Pdb  0.328
2018 Boyaci H, Chen J, Lilic M, Palka M, Mooney RA, Landick R, Darst SA, Campbell EA. Fidaxomicin jamsMycobacterium tuberculosisRNA polymerase motions needed for initiation via RbpA contacts. Elife. 7. DOI: 10.2210/Pdb6C04/Pdb  0.393
2017 Chen J, Wassarman KM, Feng S, Leon K, Feklistov A, Winkelman JT, Li Z, Walz T, Campbell EA, Darst SA. 6S RNA Mimics B-Form DNA to Regulate Escherichia coli RNA Polymerase. Molecular Cell. PMID 28988932 DOI: 10.1016/J.Molcel.2017.09.006  0.501
2017 Hubin EA, Lilic M, Darst SA, Campbell EA. Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures. Nature Communications. 8: 16072. PMID 28703128 DOI: 10.1038/Ncomms16072  0.515
2017 Feklistov A, Bae B, Hauver J, Lass-Napiorkowska A, Kalesse M, Glaus F, Altmann KH, Heyduk T, Landick R, Darst SA. RNA polymerase motions during promoter melting. Science (New York, N.Y.). 356: 863-866. PMID 28546214 DOI: 10.1126/Science.Aam7858  0.423
2017 Kang JY, Olinares PD, Chen J, Campbell EA, Mustaev A, Chait BT, Gottesman ME, Darst SA. Structural basis of transcription arrest by coliphage HK022 nun in an Escherichia coli RNA polymerase elongation complex. Elife. 6. PMID 28318486 DOI: 10.7554/Elife.25478  0.461
2017 Campbell EA, Kamath S, Rajashankar KR, Wu M, Darst SA. Crystal structure of Aquifex aeolicus σ(N) bound to promoter DNA and the structure of σ(N)-holoenzyme. Proceedings of the National Academy of Sciences of the United States of America. PMID 28223493 DOI: 10.1073/Pnas.1619464114  0.404
2017 Hubin EA, Fay A, Xu C, Bean JM, Saecker RM, Glickman MS, Darst SA, Campbell EA. Structure and function of the mycobacterial transcription initiation complex with the essential regulator RbpA. Elife. 6. PMID 28067618 DOI: 10.7554/Elife.22520  0.445
2017 Kang JY, Olinares PDB, Chen J, Campbell EA, Mustaev A, Chait BT, Gottesman ME, Darst SA. Author response: Structural basis of transcription arrest by coliphage HK022 Nun in an Escherichia coli RNA polymerase elongation complex Elife. DOI: 10.7554/Elife.25478.042  0.499
2017 Darst S, Chen J, Kang JY, Campbell E. Structural biology of bacterial transcription Acta Crystallographica Section a Foundations and Advances. 73: a85-a85. DOI: 10.1107/S0108767317099159  0.407
2016 Wang G, Hauver J, Thomas Z, Darst SA, Pertsinidis A. Single-Molecule Real-Time 3D Imaging of the Transcription Cycle by Modulation Interferometry. Cell. 167: 1839-1852.e21. PMID 27984731 DOI: 10.1016/J.Cell.2016.11.032  0.387
2016 Garner AL, Rammohan J, Huynh JP, Onder LM, Chen J, Bae B, Jensen D, Weiss LA, Ruiz Manzano A, Darst SA, Campbell EA, Nickels BE, Galburt EA, Stallings CL. Effects of Increasing the Affinity of CarD for RNA Polymerase on Mycobacterium tuberculosis Growth, rRNA Transcription, and Virulence. Journal of Bacteriology. PMID 27920294 DOI: 10.1128/Jb.00698-16  0.444
2016 Hubin EA, Fay A, Xu C, Bean JM, Saecker RM, Glickman MS, Darst SA, Campbell EA. Author response: Structure and function of the mycobacterial transcription initiation complex with the essential regulator RbpA Elife. DOI: 10.7554/Elife.22520.047  0.367
2015 Bae B, Chen J, Davis E, Leon K, Darst SA, Campbell EA. CarD uses a minor groove wedge mechanism to stabilize the RNA polymerase open promoter complex. Elife. 4. PMID 26349034 DOI: 10.7554/Elife.08505  0.44
2015 Bae B, Feklistov A, Lass-Napiorkowska A, Landick R, Darst SA. Structure of a bacterial RNA polymerase holoenzyme open promoter complex. Elife. 4. PMID 26349032 DOI: 10.7554/Elife.08504  0.514
2015 Bae B, Nayak D, Ray A, Mustaev A, Landick R, Darst SA. CBR antimicrobials inhibit RNA polymerase via at least two bridge-helix cap-mediated effects on nucleotide addition. Proceedings of the National Academy of Sciences of the United States of America. PMID 26195788 DOI: 10.1073/Pnas.1502368112  0.485
2015 Hubin EA, Tabib-Salazar A, Humphrey LJ, Flack JE, Olinares PD, Darst SA, Campbell EA, Paget MS. Structural, functional, and genetic analyses of the actinobacterial transcription factor RbpA. Proceedings of the National Academy of Sciences of the United States of America. 112: 7171-6. PMID 26040003 DOI: 10.1073/Pnas.1504942112  0.444
2015 Bick MJ, Malik S, Mustaev A, Darst SA. TFIIB is only ∼9 Å away from the 5'-end of a trimeric RNA primer in a functional RNA polymerase II preinitiation complex. Plos One. 10: e0119007. PMID 25774659 DOI: 10.1371/Journal.Pone.0119007  0.504
2015 Davis E, Chen J, Leon K, Darst SA, Campbell EA. Mycobacterial RNA polymerase forms unstable open promoter complexes that are stabilized by CarD. Nucleic Acids Research. 43: 433-45. PMID 25510492 DOI: 10.1093/Nar/Gku1231  0.436
2015 Bae B, Chen J, Davis E, Leon K, Darst SA, Campbell EA. Author response: CarD uses a minor groove wedge mechanism to stabilize the RNA polymerase open promoter complex Elife. DOI: 10.7554/Elife.08505.024  0.427
2015 Bae B, Feklistov A, Lass-Napiorkowska A, Landick R, Darst SA. Author response: Structure of a bacterial RNA polymerase holoenzyme open promoter complex Elife. DOI: 10.7554/Elife.08504.019  0.477
2015 Wang G, Hauver J, Thomas Z, Darst SA, Pertsinidis A. Probing the Transcription Cycle in Real-Time with 3D Superresolution Interferometry Biophysical Journal. 108: 35a. DOI: 10.1016/J.Bpj.2014.11.219  0.397
2014 Hein PP, Kolb KE, Windgassen T, Bellecourt MJ, Darst SA, Mooney RA, Landick R. RNA polymerase pausing and nascent-RNA structure formation are linked through clamp-domain movement. Nature Structural & Molecular Biology. 21: 794-802. PMID 25108353 DOI: 10.1038/Nsmb.2867  0.486
2014 Feklístov A, Sharon BD, Darst SA, Gross CA. Bacterial sigma factors: a historical, structural, and genomic perspective. Annual Review of Microbiology. 68: 357-76. PMID 25002089 DOI: 10.1146/Annurev-Micro-092412-155737  0.449
2014 Liu Z, Frutos S, Bick MJ, Vila-Perelló M, Debelouchina GT, Darst SA, Muir TW. Structure of the branched intermediate in protein splicing. Proceedings of the National Academy of Sciences of the United States of America. 111: 8422-7. PMID 24778214 DOI: 10.1073/Pnas.1402942111  0.359
2014 Darst SA, Feklistov A, Gross CA. Promoter melting by an alternative σ, one base at a time. Nature Structural & Molecular Biology. 21: 350-1. PMID 24699085 DOI: 10.1038/Nsmb.2798  0.453
2013 Bae B, Davis E, Brown D, Campbell EA, Wigneshweraraj S, Darst SA. Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of σ70 domain 1.1. Proceedings of the National Academy of Sciences of the United States of America. 110: 19772-7. PMID 24218560 DOI: 10.1073/Pnas.1314576110  0.452
2013 Osmundson J, Dewell S, Darst SA. RNA-Seq reveals differential gene expression in Staphylococcus aureus with single-nucleotide resolution. Plos One. 8: e76572. PMID 24116120 DOI: 10.1371/Journal.Pone.0076572  0.403
2013 Feklistov A, Darst SA. Crystallographic analysis of an RNA polymerase σ-subunit fragment complexed with -10 promoter element ssDNA: quadruplex formation as a possible tool for engineering crystal contacts in protein-ssDNA complexes. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 69: 950-5. PMID 23989139 DOI: 10.1107/S1744309113020368  0.441
2013 Srivastava DB, Leon K, Osmundson J, Garner AL, Weiss LA, Westblade LF, Glickman MS, Landick R, Darst SA, Stallings CL, Campbell EA. Structure and function of CarD, an essential mycobacterial transcription factor. Proceedings of the National Academy of Sciences of the United States of America. 110: 12619-24. PMID 23858468 DOI: 10.1073/Pnas.1308270110  0.493
2013 Montero-Diez C, Deighan P, Osmundson J, Darst SA, Hochschild A. Phage-encoded inhibitor of Staphylococcus aureus transcription exerts context-dependent effects on promoter function in a modified Escherichia coli-based transcription system. Journal of Bacteriology. 195: 3621-8. PMID 23749973 DOI: 10.1128/Jb.00499-13  0.451
2013 Weixlbaumer A, Leon K, Landick R, Darst SA. Structural basis of transcriptional pausing in bacteria. Cell. 152: 431-41. PMID 23374340 DOI: 10.1016/J.Cell.2012.12.020  0.518
2012 Osmundson J, Montero-Diez C, Westblade LF, Hochschild A, Darst SA. Promoter-specific transcription inhibition in Staphylococcus aureus by a phage protein. Cell. 151: 1005-16. PMID 23178120 DOI: 10.1016/J.Cell.2012.10.034  0.467
2012 Howan K, Smith AJ, Westblade LF, Joly N, Grange W, Zorman S, Darst SA, Savery NJ, Strick TR. Initiation of transcription-coupled repair characterized at single-molecule resolution. Nature. 490: 431-4. PMID 22960746 DOI: 10.1038/Nature11430  0.391
2012 Weiss LA, Harrison PG, Nickels BE, Glickman MS, Campbell EA, Darst SA, Stallings CL. Interaction of CarD with RNA polymerase mediates Mycobacterium tuberculosis viability, rifampin resistance, and pathogenesis. Journal of Bacteriology. 194: 5621-31. PMID 22904282 DOI: 10.1128/Jb.00879-12  0.342
2011 Feklistov A, Darst SA. Structural basis for promoter-10 element recognition by the bacterial RNA polymerase σ subunit. Cell. 147: 1257-69. PMID 22136875 DOI: 10.1016/J.Cell.2011.10.041  0.459
2011 Twist KA, Campbell EA, Deighan P, Nechaev S, Jain V, Geiduschek EP, Hochschild A, Darst SA. Crystal structure of the bacteriophage T4 late-transcription coactivator gp33 with the β-subunit flap domain of Escherichia coli RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. 108: 19961-6. PMID 22135460 DOI: 10.1073/Pnas.1113328108  0.492
2011 Twist KA, Husnain SI, Franke JD, Jain D, Campbell EA, Nickels BE, Thomas MS, Darst SA, Westblade LF. A novel method for the production of in vivo-assembled, recombinant Escherichia coli RNA polymerase lacking the α C-terminal domain. Protein Science : a Publication of the Protein Society. 20: 986-95. PMID 21416542 DOI: 10.1002/Pro.622  0.415
2011 Srivastava DB, Darst SA. Derepression of bacterial transcription-repair coupling factor is associated with a profound conformational change. Journal of Molecular Biology. 406: 275-84. PMID 21185303 DOI: 10.1016/J.Jmb.2010.12.004  0.448
2011 Berdygulova Z, Westblade LF, Florens L, Koonin EV, Chait BT, Ramanculov E, Washburn MP, Darst SA, Severinov K, Minakhin L. Temporal regulation of gene expression of the Thermus thermophilus bacteriophage P23-45. Journal of Molecular Biology. 405: 125-42. PMID 21050864 DOI: 10.1016/J.Jmb.2010.10.049  0.38
2010 Bick MJ, Banik JJ, Darst SA, Brady SF. The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14. Acta Crystallographica. Section D, Biological Crystallography. 66: 1278-86. PMID 21123867 DOI: 10.1107/S0907444910036681  0.355
2010 Opalka N, Brown J, Lane WJ, Twist KA, Landick R, Asturias FJ, Darst SA. Complete structural model of Escherichia coli RNA polymerase from a hybrid approach. Plos Biology. 8. PMID 20856905 DOI: 10.1371/Journal.Pbio.1000483  0.414
2010 Westblade LF, Campbell EA, Pukhrambam C, Padovan JC, Nickels BE, Lamour V, Darst SA. Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction. Nucleic Acids Research. 38: 8357-69. PMID 20702425 DOI: 10.1093/Nar/Gkq692  0.485
2010 Subramanian R, Wilson-Kubalek EM, Arthur CP, Bick MJ, Campbell EA, Darst SA, Milligan RA, Kapoor TM. Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. Cell. 142: 433-43. PMID 20691902 DOI: 10.1016/J.Cell.2010.07.012  0.312
2010 Chen J, Darst SA, Thirumalai D. Promoter melting triggered by bacterial RNA polymerase occurs in three steps. Proceedings of the National Academy of Sciences of the United States of America. 107: 12523-8. PMID 20615963 DOI: 10.1073/Pnas.1003533107  0.429
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, ... ... Darst SA, 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  0.373
2010 Bick MJ, Banik JJ, Darst SA, Brady SF. Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. Biochemistry. 49: 4159-68. PMID 20361791 DOI: 10.1021/Bi100150V  0.349
2010 Devi PG, Campbell EA, Darst SA, Nickels BE. Utilization of variably spaced promoter-like elements by the bacterial RNA polymerase holoenzyme during early elongation. Molecular Microbiology. 75: 607-22. PMID 20070531 DOI: 10.1111/J.1365-2958.2009.07021.X  0.465
2010 Lane WJ, Darst SA. Molecular evolution of multisubunit RNA polymerases: sequence analysis. Journal of Molecular Biology. 395: 671-85. PMID 19895820 DOI: 10.1016/J.Jmb.2009.10.062  0.48
2010 Lane WJ, Darst SA. Molecular evolution of multisubunit RNA polymerases: structural analysis. Journal of Molecular Biology. 395: 686-704. PMID 19895816 DOI: 10.1016/J.Jmb.2009.10.063  0.481
2009 Feklistov A, Darst SA. Promoter recognition by bacterial alternative sigma factors: the price of high selectivity? Genes & Development. 23: 2371-5. PMID 19833764 DOI: 10.1101/Gad.1862609  0.434
2009 Lamour V, Westblade LF, Campbell EA, Darst SA. Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex. Journal of Structural Biology. 168: 352-6. PMID 19580872 DOI: 10.1016/J.Jsb.2009.07.001  0.481
2009 Bick MJ, Lamour V, Rajashankar KR, Gordiyenko Y, Robinson CV, Darst SA. How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda. Journal of Molecular Biology. 386: 163-77. PMID 19101565 DOI: 10.1016/J.Jmb.2008.12.006  0.336
2008 Schwartz EC, Shekhtman A, Dutta K, Pratt MR, Cowburn D, Darst S, Muir TW. A full-length group 1 bacterial sigma factor adopts a compact structure incompatible with DNA binding. Chemistry & Biology. 15: 1091-103. PMID 18940669 DOI: 10.1016/J.Chembiol.2008.09.008  0.474
2008 Feklistov A, Mekler V, Jiang Q, Westblade LF, Irschik H, Jansen R, Mustaev A, Darst SA, Ebright RH. Rifamycins do not function by allosteric modulation of binding of Mg2+ to the RNA polymerase active center. Proceedings of the National Academy of Sciences of the United States of America. 105: 14820-5. PMID 18787125 DOI: 10.1073/Pnas.0802822105  0.394
2008 Lamour V, Rutherford ST, Kuznedelov K, Ramagopal UA, Gourse RL, Severinov K, Darst SA. Crystal structure of Escherichia coli Rnk, a new RNA polymerase-interacting protein. Journal of Molecular Biology. 383: 367-79. PMID 18760284 DOI: 10.1016/J.Jmb.2008.08.011  0.507
2008 Campbell EA, Westblade LF, Darst SA. Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective. Current Opinion in Microbiology. 11: 121-7. PMID 18375176 DOI: 10.1016/J.Mib.2008.02.016  0.435
2008 Westblade LF, Minakhin L, Kuznedelov K, Tackett AJ, Chang EJ, Mooney RA, Vvedenskaya I, Wang QJ, Fenyö D, Rout MP, Landick R, Chait BT, Severinov K, Darst SA. Rapid isolation and identification of bacteriophage T4-encoded modifications of Escherichia coli RNA polymerase: a generic method to study bacteriophage/host interactions. Journal of Proteome Research. 7: 1244-50. PMID 18271525 DOI: 10.1021/Pr070451J  0.418
2007 Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA. A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria. Molecular Cell. 27: 793-805. PMID 17803943 DOI: 10.1016/J.Molcel.2007.07.009  0.39
2007 Patikoglou GA, Westblade LF, Campbell EA, Lamour V, Lane WJ, Darst SA. Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4. Journal of Molecular Biology. 372: 649-59. PMID 17681541 DOI: 10.1016/J.Jmb.2007.06.081  0.463
2007 Deaconescu AM, Savery N, Darst SA. The bacterial transcription repair coupling factor. Current Opinion in Structural Biology. 17: 96-102. PMID 17239578 DOI: 10.1016/J.Sbi.2007.01.005  0.486
2006 Sorenson MK, Darst SA. Disulfide cross-linking indicates that FlgM-bound and free sigma28 adopt similar conformations. Proceedings of the National Academy of Sciences of the United States of America. 103: 16722-7. PMID 17075066 DOI: 10.1073/Pnas.0606482103  0.471
2006 Lane WJ, Darst SA. The structural basis for promoter -35 element recognition by the group IV sigma factors. Plos Biology. 4: e269. PMID 16903784 DOI: 10.1371/Journal.Pbio.0040269  0.379
2006 Kuznedelov K, Lamour V, Patikoglou G, Chlenov M, Darst SA, Severinov K. Recombinant Thermus aquaticus RNA polymerase for structural studies. Journal of Molecular Biology. 359: 110-21. PMID 16618493 DOI: 10.1016/J.Jmb.2006.03.009  0.438
2006 Deaconescu AM, Chambers AL, Smith AJ, Nickels BE, Hochschild A, Savery NJ, Darst SA. Structural basis for bacterial transcription-coupled DNA repair. Cell. 124: 507-20. PMID 16469698 DOI: 10.1016/J.Cell.2005.11.045  0.48
2006 Lamour V, Hogan BP, Erie DA, Darst SA. Crystal structure of Thermus aquaticus Gfh1, a Gre-factor paralog that inhibits rather than stimulates transcript cleavage. Journal of Molecular Biology. 356: 179-88. PMID 16337964 DOI: 10.1016/J.Jmb.2005.10.083  0.517
2005 Deaconescu AM, Darst SA. Crystallization and preliminary structure determination of Escherichia coli Mfd, the transcription-repair coupling factor. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 61: 1062-4. PMID 16511235 DOI: 10.1107/S1744309105035876  0.435
2005 Mooney RA, Darst SA, Landick R. Sigma and RNA polymerase: an on-again, off-again relationship? Molecular Cell. 20: 335-45. PMID 16285916 DOI: 10.1016/J.Molcel.2005.10.015  0.48
2005 Chlenov M, Masuda S, Murakami KS, Nikiforov V, Darst SA, Mustaev A. Structure and function of lineage-specific sequence insertions in the bacterial RNA polymerase beta' subunit. Journal of Molecular Biology. 353: 138-54. PMID 16154587 DOI: 10.1016/J.Jmb.2005.07.073  0.546
2005 Jain D, Kim Y, Maxwell KL, Beasley S, Zhang R, Gussin GN, Edwards AM, Darst SA. Crystal structure of bacteriophage lambda cII and its DNA complex. Molecular Cell. 19: 259-69. PMID 16039594 DOI: 10.1016/J.Molcel.2005.06.006  0.526
2005 Gregory BD, Nickels BE, Darst SA, Hochschild A. An altered-specificity DNA-binding mutant of Escherichia coli sigma70 facilitates the analysis of sigma70 function in vivo. Molecular Microbiology. 56: 1208-19. PMID 15882415 DOI: 10.1111/J.1365-2958.2005.04624.X  0.418
2005 Campbell EA, Pavlova O, Zenkin N, Leon F, Irschik H, Jansen R, Severinov K, Darst SA. Structural, functional, and genetic analysis of sorangicin inhibition of bacterial RNA polymerase. The Embo Journal. 24: 674-82. PMID 15692574 DOI: 10.1038/Sj.Emboj.7600499  0.435
2004 Masuda S, Murakami KS, Wang S, Anders Olson C, Donigian J, Leon F, Darst SA, Campbell EA. Crystal structures of the ADP and ATP bound forms of the Bacillus anti-sigma factor SpoIIAB in complex with the anti-anti-sigma SpoIIAA. Journal of Molecular Biology. 340: 941-56. PMID 15236958 DOI: 10.1016/J.Jmb.2004.05.040  0.55
2004 Darst SA. New inhibitors targeting bacterial RNA polymerase. Trends in Biochemical Sciences. 29: 159-60. PMID 15124627 DOI: 10.1016/J.Tibs.2004.02.005  0.39
2004 Lawson CL, Swigon D, Murakami KS, Darst SA, Berman HM, Ebright RH. Catabolite activator protein: DNA binding and transcription activation. Current Opinion in Structural Biology. 14: 10-20. PMID 15102444 DOI: 10.1016/J.Sbi.2004.01.012  0.619
2004 Sorenson MK, Ray SS, Darst SA. Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation. Molecular Cell. 14: 127-38. PMID 15068809 DOI: 10.1016/S1097-2765(04)00150-9  0.507
2004 Jain D, Nickels BE, Sun L, Hochschild A, Darst SA. Structure of a ternary transcription activation complex. Molecular Cell. 13: 45-53. PMID 14731393 DOI: 10.1016/S1097-2765(03)00483-0  0.484
2003 Murakami KS, Masuda S, Darst SA. Crystallographic analysis of Thermus aquaticus RNA polymerase holoenzyme and a holoenzyme/promoter DNA complex. Methods in Enzymology. 370: 42-53. PMID 14712632 DOI: 10.1016/S0076-6879(03)70004-4  0.675
2003 Wilson KA, Kalkum M, Ottesen J, Yuzenkova J, Chait BT, Landick R, Muir T, Severinov K, Darst SA. Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail. Journal of the American Chemical Society. 125: 12475-83. PMID 14531691 DOI: 10.1021/Ja036756Q  0.386
2003 Opalka N, Chlenov M, Chacon P, Rice WJ, Wriggers W, Darst SA. Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase. Cell. 114: 335-45. PMID 12914698 DOI: 10.1016/S0092-8674(03)00600-7  0.532
2003 Dove SL, Darst SA, Hochschild A. Region 4 of sigma as a target for transcription regulation. Molecular Microbiology. 48: 863-74. PMID 12753182 DOI: 10.1046/J.1365-2958.2003.03467.X  0.323
2003 Campbell EA, Tupy JL, Gruber TM, Wang S, Sharp MM, Gross CA, Darst SA. Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA. Molecular Cell. 11: 1067-78. PMID 12718891 DOI: 10.1016/S1097-2765(03)00148-5  0.433
2003 Murakami KS, Darst SA. Bacterial RNA polymerases: the wholo story. Current Opinion in Structural Biology. 13: 31-9. PMID 12581657 DOI: 10.1016/S0959-440X(02)00005-2  0.643
2002 Nickels BE, Dove SL, Murakami KS, Darst SA, Hochschild A. Protein-protein and protein-DNA interactions of sigma70 region 4 involved in transcription activation by lambdacI. Journal of Molecular Biology. 324: 17-34. PMID 12421556 DOI: 10.1016/S0022-2836(02)01043-4  0.587
2002 Camarero JA, Shekhtman A, Campbell EA, Chlenov M, Gruber TM, Bryant DA, Darst SA, Cowburn D, Muir TW. Autoregulation of a bacterial sigma factor explored by using segmental isotopic labeling and NMR. Proceedings of the National Academy of Sciences of the United States of America. 99: 8536-41. PMID 12084914 DOI: 10.1073/Pnas.132033899  0.443
2002 Murakami KS, Masuda S, Campbell EA, Muzzin O, Darst SA. Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science (New York, N.Y.). 296: 1285-90. PMID 12016307 DOI: 10.1126/Science.1069595  0.665
2002 Murakami KS, Masuda S, Darst SA. Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution. Science (New York, N.Y.). 296: 1280-4. PMID 12016306 DOI: 10.1126/Science.1069594  0.657
2002 Campbell EA, Masuda S, Sun JL, Muzzin O, Olson CA, Wang S, Darst SA. Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF. Cell. 108: 795-807. PMID 11955433 DOI: 10.1016/S0092-8674(02)00662-1  0.428
2002 Campbell EA, Muzzin O, Chlenov M, Sun JL, Olson CA, Weinman O, Trester-Zedlitz ML, Darst SA. Structure of the bacterial RNA polymerase promoter specificity sigma subunit. Molecular Cell. 9: 527-39. PMID 11931761 DOI: 10.1016/S1097-2765(02)00470-7  0.512
2002 Darst SA, Opalka N, Chacon P, Polyakov A, Richter C, Zhang G, Wriggers W. Conformational flexibility of bacterial RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. 99: 4296-301. PMID 11904365 DOI: 10.1073/Pnas.052054099  0.494
2001 Darst SA. Bacterial RNA polymerase. Current Opinion in Structural Biology. 11: 155-62. PMID 11297923 DOI: 10.1016/S0959-440X(00)00185-8  0.514
2001 Campbell EA, Korzheva N, Mustaev A, Murakami K, Nair S, Goldfarb A, Darst SA. Structural mechanism for rifampicin inhibition of bacterial rna polymerase. Cell. 104: 901-12. PMID 11290327 DOI: 10.1016/S0092-8674(01)00286-0  0.663
2001 Naryshkina T, Mustaev A, Darst SA, Severinov K. The beta ' subunit of Escherichia coli RNA polymerase is not required for interaction with initiating nucleotide but is necessary for interaction with rifampicin. The Journal of Biological Chemistry. 276: 13308-13. PMID 11278820 DOI: 10.1074/jbc.M011041200  0.303
2001 Minakhin L, Bhagat S, Brunning A, Campbell EA, Darst SA, Ebright RH, Severinov K. Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly. Proceedings of the National Academy of Sciences of the United States of America. 98: 892-7. PMID 11158566 DOI: 10.1073/Pnas.98.3.892  0.478
2000 Korzheva N, Mustaev A, Kozlov M, Malhotra A, Nikiforov V, Goldfarb A, Darst SA. A structural model of transcription elongation. Science (New York, N.Y.). 289: 619-25. PMID 10915625 DOI: 10.1126/Science.289.5479.619  0.48
2000 Campbell EA, Darst SA. The anti-sigma factor SpoIIAB forms a 2:1 complex with sigma(F), contacting multiple conserved regions of the sigma factor. Journal of Molecular Biology. 300: 17-28. PMID 10864495 DOI: 10.1006/Jmbi.2000.3838  0.315
2000 Kulish D, Lee J, Lomakin I, Nowicka B, Das A, Darst S, Normet K, Borukhov S. The functional role of basic patch, a structural element of Escherichia coli transcript cleavage factors GreA and GreB Journal of Biological Chemistry. 275: 12789-12798. PMID 10777576 DOI: 10.1074/jbc.275.17.12789  0.358
2000 Opalka N, Mooney RA, Richter C, Severinov K, Landick R, Darst SA. Direct localization of a beta-subunit domain on the three-dimensional structure of Escherichia coli RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. 97: 617-22. PMID 10639128 DOI: 10.1073/Pnas.97.2.617  0.455
1999 Zhang G, Campbell EA, Minakhin L, Richter C, Severinov K, Darst SA. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell. 98: 811-24. PMID 10499798 DOI: 10.1016/S0092-8674(00)81515-9  0.509
1999 Loizos N, Darst SA. Mapping interactions of Escherichia coli GreB with RNA polymerase and ternary elongation complexes. The Journal of Biological Chemistry. 274: 23378-86. PMID 10438515 DOI: 10.1074/Jbc.274.33.23378  0.503
1999 DeRosier D, Stokes DL, Darst SA. Averaging data derived from images of helical structures with different symmetries. Journal of Molecular Biology. 289: 159-65. PMID 10339413 DOI: 10.1006/Jmbi.1999.2677  0.321
1998 Darst SA, Polyakov A, Richter C, Zhang G. Structural studies of Escherichia coli RNA polymerase. Cold Spring Harbor Symposia On Quantitative Biology. 63: 269-76. PMID 10384291 DOI: 10.1101/Sqb.1998.63.269  0.479
1998 Darst SA, Polyakov A, Richter C, Zhang G. Insights into Escherichia coli RNA polymerase structure from a combination of x-ray and electron crystallography. Journal of Structural Biology. 124: 115-22. PMID 10049799 DOI: 10.1006/Jsbi.1998.4057  0.526
1998 Polyakov A, Richter C, Malhotra A, Koulich D, Borukhov S, Darst SA. Visualization of the binding site for the transcript cleavage factor GreB on Escherichia coli RNA polymerase. Journal of Molecular Biology. 281: 465-73. PMID 9698562 DOI: 10.1006/Jmbi.1998.1958  0.545
1998 Zhang G, Darst SA. Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain. Science (New York, N.Y.). 281: 262-6. PMID 9657722 DOI: 10.1126/Science.281.5374.262  0.444
1998 Darst SA. A new twist on protein crystallization. Proceedings of the National Academy of Sciences of the United States of America. 95: 7848-9. PMID 9653102 DOI: 10.1073/Pnas.95.14.7848  0.353
1998 Severinova E, Severinov K, Darst SA. Inhibition of Escherichia coli RNA polymerase by bacteriophage T4 AsiA. Journal of Molecular Biology. 279: 9-18. PMID 9636696 DOI: 10.1006/Jmbi.1998.1742  0.453
1998 Muzzin O, Campbell EA, Xia L, Severinova E, Darst SA, Severinov K. Disruption of Escherichia coli hepA, an RNA polymerase-associated protein, causes UV sensitivity. The Journal of Biological Chemistry. 273: 15157-61. PMID 9614128 DOI: 10.1074/Jbc.273.24.15157  0.422
1997 Edwards AM, Darst SA, Hemming SA, Asturias FJ, David PR, Kornberg RD. [11] Two-dimensional protein crystals in aid of three-dimensional protein crystal growth. Methods in Enzymology. 276: 166-171. PMID 27799092 DOI: 10.1016/S0076-6879(97)76057-9  0.579
1997 Severinov K, Darst SA. A mutant RNA polymerase that forms unusual open promoter complexes. Proceedings of the National Academy of Sciences of the United States of America. 94: 13481-6. PMID 9391051 DOI: 10.1073/Pnas.94.25.13481  0.433
1997 Severinov K, Mooney R, Darst SA, Landick R. Tethering of the large subunits of Escherichia coli RNA polymerase. The Journal of Biological Chemistry. 272: 24137-40. PMID 9305860 DOI: 10.1074/Jbc.272.39.24137  0.419
1997 Wang Y, Severinov K, Loizos N, Fenyö D, Heyduk E, Heyduk T, Chait BT, Darst SA. Determinants for Escherichia coli RNA polymerase assembly within the beta subunit. Journal of Molecular Biology. 270: 648-62. PMID 9245594 DOI: 10.1006/Jmbi.1997.1139  0.33
1997 Koulich D, Orlova M, Malhotra A, Sali A, Darst SA, Borukhov S. Domain organization of Escherichia coli transcript cleavage factors GreA and GreB. The Journal of Biological Chemistry. 272: 7201-10. PMID 9054416 DOI: 10.1074/Jbc.272.11.7201  0.48
1997 Edwards AM, Darst SA, Hemming SA, Asturias FJ, David PR, Kornberg RD. Two-dimensional protein crystals in aid of three-dimensional protein crystal growth Methods in Enzymology. 276: 166-171. DOI: 10.1016/S0076-6879(97)76057-9  0.494
1996 Severinova E, Severinov K, Fenyö D, Marr M, Brody EN, Roberts JW, Chait BT, Darst SA. Domain organization of the Escherichia coli RNA polymerase sigma 70 subunit. Journal of Molecular Biology. 263: 637-47. PMID 8947564 DOI: 10.1006/Jmbi.1996.0604  0.495
1996 Severinov K, Mustaev A, Kukarin A, Muzzin O, Bass I, Darst SA, Goldfarb A. Structural modules of the large subunits of RNA polymerase. Introducing archaebacterial and chloroplast split sites in the beta and beta' subunits of Escherichia coli RNA polymerase. The Journal of Biological Chemistry. 271: 27969-74. PMID 8910400 DOI: 10.1074/Jbc.271.44.27969  0.456
1996 Malhotra A, Severinova E, Darst SA. Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase. Cell. 87: 127-36. PMID 8858155 DOI: 10.1016/S0092-8674(00)81329-X  0.549
1996 Meredith GD, Chang WH, Li Y, Bushnell DA, Darst SA, Kornberg RD. The C-terminal domain revealed in the structure of RNA polymerase II. Journal of Molecular Biology. 258: 413-9. PMID 8642599 DOI: 10.1006/Jmbi.1996.0258  0.714
1995 Darst SA, Edwards AM. Epitaxial growth of protein crystals from two-dimensional crystals on lipid layers. Current Opinion in Structural Biology. 5: 640-4. PMID 8574699 DOI: 10.1016/0959-440X(95)80056-5  0.356
1995 Polyakov A, Severinova E, Darst SA. Three-dimensional structure of E. coli core RNA polymerase: promoter binding and elongation conformations of the enzyme. Cell. 83: 365-73. PMID 8521466 DOI: 10.1016/0092-8674(95)90114-0  0.451
1995 Hemming SA, Bochkarev A, Darst SA, Kornberg RD, Ala P, Yang DS, Edwards AM. The mechanism of protein crystal growth from lipid layers. Journal of Molecular Biology. 246: 308-16. PMID 7869382 DOI: 10.1006/Jmbi.1994.0086  0.541
1995 Stebbins CE, Borukhov S, Oriova M, Polyakov A, Goldfarb A, Darst SA. Crystal structure of the GreA transcript cleavage factor from Escherichia coli Nature. 373: 636-640. PMID 7854424 DOI: 10.1038/373636A0  0.551
1995 Severinov K, Mustaev A, Severinova E, Bass I, Kashlev M, Landick R, Nikiforov V, Goldfarb A, Darst SA. Assembly of functional Escherichia coli RNA polymerase containing β subunit fragments Proceedings of the National Academy of Sciences of the United States of America. 92: 4591-4595. PMID 7753849 DOI: 10.1073/Pnas.92.10.4591  0.379
1995 Severinov K, Markov D, Severinova E, Nikiforov V, Landick R, Darst SA, Goldfarb A. Streptolydigin-resistant mutants in an evolutionarily conserved region of the beta' subunit of Escherichia coli RNA polymerase. The Journal of Biological Chemistry. 270: 23926-9. PMID 7592584 DOI: 10.1074/Jbc.270.41.23926  0.375
1995 Severinov K, Mustaev A, Severinova E, Kozlov M, Darst SA, Goldfarb A. The beta subunit Rif-cluster I is only angstroms away from the active center of Escherichia coli RNA polymerase. The Journal of Biological Chemistry. 270: 29428-32. PMID 7493980 DOI: 10.1074/Jbc.270.49.29428  0.41
1994 Severinov K, Fenyo D, Severinova E, Mustaev A, Chait BT, Goldfarb A, Darst SA. The σ subunit conserved region 3 is part of '5'-face' of active center of Escherichia coli RNA polymerase Journal of Biological Chemistry. 269: 20826-20828. PMID 8063697  0.34
1994 Darst SA, Stebbins CE, Borukhov S, Orlova M, Feng G, Landick R, Goldfarb A. Crystallization of GreA, a transcript cleavage factor from Escherichia coli Journal of Molecular Biology. 242: 582-585. PMID 7932713 DOI: 10.1006/Jmbi.1994.1603  0.466
1994 Edwards AM, Darst SA, Hemming SA, Li Y, Kornberg RD. Epitaxial growth of protein crystals on lipid layers. Nature Structural Biology. 1: 195-7. PMID 7656038 DOI: 10.1038/nsb0394-195  0.497
1993 Ku AC, Darst SA, Robertson CR, Gast AP, Kornberg RD. Molecular analysis of two-dimensional protein crystallization Journal of Physical Chemistry. 97: 3013-3016. DOI: 10.1021/J100114A030  0.672
1992 Kornberg RD, Chasman DI, Darst SA, Edwards AM, Feaver WJ, Flanagan PM, Gileadi O, Henry NL, Kelleher RJ, Li Y, Lorch Y, Lue NF, Sayre MH, Tschochner H. 13 Yeast RNA Polymerase II Transcription In Vitro: General Initiation Factors; Novel Mediator of Transcriptional Activation; Three-dimensional Structure of RNA Polymerase II Cold Spring Harbor Monograph Archive. 349-362. DOI: 10.1101/087969425.22A.349  0.726
1992 Ku AC, Darst SA, Kornberg RD, Robertson CR, Gast AP. Dendritic growth of two-dimensional protein crystals Langmuir. 8: 2357-2360. DOI: 10.1021/La00046A003  0.656
1991 Darst SA, Edwards AM, Kubalek EW, Kornberg RD. Three-dimensional structure of yeast RNA polymerase II at 16 A resolution. Cell. 66: 121-8. PMID 2070414 DOI: 10.1016/0092-8674(91)90144-N  0.59
1991 Kubalek EW, Kornberg RD, Darst SA. Improved transfer of two-dimensional crystals from the air/water interface to specimen support grids for high-resolution analysis by electron microscopy. Ultramicroscopy. 35: 295-304. PMID 1926634 DOI: 10.1016/0304-3991(91)90082-H  0.478
1991 Darst SA, Kubalek EW, Edwards AM, Kornberg RD. Two-dimensional and epitaxial crystallization of a mutant form of yeast RNA polymerase II. Journal of Molecular Biology. 221: 347-57. PMID 1920413 DOI: 10.1016/0022-2836(91)80223-H  0.58
1991 Darst SA, Ahlers M, Meller PH, Kubalek EW, Blankenburg R, Ribi HO, Ringsdorf H, Kornberg RD. Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules. Biophysical Journal. 59: 387-96. PMID 1901232 DOI: 10.1016/S0006-3495(91)82232-9  0.527
1991 Kornberg RD, Darst SA. Two-dimensional crystals of proteins on lipid layers Current Opinion in Structural Biology. 1: 642-646. DOI: 10.1016/S0959-440X(05)80090-9  0.497
1990 Schultz P, Célia H, Riva M, Darst SA, Colin P, Kornberg RD, Sentenac A, Oudet P. Structural study of the yeast RNA polymerase A. Electron microscopy of lipid-bound molecules and two-dimensional crystals. Journal of Molecular Biology. 216: 353-62. PMID 2254934 DOI: 10.1016/S0022-2836(05)80326-2  0.593
1990 Edwards AM, Darst SA, Feaver WJ, Thompson NE, Burgess RR, Kornberg RD. Purification and lipid-layer crystallization of yeast RNA polymerase II. Proceedings of the National Academy of Sciences of the United States of America. 87: 2122-6. PMID 2179949 DOI: 10.1073/Pnas.87.6.2122  0.647
1989 Darst SA, Kubalek EW, Kornberg RD. Three-dimensional structure of Escherichia coli RNA polymerase holoenzyme determined by electron crystallography. Nature. 340: 730-2. PMID 2671751 DOI: 10.1038/340730a0  0.645
1988 Darst SA, Robertson CR, Berzofsky JA. Adsorption of the protein antigen myoglobin affects the binding of conformation-specific monoclonal antibodies. Biophysical Journal. 53: 533-9. PMID 3382711 DOI: 10.1016/S0006-3495(88)83133-3  0.467
1988 Darst SA, Ribi HO, Pierce DW, Kornberg RD. Two-dimensional crystals of Escherichia coli RNA polymerase holoenzyme on positively charged lipid layers. Journal of Molecular Biology. 203: 269-73. PMID 3054121 DOI: 10.1016/0022-2836(88)90107-6  0.565
1987 Cheng YL, Darst SA, Robertson CR. Bovine serum albumin adsorption and desorption rates on solid surfaces with varying surface properties Journal of Colloid and Interface Science. 118: 212-223. DOI: 10.1016/0021-9797(87)90450-4  0.449
1986 Darst SA, Robertson CR, Berzofsky JA. Myoglobin adsorption onto crosslinked polydimethylsiloxane Journal of Colloid and Interface Science. 111: 466-474. DOI: 10.1016/0021-9797(86)90049-4  0.425
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