Robert M. Stroud - Publications

Affiliations: 
University of California, San Francisco, San Francisco, CA 
Area:
membrane protein characterizations and crystal structures
Website:
http://www.msg.ucsf.edu/stroud/people/stroud.htm

294 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
2022 Dickinson MS, Lu J, Gupta M, Marten I, Hedrich R, Stroud RM. Molecular basis of multistep voltage activation in plant two-pore channel 1. Proceedings of the National Academy of Sciences of the United States of America. 119. PMID 35210362 DOI: 10.1073/pnas.2110936119  0.803
2021 Dickinson MS, Pourmal S, Gupta M, Bi M, Stroud RM. Symmetry Reduction in a Hyperpolarization-Activated Homotetrameric Ion Channel. Biochemistry. PMID 34964607 DOI: 10.1021/acs.biochem.1c00654  0.779
2021 Verba K, Gupta M, Azumaya C, Moritz M, Pourmal S, Diallo A, Merz G, Jang G, Bouhaddou M, Fossati A, Brilot A, Diwanji D, Hernandez E, Herrera N, Kratochvil H, ... ... Stroud R, et al. CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes. Research Square. PMID 34031651 DOI: 10.21203/rs.3.rs-515215/v1  0.81
2021 Gupta M, Azumaya CM, Moritz M, Pourmal S, Diallo A, Merz GE, Jang G, Bouhaddou M, Fossati A, Brilot AF, Diwanji D, Hernandez E, Herrera N, Kratochvil HT, Lam VL, ... ... Stroud RM, et al. CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes. Biorxiv : the Preprint Server For Biology. PMID 34013269 DOI: 10.1101/2021.05.10.443524  0.81
2021 Li F, Egea PF, Vecchio AJ, Asial I, Gupta M, Paulino J, Bajaj R, Dickinson MS, Ferguson-Miller S, Monk BC, Stroud RM. Highlighting membrane protein structure and function: A celebration of the Protein Data Bank. The Journal of Biological Chemistry. 100557. PMID 33744283 DOI: 10.1016/j.jbc.2021.100557  0.816
2020 Miller-Vedam LE, Bräuning B, Popova KD, Schirle Oakdale NT, Bonnar JL, Prabu JR, Boydston EA, Sevillano N, Shurtleff MJ, Stroud RM, Craik CS, Schulman BA, Frost A, Weissman JS. Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients. Elife. 9. PMID 33236988 DOI: 10.7554/eLife.62611  0.436
2020 Gordon DE, Hiatt J, Bouhaddou M, Rezelj VV, Ulferts S, Braberg H, Jureka AS, Obernier K, Guo JZ, Batra J, Kaake RM, Weckstein AR, Owens TW, Gupta M, Pourmal S, ... ... Stroud RM, et al. Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms. Science (New York, N.Y.). PMID 33060197 DOI: 10.1126/science.abe9403  0.775
2020 Kumar H, Finer-Moore J, Smirnova I, Kasho V, Pardon E, Steyaert J, Kaback HR, Stroud RM. Diversity in kinetics correlated with structure in nano body-stabilized LacY. Plos One. 15: e0232846. PMID 32380514 DOI: 10.1371/Journal.Pone.0232846  0.491
2020 Gordon DE, Jang GM, Bouhaddou M, Xu J, Obernier K, White KM, O'Meara MJ, Rezelj VV, Guo JZ, Swaney DL, Tummino TA, Huettenhain R, Kaake RM, Richards AL, Tutuncuoglu B, ... ... Stroud RM, et al. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature. PMID 32353859 DOI: 10.1038/S41586-020-2286-9  0.75
2020 Dickinson MS, Myasnikov A, Eriksen J, Poweleit N, Stroud RM. Resting state structure of the hyperdepolarization activated two-pore channel 3. Proceedings of the National Academy of Sciences of the United States of America. PMID 31924746 DOI: 10.1073/Pnas.1915144117  0.799
2020 Gupta M, Stroud RM. Structural Analysis of a Phosphate ‘Transceptor’ Biophysical Journal. 118: 210a. DOI: 10.1016/J.Bpj.2019.11.1255  0.443
2019 Vecchio AJ, Stroud RM. Claudin-9 structures reveal mechanism for toxin-induced gut barrier breakdown. Proceedings of the National Academy of Sciences of the United States of America. PMID 31434788 DOI: 10.1073/Pnas.1908929116  0.481
2019 Vecchio AJ, Stroud RM. High-Throughput Nano-Scale Characterization of Membrane Proteins Using Fluorescence-Detection Size-Exclusion Chromatography. Methods in Molecular Biology (Clifton, N.J.). 2025: 361-388. PMID 31267462 DOI: 10.1007/978-1-4939-9624-7_17  0.481
2019 Torres SE, Gallagher CM, Plate L, Gupta M, Liem CR, Guo X, Tian R, Stroud RM, Kampmann M, Weissman JS, Walter P. Ceapins block the unfolded protein response sensor ATF6α by inducing a neomorphic inter-organelle tether. Elife. 8. PMID 31149896 DOI: 10.7554/Elife.46595  0.539
2019 Leano JB, Batarni S, Eriksen J, Juge N, Pak JE, Kimura-Someya T, Robles-Colmenares Y, Moriyama Y, Stroud RM, Edwards RH. Structures suggest a mechanism for energy coupling by a family of organic anion transporters. Plos Biology. 17: e3000260. PMID 31083648 DOI: 10.1371/Journal.Pbio.3000260  0.427
2019 Torres SE, Gallagher CM, Plate L, Gupta M, Liem CR, Guo X, Tian R, Stroud RM, Kampmann M, Weissman JS, Walter P. Author response: Ceapins block the unfolded protein response sensor ATF6α by inducing a neomorphic inter-organelle tether Elife. DOI: 10.7554/Elife.46595.022  0.485
2018 Kintzer AF, Green EM, Dominik PK, Bridges M, Armache JP, Deneka D, Kim SS, Hubbell W, Kossiakoff AA, Cheng Y, Stroud RM. Structural basis for activation of voltage sensor domains in an ion channel TPC1. Proceedings of the National Academy of Sciences of the United States of America. PMID 30190435 DOI: 10.1073/pnas.1805651115  0.727
2018 Chen SH, Jang GM, Hüttenhain R, Gordon DE, Du D, Newton BW, Johnson JR, Hiatt J, Hultquist JF, Johnson TL, Liu YL, Burton LA, Ye J, Reichermeier KM, Stroud RM, et al. CRL4 targets Elongin C for ubiquitination and degradation to modulate CRL5 signaling. The Embo Journal. PMID 30166453 DOI: 10.15252/Embj.201797508  0.405
2018 Kumar H, Finer-Moore JS, Jiang X, Smirnova I, Kasho V, Pardon E, Steyaert J, Kaback HR, Stroud RM. Crystal Structure of a ligand-bound LacY-Nanobody Complex. Proceedings of the National Academy of Sciences of the United States of America. PMID 30108145 DOI: 10.1073/Pnas.1801774115  0.521
2018 Finer-Moore JS, Lee TT, Stroud RM. A Single Mutation Traps a Half-Sites Reactive Enzyme in Midstream, Explaining Asymmetry in Hydride Transfer. Biochemistry. PMID 29717875 DOI: 10.1021/Acs.Biochem.8B00176  0.447
2018 Stroud R, Kintzer AF. Structure and Mechanisms of Selectivity Gating, Inhibition and Activation in an Ion Channel Biophysical Journal. 114: 34a-35a. DOI: 10.1016/J.Bpj.2017.11.247  0.431
2018 Kumar H, Kaback HR, Stroud RM. Lactose Permease: Mechanism through Structures Biophysical Journal. 114: 333a. DOI: 10.1016/J.Bpj.2017.11.1865  0.443
2017 Kintzer AF, Stroud RM. On the Structure and Mechanism of Two-Pore Channels. The Febs Journal. PMID 28656706 DOI: 10.1111/Febs.14154  0.476
2017 Nöll A, Thomas C, Herbring V, Zollmann T, Barth K, Mehdipour AR, Tomasiak TM, Brüchert S, Joseph B, Abele R, Oliéric V, Wang M, Diederichs K, Hummer G, Stroud RM, et al. Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP. Proceedings of the National Academy of Sciences of the United States of America. PMID 28069938 DOI: 10.1073/Pnas.1620009114  0.498
2017 Stroud RM. Two Mechanisms in One Family: Packaging of Glutamate into Synaptic Vesicles against a Proton Gradient, a Transporter Driven by Membrane Potential, versus a Homolog Driven Downhill with Proton Gradients Biophysical Journal. 112: 127a. DOI: 10.1016/J.Bpj.2016.11.709  0.418
2017 Kintzer AF, Stroud RM. Structure Inhibition and Regulation of a Two-Pore Channel TPC1 Biophysical Journal. 112: 21a. DOI: 10.1016/J.Bpj.2016.11.149  0.487
2016 Galilee M, Britan-Rosich E, Griner SL, Uysal S, Baumgärtel V, Lamb DC, Kossiakoff AA, Kotler M, Stroud RM, Marx A, Alian A. The Preserved HTH-Docking Cleft of HIV-1 Integrase Is Functionally Critical. Structure (London, England : 1993). PMID 27692964 DOI: 10.1016/J.Str.2016.08.015  0.763
2016 Thurtle-Schmidt BH, Stroud RM. Structure of Bor1 supports an elevator transport mechanism for SLC4 anion exchangers. Proceedings of the National Academy of Sciences of the United States of America. PMID 27601653 DOI: 10.1073/Pnas.1612603113  0.426
2016 Chaudhary S, Saha S, Thamminana S, Stroud RM. Small-Scale Screening to Large-Scale Over-Expression of Human Membrane Proteins for Structural Studies. Methods in Molecular Biology (Clifton, N.J.). 1432: 203-21. PMID 27485338 DOI: 10.1007/978-1-4939-3637-3_13  0.445
2016 Boswell-Casteel RC, Johnson JM, Stroud RM, Hays FA. Integral Membrane Protein Expression in Saccharomyces cerevisiae. Methods in Molecular Biology (Clifton, N.J.). 1432: 163-86. PMID 27485336 DOI: 10.1007/978-1-4939-3637-3_11  0.789
2016 Shcherbatko A, Foletti D, Poulsen K, Strop P, Zhu G, Hasa-Moreno A, Melton Witt J, Loo C, Krimm S, Pios A, Yu J, Brown C, Lee JK, Stroud R, Rajpal A, et al. Modulation of P2X3 and P2X2/3 receptors by monoclonal antibodies. The Journal of Biological Chemistry. PMID 27129281 DOI: 10.1074/Jbc.M116.722330  0.611
2016 Kapoor K, Finer-Moore JS, Pedersen BP, Caboni L, Waight A, Hillig RC, Bringmann P, Heisler I, Müller T, Siebeneicher H, Stroud RM. Mechanism of inhibition of human glucose transporter GLUT1 is conserved between cytochalasin B and phenylalanine amides. Proceedings of the National Academy of Sciences of the United States of America. PMID 27078104 DOI: 10.1073/Pnas.1603735113  0.448
2016 Kintzer AF, Stroud RM. Structure, inhibition and regulation of two-pore channel TPC1 from Arabidopsis thaliana. Nature. 531: 258-62. PMID 26961658 DOI: 10.1038/Nature17194  0.496
2015 Finer-Moore J, Czudnochowski N, O'Connell JD, Wang AL, Stroud RM. Crystal Structure of the Human tRNA m(1)A58 Methyltransferase-tRNA3(Lys) Complex: Refolding of Substrate tRNA Allows Access to the Methylation Target. Journal of Molecular Biology. PMID 26470919 DOI: 10.1016/J.Jmb.2015.10.005  0.746
2015 Kumar H, Finer-Moore JS, Kaback HR, Stroud RM. Structure of LacY with an α-substituted galactoside: Connecting the binding site to the protonation site. Proceedings of the National Academy of Sciences of the United States of America. 112: 9004-9. PMID 26157133 DOI: 10.1073/Pnas.1509854112  0.446
2015 Rosenberg OS, Dovala D, Li X, Connolly L, Bendebury A, Finer-Moore J, Holton J, Cheng Y, Stroud RM, Cox JS. Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. Cell. 161: 501-12. PMID 25865481 DOI: 10.1016/J.Cell.2015.03.040  0.737
2015 Salo-Ahen OM, Tochowicz A, Pozzi C, Cardinale D, Ferrari S, Boum Y, Mangani S, Stroud RM, Saxena P, Myllykallio H, Costi MP, Ponterini G, Wade RC. Hotspots in an obligate homodimeric anticancer target. Structural and functional effects of interfacial mutations in human thymidylate synthase. Journal of Medicinal Chemistry. 58: 3572-81. PMID 25798950 DOI: 10.1021/Acs.Jmedchem.5B00137  0.432
2015 Kim JM, Wu S, Tomasiak TM, Mergel C, Winter MB, Stiller SB, Robles-Colmanares Y, Stroud RM, Tampé R, Craik CS, Cheng Y. Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter Nature. 517: 396-400. PMID 25363761 DOI: 10.1038/Nature13872  0.475
2014 Tomasiak TM, Pedersen BP, Chaudhary S, Rodriguez A, Colmanares YR, Roe-Zurz Z, Thamminana S, Tessema M, Stroud RM. General qPCR and Plate Reader Methods for Rapid Optimization of Membrane Protein Purification and Crystallization Using Thermostability Assays. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. 77: 29.11.1-29.11.14. PMID 25081745 DOI: 10.1002/0471140864.Ps2911S77  0.479
2014 Miercke LJ, Robbins RA, Stroud RM. Tetra detector analysis of membrane proteins. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. 77: 29.10.1-29.10.30. PMID 25081744 DOI: 10.1002/0471140864.Ps2910S77  0.417
2014 Lohse MB, Rosenberg OS, Cox JS, Stroud RM, Finer-Moore JS, Johnson AD. Structure of a new DNA-binding domain which regulates pathogenesis in a wide variety of fungi. Proceedings of the National Academy of Sciences of the United States of America. 111: 10404-10. PMID 24994900 DOI: 10.1073/Pnas.1410110111  0.732
2014 Monk BC, Tomasiak TM, Keniya MV, Huschmann FU, Tyndall JDA, O'Connell JD, Cannon RD, McDonald JG, Rodriguez A, Finer-Moore JS, Stroud RM. Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer Proceedings of the National Academy of Sciences of the United States of America. 111: 3865-3870. PMID 24613931 DOI: 10.1073/Pnas.1324245111  0.519
2014 Kumar H, Kasho V, Smirnova I, Finer-Moore JS, Kaback HR, Stroud RM. Structure of sugar-bound LacY. Proceedings of the National Academy of Sciences of the United States of America. 111: 1784-8. PMID 24453216 DOI: 10.1073/Pnas.1324141111  0.534
2014 Czudnochowski N, Ashley GW, Santi DV, Alian A, Finer-Moore J, Stroud RM. The mechanism of pseudouridine synthases from a covalent complex with RNA, and alternate specificity for U2605 versus U2604 between close homologs Nucleic Acids Research. 42: 2037-2048. PMID 24214967 DOI: 10.1093/Nar/Gkt1050  0.762
2013 Pak JE, Ekendé EN, Kifle EG, O'Connell JD, De Angelis F, Tessema MB, Derfoufi KM, Robles-Colmenares Y, Robbins RA, Goormaghtigh E, Vandenbussche G, Stroud RM. Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter Proceedings of the National Academy of Sciences of the United States of America. 110: 18484-18489. PMID 24173033 DOI: 10.1073/Pnas.1318705110  0.453
2013 Czudnochowski N, Wang AL, Finer-Moore J, Stroud RM. In human pseudouridine synthase 1 (hPus1), a C-terminal helical insert blocks tRNA from binding in the same orientation as in the Pus1 bacterial homologue TruA, consistent with their different target selectivities Journal of Molecular Biology. 425: 3875-3887. PMID 23707380 DOI: 10.1016/J.Jmb.2013.05.014  0.778
2013 Wang Z, Sapienza PJ, Abeysinghe T, Luzum C, Lee AL, Finer-Moore JS, Stroud RM, Kohen A. Mg2+ binds to the surface of thymidylate synthase and affects hydride transfer at the interior active site. Journal of the American Chemical Society. 135: 7583-92. PMID 23611499 DOI: 10.1021/Ja400761X  0.443
2013 Pedersen BP, Kumar H, Waight AB, Risenmay AJ, Roe-Zurz Z, Chau BH, Schlessinger A, Bonomi M, Harries W, Sali A, Johri AK, Stroud RM. Crystal structure of a eukaryotic phosphate transporter. Nature. 496: 533-6. PMID 23542591 DOI: 10.1038/Nature12042  0.782
2013 Pieper U, Schlessinger A, Kloppmann E, Chang GA, Chou JJ, Dumont ME, Fox BG, Fromme P, Hendrickson WA, Malkowski MG, Rees DC, Stokes DL, Stowell MH, Wiener MC, Rost B, ... Stroud RM, et al. Coordinating the impact of structural genomics on the human α-helical transmembrane proteome. Nature Structural & Molecular Biology. 20: 135-8. PMID 23381628 DOI: 10.1038/Nsmb.2508  0.699
2013 Chae PS, Gotfryd K, Pacyna J, Miercke LJW, Rasmussen SGF, Robbins RA, Rana RR, Loland CJ, Kobilka B, Stroud R, Byrne B, Gether U, Gellman SH. Correction to “Tandem Facial Amphiphiles for Membrane Protein Stabilization” Journal of the American Chemical Society. 135: 12922-12922. DOI: 10.1021/Ja407245M  0.576
2012 Metzger LE, Lee JK, Finer-Moore JS, Raetz CR, Stroud RM. LpxI structures reveal how a lipid A precursor is synthesized. Nature Structural & Molecular Biology. 19: 1132-8. PMID 23042606 DOI: 10.1038/Nsmb.2393  0.638
2012 Wang Z, Abeysinghe T, Finer-Moore JS, Stroud RM, Kohen A. A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase. Journal of the American Chemical Society. 134: 17722-30. PMID 23034004 DOI: 10.1021/Ja307859M  0.451
2012 Pozzi C, Ferrari S, Cortesi D, Luciani R, Stroud RM, Catalano A, Costi MP, Mangani S. The structure of Enterococcus faecalis thymidylate synthase provides clues about folate bacterial metabolism. Acta Crystallographica. Section D, Biological Crystallography. 68: 1232-41. PMID 22948925 DOI: 10.1107/S0907444912026236  0.458
2012 Egea PF, Muller-Steffner H, Kuhn I, Cakir-Kiefer C, Oppenheimer NJ, Stroud RM, Kellenberger E, Schuber F. Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the X-ray structures of its Michaelis complex and covalently-trapped intermediates. Plos One. 7: e34918. PMID 22529956 DOI: 10.1371/Journal.Pone.0034918  0.756
2012 Wu S, Avila-Sakar A, Kim J, Booth DS, Greenberg CH, Rossi A, Liao M, Li X, Alian A, Griner SL, Juge N, Yu Y, Mergel CM, Chaparro-Riggers J, Strop P, ... ... Stroud RM, et al. Fabs enable single particle cryoEM studies of small proteins. Structure (London, England : 1993). 20: 582-92. PMID 22483106 DOI: 10.1016/J.Str.2012.02.017  0.424
2012 Chaudhary S, Pak JE, Gruswitz F, Sharma V, Stroud RM. Overexpressing human membrane proteins in stably transfected and clonal human embryonic kidney 293S cells Nature Protocols. 7: 453-466. PMID 22322218 DOI: 10.1038/Nprot.2011.453  0.467
2012 Fromme P, Chapman H, Kupitz C, Hunter MS, Kirian RA, Barty A, White TA, Aquilla A, Stellato F, Beyerlein K, DePonte DP, Frank M, Schlichting I, Shoeman R, Lomb L, ... ... Stroud R, et al. Femtosecond nanocrystallography of membrane proteins opens a new era for structural biology Acta Crystallographica Section a Foundations of Crystallography. 68: s28-s28. DOI: 10.1107/S0108767312099461  0.483
2012 Metzger LE, Lee JK, Finer-Moore JS, Raetz CR, Stroud RM. LpxI: A Novel Phosphosaccharolipid Hydrolase Biophysical Journal. 102: 303a. DOI: 10.1016/J.Bpj.2011.11.1675  0.682
2011 Kim J, Stroud RM, Craik CS. Rapid identification of recombinant Fabs that bind to membrane proteins Methods. 55: 303-309. PMID 21958987 DOI: 10.1016/J.Ymeth.2011.09.012  0.49
2011 Chaudhary S, Pak JE, Pedersen BP, Bang LJ, Zhang LB, Ngaw SMM, Green RG, Sharma V, Stroud RM. Efficient expression screening of human membrane proteins in transiently transfected Human Embryonic Kidney 293S cells Methods. 55: 273-280. PMID 21925269 DOI: 10.1016/J.Ymeth.2011.08.018  0.426
2011 Rosenberg OS, Dovey C, Tempesta M, Robbins RA, Finer-Moore JS, Stroud RM, Cox JS. EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure among helix-turn-helix proteins Proceedings of the National Academy of Sciences of the United States of America. 108: 13450-13455. PMID 21795602 DOI: 10.1073/Pnas.1110242108  0.732
2011 Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Stroud RM, Zhang C, Shokat KM, Walter P. Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1. Bmc Biology. 9: 48. PMID 21729334 DOI: 10.1186/1741-7007-9-48  0.776
2011 Korennykh AV, Korostelev AA, Egea PF, Finer-Moore J, Stroud RM, Zhang C, Shokat KM, Walter P. Structural and functional basis for RNA cleavage by Ire1. Bmc Biology. 9: 47. PMID 21729333 DOI: 10.1186/1741-7007-9-47  0.79
2011 Stroud RM. New tools in membrane protein determination. F1000 Biology Reports. 3: 8. PMID 21655333 DOI: 10.3410/B3-8  0.489
2010 Nelson PA, Khodadoust M, Prodhomme T, Spencer C, Patarroyo JC, Varrin-Doyer M, Ho JD, Stroud RM, Zamvil SS. Immunodominant T cell determinants of aquaporin-4, the autoantigen associated with neuromyelitis optica. Plos One. 5: e15050. PMID 21151500 DOI: 10.1371/Journal.Pone.0015050  0.581
2010 Chae PS, Gotfryd K, Pacyna J, Miercke LJ, Rasmussen SG, Robbins RA, Rana RR, Loland CJ, Kobilka B, Stroud R, Byrne B, Gether U, Gellman SH. Tandem facial amphiphiles for membrane protein stabilization. Journal of the American Chemical Society. 132: 16750-2. PMID 21049926 DOI: 10.1021/Ja1072959  0.587
2010 Hays FA, Roe-Zurz Z, Stroud RM. Overexpression and purification of integral membrane proteins in yeast. Methods in Enzymology. 470: 695-707. PMID 20946832 DOI: 10.1016/S0076-6879(10)70029-X  0.707
2010 Egea PF, Stroud RM. Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proceedings of the National Academy of Sciences of the United States of America. 107: 17182-7. PMID 20855604 DOI: 10.1073/Pnas.1012556107  0.776
2010 Savage DF, O'Connell JD, Miercke LJ, Finer-Moore J, Stroud RM. Structural context shapes the aquaporin selectivity filter. Proceedings of the National Academy of Sciences of the United States of America. 107: 17164-9. PMID 20855585 DOI: 10.1073/Pnas.1009864107  0.676
2010 Lee JK, Stroud RM. Unlocking the eukaryotic membrane protein structural proteome. Current Opinion in Structural Biology. 20: 464-70. PMID 20739007 DOI: 10.1016/J.Sbi.2010.05.004  0.672
2010 De Angelis F, Lee JK, O'Connell JD, Miercke LJ, Verschueren KH, Srinivasan V, Bauvois C, Govaerts C, Robbins RA, Ruysschaert JM, Stroud RM, Vandenbussche G. Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proceedings of the National Academy of Sciences of the United States of America. 107: 11038-43. PMID 20534468 DOI: 10.1073/Pnas.1003908107  0.669
2010 Gruswitz F, Chaudhary S, Ho JD, Schlessinger A, Pezeshki B, Ho CM, Sali A, Westhoff CM, Stroud RM. Function of human Rh based on structure of RhCG at 2.1 A. Proceedings of the National Academy of Sciences of the United States of America. 107: 9638-43. PMID 20457942 DOI: 10.1073/Pnas.1003587107  0.658
2010 Schlessinger A, Matsson P, Shima JE, Pieper U, Yee SW, Kelly L, Apeltsin L, Stroud RM, Ferrin TE, Giacomini KM, Sali A. Comparison of human solute carriers. Protein Science : a Publication of the Protein Society. 19: 412-28. PMID 20052679 DOI: 10.1002/Pro.320  0.4
2010 Pozzi C, Benvenuti M, Ferrari S, Luciani R, Catalano A, Stroud RM, Costi MP, Mangani S. Crystal structure ofEnterococcus faecalisthymidylate synthase Acta Crystallographica Section a Foundations of Crystallography. 66: s148-s148. DOI: 10.1107/S0108767310096704  0.441
2010 Miercke LJ, Robbins RA, Ho M, Sandstrom A, Bond RK, Stroud RM. Monitoring and Optimizing Detergent Concentration For Membrane Protein Crystallization While Following Protein Homogeneity Biophysical Journal. 98: 50a. DOI: 10.1016/J.Bpj.2009.12.288  0.42
2010 De Angelis F, Lee JK, O'Connell JD, Miercke LJ, Verschueren KH, Srinivasan V, Robbins RA, Govaerts C, Ruysschaert J, Stroud RM, Vandenbussche G. Crystal Structure and Metal-Binding Specificity of ZneB, the Periplasmic Adaptor Protein of A Heavy Metal Resistance System from Cupriavidus Metallidurans CH34 Biophysical Journal. 98: 248a. DOI: 10.1016/J.Bpj.2009.12.1347  0.667
2010 Stroud R. The Role of Detergents and Lipids in Membrane Protein Crystallography Biophysical Journal. 98: 209a. DOI: 10.1016/J.Bpj.2009.12.1122  0.424
2009 Kelly L, Pieper U, Eswar N, Hays FA, Li M, Roe-Zurz Z, Kroetz DL, Giacomini KM, Stroud RM, Sali A. A survey of integral alpha-helical membrane proteins. Journal of Structural and Functional Genomics. 10: 269-80. PMID 19760129 DOI: 10.1007/S10969-009-9069-8  0.723
2009 Alian A, Griner SL, Chiang V, Tsiang M, Jones G, Birkus G, Geleziunas R, Leavitt AD, Stroud RM. Catalytically-active complex of HIV-1 integrase with a viral DNA substrate binds anti-integrase drugs. Proceedings of the National Academy of Sciences of the United States of America. 106: 8192-7. PMID 19416821 DOI: 10.1073/Pnas.0811919106  0.416
2009 Ho JD, Yeh R, Sandstrom A, Chorny I, Harries WE, Robbins RA, Miercke LJ, Stroud RM. Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance. Proceedings of the National Academy of Sciences of the United States of America. 106: 7437-42. PMID 19383790 DOI: 10.1073/Pnas.0902725106  0.793
2009 Newby ZE, O'Connell JD, Gruswitz F, Hays FA, Harries WE, Harwood IM, Ho JD, Lee JK, Savage DF, Miercke LJ, Stroud RM. A general protocol for the crystallization of membrane proteins for X-ray structural investigation. Nature Protocols. 4: 619-37. PMID 19360018 DOI: 10.1038/Nprot.2009.27  0.794
2009 Stroud RM, Choe S, Holton J, Kaback HR, Kwiatkowski W, Minor DL, Riek R, Sali A, Stahlberg H, Harries W. 2007 annual progress report synopsis of the Center for Structures of Membrane Proteins. Journal of Structural and Functional Genomics. 10: 193-208. PMID 19148774 DOI: 10.1007/S10969-008-9058-3  0.817
2009 Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Zhang C, Shokat KM, Stroud RM, Walter P. The unfolded protein response signals through high-order assembly of Ire1. Nature. 457: 687-93. PMID 19079236 DOI: 10.1038/Nature07661  0.778
2009 Li M, Hays FA, Roe-Zurz Z, Vuong L, Kelly L, Ho CM, Robbins RM, Pieper U, O'Connell JD, Miercke LJ, Giacomini KM, Sali A, Stroud RM. Selecting optimum eukaryotic integral membrane proteins for structure determination by rapid expression and solubilization screening. Journal of Molecular Biology. 385: 820-30. PMID 19061901 DOI: 10.1016/J.Jmb.2008.11.021  0.733
2009 Hays FA, Roe-Zurz Z, Li M, Kelly L, Gruswitz F, Sali A, Stroud RM. Ratiocinative screen of eukaryotic integral membrane protein expression and solubilization for structure determination. Journal of Structural and Functional Genomics. 10: 9-16. PMID 19031011 DOI: 10.1007/S10969-008-9046-7  0.742
2008 Egea PF, Tsuruta H, de Leon GP, Napetschnig J, Walter P, Stroud RM. Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane. Plos One. 3: e3619. PMID 18978942 DOI: 10.1371/Journal.Pone.0003619  0.794
2008 Egea PF, Napetschnig J, Walter P, Stroud RM. Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus. Plos One. 3: e3528. PMID 18953414 DOI: 10.1371/Journal.Pone.0003528  0.798
2008 Lee JK, Belogrudov GI, Stroud RM. Crystal structure of bovine mitochondrial factor B at 0.96-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 105: 13379-84. PMID 18768789 DOI: 10.1073/Pnas.0805689105  0.666
2008 Newby ZE, O'Connell J, Robles-Colmenares Y, Khademi S, Miercke LJ, Stroud RM. Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum. Nature Structural & Molecular Biology. 15: 619-25. PMID 18500352 DOI: 10.1038/Nsmb.1431  0.8
2008 Alian A, Lee TT, Griner SL, Stroud RM, Finer-Moore J. Structure of a TrmA-RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases. Proceedings of the National Academy of Sciences of the United States of America. 105: 6876-81. PMID 18451029 DOI: 10.1073/Pnas.0802247105  0.456
2008 Du Z, Lee JK, Tjhen R, Stroud RM, James TL. Structural and biochemical insights into the dicing mechanism of mouse Dicer: a conserved lysine is critical for dsRNA cleavage. Proceedings of the National Academy of Sciences of the United States of America. 105: 2391-6. PMID 18268334 DOI: 10.1073/Pnas.0711506105  0.673
2007 Menuz K, Stroud RM, Nicoll RA, Hays FA. TARP auxiliary subunits switch AMPA receptor antagonists into partial agonists. Science (New York, N.Y.). 318: 815-7. PMID 17975069 DOI: 10.1126/Science.1146317  0.701
2007 Reyes CL, Rutenber E, Walter P, Stroud RM. X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates. Plos One. 2: e607. PMID 17622352 DOI: 10.1371/Journal.Pone.0000607  0.816
2007 Du Z, Lee JK, Fenn S, Tjhen R, Stroud RM, James TL. X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2. Rna (New York, N.Y.). 13: 1043-51. PMID 17526645 DOI: 10.1261/Rna.410107  0.677
2007 Hur S, Stroud RM. How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Molecular Cell. 26: 189-203. PMID 17466622 DOI: 10.1016/J.Molcel.2007.02.027  0.624
2007 Savage DF, Anderson CL, Robles-Colmenares Y, Newby ZE, Stroud RM. Cell-free complements in vivo expression of the E. coli membrane proteome. Protein Science : a Publication of the Protein Society. 16: 966-76. PMID 17456747 DOI: 10.1110/Ps.062696307  0.79
2007 Fenn S, Du Z, Lee JK, Tjhen R, Stroud RM, James TL. Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 A resolution. Nucleic Acids Research. 35: 2651-60. PMID 17426136 DOI: 10.1093/Nar/Gkm139  0.674
2007 Savage DF, Stroud RM. Structural basis of aquaporin inhibition by mercury. Journal of Molecular Biology. 368: 607-17. PMID 17376483 DOI: 10.1016/J.Jmb.2007.02.070  0.7
2007 Pan H, Ho JD, Stroud RM, Finer-Moore J. The crystal structure of E. coli rRNA pseudouridine synthase RluE. Journal of Molecular Biology. 367: 1459-70. PMID 17320904 DOI: 10.1016/J.Jmb.2007.01.084  0.661
2007 Gruswitz F, O'Connell J, Stroud RM. Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 A. Proceedings of the National Academy of Sciences of the United States of America. 104: 42-7. PMID 17190799 DOI: 10.1073/Pnas.0609796104  0.448
2007 Harries WEC, Khademi S, Stroud RM. The role of tryptophan cation-pi interactions on ammonia transport through the AmtB ammonia channel International Congress Series. 1304: 15-21. DOI: 10.1016/j.ics.2007.07.054  0.638
2006 Khademi S, Stroud RM. The Amt/MEP/Rh family: structure of AmtB and the mechanism of ammonia gas conduction. Physiology (Bethesda, Md.). 21: 419-29. PMID 17119155 DOI: 10.1152/Physiol.00051.2005  0.717
2006 Hur S, Stroud RM, Finer-Moore J. Substrate recognition by RNA 5-methyluridine methyltransferases and pseudouridine synthases: a structural perspective. The Journal of Biological Chemistry. 281: 38969-73. PMID 17085441 DOI: 10.1074/Jbc.R600034200  0.587
2006 He X, Alian A, Stroud R, Ortiz de Montellano PR. Pyrrolidine carboxamides as a novel class of inhibitors of enoyl acyl carrier protein reductase from Mycobacterium tuberculosis. Journal of Medicinal Chemistry. 49: 6308-23. PMID 17034137 DOI: 10.1021/Jm060715Y  0.419
2006 Newby Z, Lee TT, Morse RJ, Liu Y, Liu L, Venkatraman P, Santi DV, Finer-Moore JS, Stroud RM. The role of protein dynamics in thymidylate synthase catalysis: variants of conserved 2'-deoxyuridine 5'-monophosphate (dUMP)-binding Tyr-261. Biochemistry. 45: 7415-28. PMID 16768437 DOI: 10.1021/Bi060152S  0.813
2006 Keatinge-Clay AT, Stroud RM. The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases. Structure (London, England : 1993). 14: 737-48. PMID 16564177 DOI: 10.1016/J.Str.2006.01.009  0.719
2006 Stroud RM. Present at the flood: How structural biology came about, by Richard E. Dickerson Protein Science. 16: 135-136. DOI: 10.1110/Ps.062627807  0.463
2005 Credle JJ, Finer-Moore JS, Papa FR, Stroud RM, Walter P. On the mechanism of sensing unfolded protein in the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America. 102: 18773-84. PMID 16365312 DOI: 10.1073/Pnas.0509487102  0.609
2005 Lee JK, Kozono D, Remis J, Kitagawa Y, Agre P, Stroud RM. Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A. Proceedings of the National Academy of Sciences of the United States of America. 102: 18932-7. PMID 16361443 DOI: 10.1073/Pnas.0509469102  0.673
2005 Finer-Moore JS, Anderson AC, O'Neil RH, Costi MP, Ferrari S, Krucinski J, Stroud RM. The structure of Cryptococcus neoformans thymidylate synthase suggests strategies for using target dynamics for species-specific inhibition. Acta Crystallographica. Section D, Biological Crystallography. 61: 1320-34. PMID 16204883 DOI: 10.1107/S0907444905022638  0.648
2005 Du Z, Lee JK, Tjhen R, Li S, Pan H, Stroud RM, James TL. Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 A. The Journal of Biological Chemistry. 280: 38823-30. PMID 16186123 DOI: 10.1074/Jbc.M508183200  0.664
2005 Egea PF, Stroud RM, Walter P. Targeting proteins to membranes: structure of the signal recognition particle. Current Opinion in Structural Biology. 15: 213-20. PMID 15837181 DOI: 10.1016/J.Sbi.2005.03.007  0.795
2005 Lee TT, Agarwalla S, Stroud RM. A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function. Cell. 120: 599-611. PMID 15766524 DOI: 10.1016/J.Cell.2004.12.037  0.302
2004 Chu F, Shan SO, Moustakas DT, Alber F, Egea PF, Stroud RM, Walter P, Burlingame AL. Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 101: 16454-9. PMID 15546976 DOI: 10.1073/Pnas.0407456101  0.777
2004 Shan SO, Stroud RM, Walter P. Mechanism of association and reciprocal activation of two GTPases. Plos Biology. 2: e320. PMID 15383838 DOI: 10.1371/Journal.Pbio.0020320  0.587
2004 Harries WE, Akhavan D, Miercke LJ, Khademi S, Stroud RM. The channel architecture of aquaporin 0 at a 2.2-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 101: 14045-50. PMID 15377788 DOI: 10.1073/Pnas.0405274101  0.819
2004 Khademi S, O'Connell J, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM. Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A. Science (New York, N.Y.). 305: 1587-94. PMID 15361618 DOI: 10.1126/Science.1101952  0.729
2004 Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM. An antibiotic factory caught in action. Nature Structural & Molecular Biology. 11: 888-93. PMID 15286722 DOI: 10.1038/Nsmb808  0.678
2004 Stroud RM, Wells JA. Mechanistic diversity of cytokine receptor signaling across cell membranes. Science's Stke : Signal Transduction Knowledge Environment. 2004: re7. PMID 15126678 DOI: 10.1126/Stke.2312004Re7  0.409
2004 Lee TT, Agarwalla S, Stroud RM. Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase. Structure (London, England : 1993). 12: 397-407. PMID 15016356 DOI: 10.1016/J.Str.2004.02.009  0.466
2004 Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM. Substrate twinning activates the signal recognition particle and its receptor. Nature. 427: 215-21. PMID 14724630 DOI: 10.1038/Nature02250  0.806
2004 Lee JK, Khademi S, Harries W, Savage D, Miercke L, Stroud RM. Water and glycerol permeation through the glycerol channel GlpF and the aquaporin family. Journal of Synchrotron Radiation. 11: 86-8. PMID 14646142 DOI: 10.1107/S0909049503023872  0.81
2003 O'Neil RH, Lilien RH, Donald BR, Stroud RM, Anderson AC. The crystal structure of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveals a novel architecture for the bifunctional enzyme. The Journal of Eukaryotic Microbiology. 50: 555-6. PMID 14736160 DOI: 10.1111/J.1550-7408.2003.Tb00627.X  0.654
2003 Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD, Stroud RM. Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z. Plos Biology. 1: E72. PMID 14691544 DOI: 10.1371/Journal.Pbio.0000072  0.827
2003 Foster PG, Nunes CR, Greene P, Moustakas D, Stroud RM. The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate. Structure (London, England : 1993). 11: 1609-20. PMID 14656444 DOI: 10.1016/J.Str.2003.10.014  0.806
2003 Stroud RM, Savage D, Miercke LJ, Lee JK, Khademi S, Harries W. Selectivity and conductance among the glycerol and water conducting aquaporin family of channels. Febs Letters. 555: 79-84. PMID 14630323 DOI: 10.1016/S0014-5793(03)01195-5  0.789
2003 Watanabe K, Khosla C, Stroud RM, Tsai SC. Crystal structure of an Acyl-ACP dehydrogenase from the FK520 polyketide biosynthetic pathway: insights into extender unit biosynthesis. Journal of Molecular Biology. 334: 435-44. PMID 14623185 DOI: 10.1016/J.Jmb.2003.10.021  0.491
2003 Pan H, Agarwalla S, Moustakas DT, Finer-Moore J, Stroud RM. Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proceedings of the National Academy of Sciences of the United States of America. 100: 12648-53. PMID 14566049 DOI: 10.1073/Pnas.2135585100  0.435
2003 O'Neil RH, Lilien RH, Donald BR, Stroud RM, Anderson AC. Phylogenetic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase-thymidylate synthase. The Journal of Biological Chemistry. 278: 52980-7. PMID 14555647 DOI: 10.1074/Jbc.M310328200  0.671
2003 Gonzalez-Pacanowska D, Ruiz-Perez LM, Carreras-Gómez MA, Costi MP, Stroud RM, Finer-Moore J, Santi DV. The structural roles of conserved Pro196, Pro197 and His199 in the mechanism of thymidylate synthase. Protein Engineering. 16: 607-14. PMID 12968078 DOI: 10.1093/Protein/Gzg076  0.407
2003 Stroud RM, Miercke LJ, O'Connell J, Khademi S, Lee JK, Remis J, Harries W, Robles Y, Akhavan D. Glycerol facilitator GlpF and the associated aquaporin family of channels. Current Opinion in Structural Biology. 13: 424-31. PMID 12948772 DOI: 10.1016/S0959-440X(03)00114-3  0.802
2003 Jez JM, Chen JC, Rastelli G, Stroud RM, Santi DV. Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chemistry & Biology. 10: 361-8. PMID 12725864 DOI: 10.1016/S1074-5521(03)00075-9  0.474
2003 Birdsall DL, Finer-Moore J, Stroud RM. The only active mutant of thymidylate synthase D169, a residue far from the site of methyl transfer, demonstrates the exquisite nature of enzyme specificity. Protein Engineering. 16: 229-40. PMID 12702803 DOI: 10.1093/Proeng/Gzg020  0.424
2003 Stroud RM, Nollert P, Miercke L. The glycerol facilitator GlpF its aquaporin family of channels, and their selectivity. Advances in Protein Chemistry. 63: 291-316. PMID 12629974 DOI: 10.1016/S0065-3233(03)63011-1  0.704
2003 Reiling KK, Krucinski J, Miercke LJ, Raymond WW, Caughey GH, Stroud RM. Structure of human pro-chymase: a model for the activating transition of granule-associated proteases. Biochemistry. 42: 2616-24. PMID 12614156 DOI: 10.1021/Bi020594D  0.471
2003 Keatinge-Clay AT, Shelat AA, Savage DF, Tsai SC, Miercke LJ, O'Connell JD, Khosla C, Stroud RM. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure (London, England : 1993). 11: 147-54. PMID 12575934 DOI: 10.1016/S0969-2126(03)00004-2  0.777
2003 Finer-Moore JS, Santi DV, Stroud RM. Lessons and conclusions from dissecting the mechanism of a bisubstrate enzyme: thymidylate synthase mutagenesis, function, and structure. Biochemistry. 42: 248-56. PMID 12525151 DOI: 10.1021/Bi020599A  0.436
2002 Stroud RM, Nollert P, Miercke LJW, Harries WEC, O'Connell J. Encoding Selectivity of a Transmembrane Channel. Thescientificworldjournal. 2: 111. PMID 29973827 DOI: 10.1100/Tsw.2002.52  0.743
2002 Pan H, Tsai Sc, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM. Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway. Structure (London, England : 1993). 10: 1559-68. PMID 12429097 DOI: 10.1016/S0969-2126(02)00889-4  0.716
2002 Tsai SC, Lu H, Cane DE, Khosla C, Stroud RM. Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases. Biochemistry. 41: 12598-606. PMID 12379102 DOI: 10.1021/Bi0260177  0.501
2002 Ramirez UD, Minasov G, Focia PJ, Stroud RM, Walter P, Kuhn P, Freymann DM. Structural basis for mobility in the 1.1 A crystal structure of the NG domain of Thermus aquaticus Ffh. Journal of Molecular Biology. 320: 783-99. PMID 12095255 DOI: 10.1016/S0022-2836(02)00476-X  0.803
2002 Costi MP, Tondi D, Rinaldi M, Barlocco D, Pecorari P, Soragni F, Venturelli A, Stroud RM. Structure-based studies on species-specific inhibition of thymidylate synthase. Biochimica Et Biophysica Acta. 1587: 206-14. PMID 12084462 DOI: 10.1016/S0925-4439(02)00083-2  0.425
2002 Fritz TA, Liu L, Finer-Moore JS, Stroud RM. Tryptophan 80 and leucine 143 are critical for the hydride transfer step of thymidylate synthase by controlling active site access. Biochemistry. 41: 7021-9. PMID 12033935 DOI: 10.1021/Bi012108C  0.432
2002 Fu D, Libson A, Stroud R. The structure of GlpF, a glycerol conducting channel. Novartis Foundation Symposium. 245: 51-61; discussion 61. PMID 12027015  0.445
2002 Tajkhorshid E, Nollert P, Jensen MØ, Miercke LJ, O'Connell J, Stroud RM, Schulten K. Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science (New York, N.Y.). 296: 525-30. PMID 11964478 DOI: 10.1126/Science.1067778  0.722
2002 Reiling KK, Endres NF, Dauber DS, Craik CS, Stroud RM. Anisotropic dynamics of the JE-2147-HIV protease complex: drug resistance and thermodynamic binding mode examined in a 1.09 A structure. Biochemistry. 41: 4582-94. PMID 11926820 DOI: 10.1021/Bi011781Z  0.406
2002 Agarwalla S, Kealey JT, Santi DV, Stroud RM. Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli. The Journal of Biological Chemistry. 277: 8835-40. PMID 11779873 DOI: 10.1074/Jbc.M111825200  0.408
2002 Fu D, Libson A, Stroud R. The structure of GlpF, a glycerol conducting channel. Novartis Foundation Symposium. 245: 51-65. DOI: 10.1002/0470868759.Ch5  0.524
2001 Tsai SC, Miercke LJ, Krucinski J, Gokhale R, Chen JC, Foster PG, Cane DE, Khosla C, Stroud RM. Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel. Proceedings of the National Academy of Sciences of the United States of America. 98: 14808-13. PMID 11752428 DOI: 10.1073/Pnas.011399198  0.528
2001 Sayre PH, Finer-Moore JS, Fritz TA, Biermann D, Gates SB, MacKellar WC, Patel VF, Stroud RM. Multi-targeted antifolates aimed at avoiding drug resistance form covalent closed inhibitory complexes with human and Escherichia coli thymidylate synthases. Journal of Molecular Biology. 313: 813-29. PMID 11697906 DOI: 10.1006/Jmbi.2001.5074  0.476
2001 Fritz TA, Tondi D, Finer-Moore JS, Costi MP, Stroud RM. Predicting and harnessing protein flexibility in the design of species-specific inhibitors of thymidylate synthase. Chemistry & Biology. 8: 981-95. PMID 11590022 DOI: 10.1016/S1074-5521(01)00067-9  0.507
2001 Nollert P, Harries WE, Fu D, Miercke LJ, Stroud RM. Atomic structure of a glycerol channel and implications for substrate permeation in aqua(glycero)porins. Febs Letters. 504: 112-7. PMID 11532442 DOI: 10.1016/S0014-5793(01)02710-7  0.81
2001 Keenan RJ, Freymann DM, Stroud RM, Walter P. The signal recognition particle. Annual Review of Biochemistry. 70: 755-75. PMID 11395422 DOI: 10.1146/Annurev.Biochem.70.1.755  0.794
2001 Morse RJ, Yamamoto T, Stroud RM. Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure (London, England : 1993). 9: 409-17. PMID 11377201 DOI: 10.1016/S0969-2126(01)00601-3  0.522
2001 Anderson AC, O'Neil RH, Surti TS, Stroud RM. Approaches to solving the rigid receptor problem by identifying a minimal set of flexible residues during ligand docking. Chemistry & Biology. 8: 445-57. PMID 11358692 DOI: 10.1016/S1074-5521(01)00023-0  0.654
2000 Reiling KK, Pray TR, Craik CS, Stroud RM. Functional consequences of the Kaposi's sarcoma-associated herpesvirus protease structure: regulation of activity and dimerization by conserved structural elements. Biochemistry. 39: 12796-803. PMID 11041844 DOI: 10.1021/Bi001019H  0.473
2000 Fu D, Libson A, Miercke LJ, Weitzman C, Nollert P, Krucinski J, Stroud RM. Structure of a glycerol-conducting channel and the basis for its selectivity. Science (New York, N.Y.). 290: 481-6. PMID 11039922 DOI: 10.1126/Science.290.5491.481  0.758
2000 Erlanson DA, Braisted AC, Raphael DR, Randal M, Stroud RM, Gordon EM, Wells JA. Site-directed ligand discovery. Proceedings of the National Academy of Sciences of the United States of America. 97: 9367-72. PMID 10944209 DOI: 10.1073/Pnas.97.17.9367  0.439
2000 Wiener MC, Verkman AS, Stroud RM, van Hoek AN. Mesoscopic surfactant organization and membrane protein crystallization. Protein Science : a Publication of the Protein Society. 9: 1407-9. PMID 10933509 DOI: 10.1110/Ps.9.7.1407  0.701
2000 Chen JC, Krucinski J, Miercke LJ, Finer-Moore JS, Tang AH, Leavitt AD, Stroud RM. Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding. Proceedings of the National Academy of Sciences of the United States of America. 97: 8233-8. PMID 10890912 DOI: 10.1073/Pnas.150220297  0.462
2000 Anderson AC, Perry KM, Freymann DM, Stroud RM. The crystal structure of thymidylate synthase from Pneumocystis carinii reveals a fungal insert important for drug design. Journal of Molecular Biology. 297: 645-57. PMID 10731418 DOI: 10.1006/Jmbi.2000.3544  0.784
2000 Variath P, Liu Y, Lee TT, Stroud RM, Santi DV. Effects of subunit occupancy on partitioning of an intermediate in thymidylate synthase mutants. Biochemistry. 39: 2429-35. PMID 10704192 DOI: 10.1021/Bi991802D  0.405
2000 Morse RJ, Kawase S, Santi DV, Finer-Moore J, Stroud RM. Energetic contributions of four arginines to phosphate-binding in thymidylate synthase are more than additive and depend on optimization of "effective charge balance". Biochemistry. 39: 1011-20. PMID 10653645 DOI: 10.1021/Bi9918590  0.454
2000 Foster PG, Huang L, Santi DV, Stroud RM. The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nature Structural Biology. 7: 23-7. PMID 10625422 DOI: 10.1038/71219  0.479
2000 Cherbavaz DB, Lee ME, Stroud RM, Koshland DE. Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase. Journal of Molecular Biology. 295: 377-85. PMID 10623532 DOI: 10.1006/Jmbi.1999.3195  0.472
1999 Stroud RM, Walter P. Signal sequence recognition and protein targeting. Current Opinion in Structural Biology. 9: 754-9. PMID 10607673 DOI: 10.1016/S0959-440X(99)00040-8  0.561
1999 Turner GJ, Miercke LJ, Mitra AK, Stroud RM, Betlach MC, Winter-Vann A. Expression, purification, and structural characterization of the bacteriorhodopsin-aspartyl transcarbamylase fusion protein. Protein Expression and Purification. 17: 324-38. PMID 10545282 DOI: 10.1006/Prep.1999.1111  0.499
1999 Anderson AC, O'Neil RH, DeLano WL, Stroud RM. The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits. Biochemistry. 38: 13829-36. PMID 10529228 DOI: 10.1021/Bi991610I  0.661
1999 Freymann DM, Keenan RJ, Stroud RM, Walter P. Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nature Structural Biology. 6: 793-801. PMID 10426959 DOI: 10.1038/11572  0.806
1999 Zhan H, Liu B, Reid SW, Aoki KH, Li C, Syed RS, Karkaria C, Koe G, Sitney K, Hayenga K, Mistry F, Savel L, Dreyer M, Katz BA, Schreurs J, ... ... Stroud RM, et al. Engineering a soluble extracellular erythropoietin receptor (EPObp) in Pichia pastoris to eliminate microheterogeneity, and its complex with erythropoietin. Protein Engineering. 12: 505-13. PMID 10388848 DOI: 10.1093/Protein/12.6.505  0.435
1999 Costi PM, Rinaldi M, Tondi D, Pecorari P, Barlocco D, Ghelli S, Stroud RM, Santi DV, Stout TJ, Musiu C, Marangiu EM, Pani A, Congiu D, Loi GA, La Colla P. Phthalein derivatives as a new tool for selectivity in thymidylate synthase inhibition. Journal of Medicinal Chemistry. 42: 2112-24. PMID 10377217 DOI: 10.1021/jm9900016  0.641
1999 Stout TJ, Tondi D, Rinaldi M, Barlocco D, Pecorari P, Santi DV, Kuntz ID, Stroud RM, Shoichet BK, Costi MP. Structure-based design of inhibitors specific for bacterial thymidylate synthase. Biochemistry. 38: 1607-17. PMID 9931028 DOI: 10.1021/Bi9815896  0.707
1998 Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM. Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer. Journal of Molecular Biology. 284: 699-712. PMID 9826509 DOI: 10.1006/Jmbi.1998.2205  0.77
1998 Stout TJ, Schellenberger U, Santi DV, Stroud RM. Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis. Biochemistry. 37: 14736-47. PMID 9778348 DOI: 10.1021/Bi981270L  0.736
1998 Syed RS, Reid SW, Li C, Cheetham JC, Aoki KH, Liu B, Zhan H, Osslund TD, Chirino AJ, Zhang J, Finer-Moore J, Elliott S, Sitney K, Katz BA, Matthews DJ, ... ... Stroud RM, et al. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature. 395: 511-6. PMID 9774108 DOI: 10.1038/26773  0.412
1998 Sage CR, Michelitsch MD, Stout TJ, Biermann D, Nissen R, Finer-Moore J, Stroud RM. D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidine. Biochemistry. 37: 13893-901. PMID 9753479 DOI: 10.2210/Pdb1Bjg/Pdb  0.713
1998 Stroud RM, Reiling K, Wiener M, Freymann D. Ion-channel-forming colicins. Current Opinion in Structural Biology. 8: 525-33. PMID 9729746 DOI: 10.1016/S0959-440X(98)80132-2  0.808
1998 Schafmeister CE, Stroud RM. Helical protein design. Current Opinion in Biotechnology. 9: 350-3. PMID 9720261 DOI: 10.1016/S0958-1669(98)80006-2  0.719
1998 Keenan RJ, Freymann DM, Walter P, Stroud RM. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell. 94: 181-91. PMID 9695947 DOI: 10.1016/S0092-8674(00)81418-X  0.799
1998 Stout TJ, Sage CR, Stroud RM. The additivity of substrate fragments in enzyme-ligand binding. Structure (London, England : 1993). 6: 839-48. PMID 9687366 DOI: 10.1016/S0969-2126(98)00086-0  0.693
1998 Birdsall DL, Huang W, Santi DV, Stroud RM, Finer-Moore J. The separate effects of E60Q in Lactobacillus casei thymidylate synthase delineate between mechanisms for formation of intermediates in catalysis. Protein Engineering. 11: 171-83. PMID 9613841 DOI: 10.1093/Protein/11.3.171  0.462
1998 Chen JC, Miercke LJ, Krucinski J, Starr JR, Saenz G, Wang X, Spilburg CA, Lange LG, Ellsworth JL, Stroud RM. Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel structural features involved in lipase activation. Biochemistry. 37: 5107-17. PMID 9548741 DOI: 10.1021/Bi972989G  0.47
1998 Finer-Moore JS, Liu L, Birdsall DL, Brem R, Apfeld J, Santi DV, Stroud RM. Contributions of orientation and hydrogen bonding to catalysis in Asn229 mutants of thymidylate synthase Journal of Molecular Biology. 276: 113-129. PMID 9514716 DOI: 10.1006/Jmbi.1997.1495  0.431
1998 Rose RB, Craik CS, Stroud RM. Domain flexibility in retroviral proteases: structural implications for drug resistant mutations. Biochemistry. 37: 2607-21. PMID 9485411 DOI: 10.1021/Bi9716074  0.715
1998 Katz BA, Clark JM, Finer-Moore JS, Jenkins TE, Johnson CR, Ross MJ, Luong C, Moore WR, Stroud RM. Design of potent selective zinc-mediated serine protease inhibitors. Nature. 391: 608-12. PMID 9468142 DOI: 10.1038/35422  0.427
1998 Agarwalla S, LaPorte S, Liu L, Finer-Moore J, Stroud RM, Santi DV. A novel dCMP methylase by engineering thymidylate synthase. Biochemistry. 36: 15909-17. PMID 9398324 DOI: 10.1021/Bi971873H  0.448
1997 Schafmeister CE, LaPorte SL, Miercke LJ, Stroud RM. A designed four helix bundle protein with native-like structure. Nature Structural Biology. 4: 1039-46. PMID 9406555 DOI: 10.1038/Nsb1297-1039  0.75
1997 Rutenber EE, De Voss JJ, Hoffman L, Stroud RM, Lee KH, Alvarez J, McPhee F, Craik C, Ortiz De Montellano PR. The discovery, characterization and crystallographically determined binding mode of an FMOC-containing inhibitor of HIV-1 protease Bioorganic and Medicinal Chemistry. 5: 1311-1320. PMID 9377091 DOI: 10.1016/S0968-0896(97)00078-3  0.433
1997 Finer-Moore J, Tsutakawa SE, Cherbavaz DB, LaPorte DC, Koshland DE, Stroud RM. Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting Biochemistry. 36: 13890-13896. PMID 9374867 DOI: 10.1021/Bi9711691  0.469
1997 Wiener M, Freymann D, Ghosh P, Stroud RM. Crystal structure of colicin Ia. Nature. 385: 461-4. PMID 9009197 DOI: 10.1038/385461A0  0.817
1997 Freymann DM, Keenan RJ, Stroud RM, Walter P. Structure of the conserved GTPase domain of the signal recognition particle. Nature. 385: 361-4. PMID 9002524 DOI: 10.1038/385361A0  0.808
1997 Sage CR, Rutenber EE, Stout TJ, Stroud RM. An essential role for water in an enzyme reaction mechanism: the crystal structure of the thymidylate synthase mutant E58Q. Biochemistry. 35: 16270-81. PMID 8973201 DOI: 10.1021/Bi961269R  0.725
1997 Rutenber E, Fauman EB, Keenan RJ, Fong S, Furth PS, Montellano PROd, Meng E, Kuntz ID, DeCamp DL, Salto R, Rose JR, Craik CS, Stroud RM. Structure of a non-peptide inhibitor complexed with HIV-1 protease. Developing a cycle of structure-based drug design. Journal of Biological Chemistry. 268: 15343-15346. DOI: 10.2210/Pdb2Aid/Pdb  0.589
1996 Finer-Moore JS, Fauman EB, Morse RJ, Santi DV, Stroud RM. Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase. Protein Engineering. 9: 69-75. PMID 9053905 DOI: 10.1093/Protein/9.1.69  0.437
1996 Rutenber EE, McPhee F, Kaplan AP, Gallion SL, Hogan JC, Craik CS, Stroud RM. A new class of HIV-1 protease inhibitor: The crystallographic structure, inhibition and chemical synthesis of an aminimide peptide isostere Bioorganic and Medicinal Chemistry. 4: 1545-1558. PMID 8894111 DOI: 10.1016/0968-0896(96)00147-2  0.419
1996 Rose RB, Craik CS, Douglas NL, Stroud RM. Three-dimensional structures of HIV-1 and SIV protease product complexes. Biochemistry. 35: 12933-44. PMID 8841139 DOI: 10.1021/Bi9612733  0.705
1996 Stout TJ, Stroud RM. The complex of the anti-cancer therapeutic, BW1843U89, with thymidylate synthase at 2.0 A resolution: implications for a new mode of inhibition. Structure (London, England : 1993). 4: 67-77. PMID 8805515 DOI: 10.1016/S0969-2126(96)00010-X  0.67
1996 Stroud RM. Balancing ATP in the cell. Nature Structural Biology. 3: 567-9. PMID 8673595 DOI: 10.1038/Nsb0796-567  0.406
1996 Costi PM, Liu L, Finer-Moore JS, Stroud RM, Santi DV. Asparagine 229 mutants of thymidylate synthase catalyze the methylation of 3-methyl-2'-deoxyuridine 5'-monophosphate. Biochemistry. 35: 3944-9. PMID 8672425 DOI: 10.1021/Bi952642I  0.412
1996 Finer-Moore JS, Liu L, Schafmeister CE, Birdsall DL, Mau T, Santi DV, Stroud RM. Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase. Biochemistry. 35: 5125-36. PMID 8611496 DOI: 10.1021/Bi952751X  0.731
1996 Birdsall DL, Finer-Moore J, Stroud RM. Entropy in bi-substrate enzymes: proposed role of an alternate site in chaperoning substrate into, and products out of, thymidylate synthase. Journal of Molecular Biology. 255: 522-35. PMID 8568895 DOI: 10.1006/Jmbi.1996.0043  0.433
1996 Stroud RM, Fauman EB. Significance of structural changes in proteins: expected errors in refined protein structures. Protein Science : a Publication of the Protein Society. 4: 2392-404. PMID 8563637 DOI: 10.1002/Pro.5560041118  0.478
1996 Morse RJ, Ramalingam V, Stroud RM. Progress towards the structure of a membrane pore-forming toxin Acta Crystallographica Section a Foundations of Crystallography. 52: C145-C145. DOI: 10.1107/S0108767396093440  0.461
1996 Freymann D, Keenan R, Stroud R, Walter P. Progress torwards the crystal structure of Ffh, the bacterial homolog of SRP54 Acta Crystallographica Section a Foundations of Crystallography. 52: C167-C167. DOI: 10.1107/S0108767396092574  0.793
1996 Wiener M, Freymann D, Ghosh P, Stroud R. The crystal structure of colicin IA Acta Crystallographica Section a Foundations of Crystallography. 52: C173-C173. DOI: 10.1107/S0108767396092379  0.796
1996 Stout TJ, Costi MP, Barlocco D, Rinaldi M, Shoichet B, Perry KM, Kuntz ID, Stroud RM. Structure-based discovery of a new class of enzyme inhibitors Acta Crystallographica Section a Foundations of Crystallography. 52: C207-C207. DOI: 10.1107/S0108767396091064  0.693
1996 Schafmeister CE, LaPorte S, Stroud RM. Crystal structure of an artificial 4-helix bundle protein Acta Crystallographica Section a Foundations of Crystallography. 52: C212-C212. DOI: 10.1107/S0108767396090861  0.487
1996 Sage CR, Rutenber EE, Stout TJ, Stroud RM. Short-circuiting a water-mediated enzyme reaction Acta Crystallographica Section a Foundations of Crystallography. 52: C239-C239. DOI: 10.1107/S0108767396089830  0.663
1995 Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM. Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site. Biochemistry. 34: 16279-87. PMID 8845352 DOI: 10.1021/Bi00050A007  0.714
1995 Stroud RM. An electrostatic highway. Nature Structural Biology. 1: 131-4. PMID 7656026 DOI: 10.1038/Nsb0394-131  0.487
1995 Katz BA, Finer-Moore J, Mortezaei R, Rich DH, Stroud RM. Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface. Biochemistry. 34: 8264-80. PMID 7599119 DOI: 10.1021/Bi00026A008  0.402
1994 Fauman EB, Rutenber EE, Maley GF, Maley F, Stroud RM. Water-mediated substrate/product discrimination: the product complex of thymidylate synthase at 1.83 A. Biochemistry. 33: 1502-11. PMID 8312270 DOI: 10.1021/Bi00172A029  0.466
1994 Finer-Moore JS, Maley GF, Maley F, Montfort WR, Stroud RM. Crystal structure of thymidylate synthase from T4 phage: component of a deoxynucleoside triphosphate-synthesizing complex. Biochemistry. 33: 15459-68. PMID 7803410 DOI: 10.1021/Bi00255A028  0.699
1994 Ghosh P, Mel SF, Stroud RM. The domain structure of the ion channel-forming protein colicin Ia. Nature Structural Biology. 1: 597-604. PMID 7543362 DOI: 10.1038/Nsb0994-597  0.82
1993 Shoichet BK, Stroud RM, Santi DV, Kuntz ID, Perry KM. Structure-based discovery of inhibitors of thymidylate synthase. Science (New York, N.Y.). 259: 1445-50. PMID 8451640 DOI: 10.1126/Science.8451640  0.458
1993 Mel SF, Stroud RM. Colicin Ia inserts into negatively charged membranes at low pH with a tertiary but little secondary structural change. Biochemistry. 32: 2082-9. PMID 8448167 DOI: 10.1021/Bi00059A028  0.794
1993 Finer-Moore J, Fauman EB, Foster PG, Perry KM, Santi DV, Stroud RM. Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei. Journal of Molecular Biology. 232: 1101-16. PMID 8371269 DOI: 10.1006/Jmbi.1993.1463  0.491
1993 Perry KM, Carreras CW, Chang LC, Santi DV, Stroud RM. Structures of thymidylate synthase with a C-terminal deletion: Role of the C-terminus in alignment of 2′-deoxyuridine 5′-monophosphate and 5,10-methylenetetrahydrofolate Biochemistry. 32: 7116-7125. PMID 8343503 DOI: 10.1021/Bi00079A007  0.499
1993 Mitra AK, Miercke LJW, Turner GJ, Shand RF, Betlach MC, Stroud RM. Two-dimensional crystallization of Escherichia coli-expressed bacteriorhodopsin and its D96N variant: High resolution structural studies in projection Biophysical Journal. 65: 1295-1306. PMID 8241409 DOI: 10.1016/S0006-3495(93)81169-X  0.453
1993 Rose RB, Rosé JR, Salto R, Craik CS, Stroud RM. Structure of the protease from simian immunodeficiency virus: complex with an irreversible nonpeptide inhibitor. Biochemistry. 32: 12498-507. PMID 8241141 DOI: 10.1021/Bi00097A030  0.717
1993 Schafmeister CE, Miercke LJ, Stroud RM. Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins. Science (New York, N.Y.). 262: 734-8. PMID 8235592 DOI: 10.1126/Science.8235592  0.73
1993 Ghosh P, Mel SF, Stroud RM. A carboxy-terminal fragment of colicin Ia forms ion channels. The Journal of Membrane Biology. 134: 85-92. PMID 7692058 DOI: 10.1007/Bf00232745  0.791
1993 Mel SF, Falick AM, Burlingame AL, Stroud RM. Mapping a membrane-associated conformation of colicin Ia. Biochemistry. 32: 9473-9. PMID 7690252 DOI: 10.1021/Bi00087A027  0.807
1993 Kamb A, Finer-Moore JS, Stroud RM. Cofactor triggers the conformational change in thymidylate synthase: implications for an ordered binding mechanism. Biochemistry. 31: 12876-84. PMID 1281428 DOI: 10.1021/Bi00166A024  0.479
1993 Schiffer CA, Caldwell JW, Kollman PA, Stroud RM. Protein Structure Prediction with a Combined Solvation Free Energy-Molecular Mechanics Force Field Molecular Simulation. 10: 121-149. DOI: 10.1080/08927029308022162  0.683
1992 Finer-Moore JS, Kossiakoff AA, Hurley JH, Earnest T, Stroud RM. Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction. Proteins. 12: 203-22. PMID 1557349 DOI: 10.1002/Prot.340120302  0.776
1992 Kamb A, Finer-Moore J, Calvert AH, Stroud RM. Structural basis for recognition of polyglutamyl folates by thymidylate synthase. Biochemistry. 31: 9883-90. PMID 1390771 DOI: 10.1021/Bi00156A005  0.458
1992 Perry KM, Pookanjanatavip M, Zhao J, Santi DV, Stroud RM. Reversible dissociation and unfolding of the dimeric protein thymidylate synthase Protein Science. 1: 796-800. PMID 1304920 DOI: 10.1002/Pro.5560010611  0.42
1992 Schiffer CA, Caldwell JW, Stroud RM, Kollman PA. Inclusion of solvation free energy with molecular mechanics energy: alanyl dipeptide as a test case. Protein Science : a Publication of the Protein Society. 1: 396-400. PMID 1304346 DOI: 10.1002/Pro.5560010311  0.621
1991 Schiffer CA, Davisson VJ, Santi DV, Stroud RM. Crystallization of human thymidylate synthase. Journal of Molecular Biology. 219: 161-3. PMID 2038053 DOI: 10.1016/0022-2836(91)90558-N  0.657
1991 Shand RF, Miercke LJW, Mitra AK, Fong SK, Stroud RM, Betlach MC. Wild-type and mutant bacterioopsins D85N, D96N, and R82Q: High-level expression in Escherichia coli Biochemistry. 30: 3082-3088. PMID 2007142 DOI: 10.1021/Bi00226A015  0.431
1991 Hurley JH, Dean AM, Koshland DE, Stroud RM. Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes. Biochemistry. 30: 8671-8. PMID 1888729 DOI: 10.1021/Bi00099A026  0.647
1991 Miercke LJW, Betlach MC, Mitra AK, Shand RF, Fong SK, Stroud RM. Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: Purification to homogeneity, pH dependence of pumping, and electron diffraction Biochemistry. 30: 3088-3098. PMID 1848786 DOI: 10.1021/Bi00226A016  0.436
1991 Ghosh P, Stroud RM. Ion channels formed by a highly charged peptide. Biochemistry. 30: 3551-7. PMID 1707312 DOI: 10.1021/Bi00228A028  0.556
1991 Stroud RM. Mechanisms of biological control by phosphorylation Current Opinion in Structural Biology. 1: 826-835. DOI: 10.1016/0959-440X(91)90186-W  0.458
1990 Hurley JH, Dean AM, Thorsness PE, Koshland DE, Stroud RM. Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme. The Journal of Biological Chemistry. 265: 3599-602. PMID 2406256 DOI: 10.2210/Pdb4Icd/Pdb  0.617
1990 Mitra AK, Stroud RM. High sensitivity electron diffraction analysis. A study of divalent cation binding to purple membrane Biophysical Journal. 57: 301-311. PMID 2317552 DOI: 10.1016/S0006-3495(90)82532-7  0.439
1990 Mangel WF, Singer PT, Cyr DM, Umland TC, Toledo DL, Stroud RM, Pflugrath JW, Sweet RM. Structure of an acyl-enzyme intermediate during catalysis: (Guanidinobenzoyl)trypsint Biochemistry®. 29: 8351-8357. PMID 2252895 DOI: 10.1021/Bi00488A022  0.497
1990 Finer-Moore JS, Montfort WR, Stroud RM. Pairwise specificity and sequential binding in enzyme catalysis: thymidylate synthase. Biochemistry. 29: 6977-86. PMID 2223755 DOI: 10.1021/Bi00482A005  0.695
1990 Montfort WR, Perry KM, Fauman EB, Finer-Moore JS, Maley GF, Hardy L, Maley F, Stroud RM. Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate. Biochemistry. 29: 6964-77. PMID 2223754 DOI: 10.1021/Bi00482A004  0.72
1990 Schiffer CA, Caldwell JW, Kollman PA, Stroud RM. Prediction of homologous protein structures based on conformational searches and energetics. Proteins. 8: 30-43. PMID 2217162 DOI: 10.1002/Prot.340080107  0.702
1990 Hurley JH, Dean AM, Sohl JL, Koshland DE, Stroud RM. Regulation of an enzyme by phosphorylation at the active site. Science (New York, N.Y.). 249: 1012-6. PMID 2204109 DOI: 10.1126/Science.2204109  0.615
1990 Perry KM, Fauman EB, Finer-Moore JS, Montfort WR, Maley GF, Maley F, Stroud RM. Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases. Proteins. 8: 315-33. PMID 2128651 DOI: 10.1002/Prot.340080406  0.676
1990 Montfort WR, Perry KM, Fauman EB, Finer-Moore JS, Maley GF, Hardy L, Maley F, Stroud RM. Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate [Erratum to document cited in CA113(7):54978v] Biochemistry. 29: 10864-10864. DOI: 10.1021/Bi00500A022  0.648
1990 Stroud RM. What the structure of the acetylcholine receptor tells us about function of the ligand gated ion channel family Progress in Cell Research. 1: 123-138. DOI: 10.1016/B978-0-444-81125-7.50018-9  0.421
1989 Love RA, Stroud RM. The crystal structure of alpha-bungarotoxin at 2.5 A resolution: relation to solution structure and binding to acetylcholine receptor. Protein Engineering. 1: 37-46. PMID 3507686 DOI: 10.1093/Protein/1.1.37  0.474
1989 Basson ME, Thorsness M, Finer-Moore J, Stroud RM, Rine J. Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis. Molecular and Cellular Biology. 8: 3797-808. PMID 3065625 DOI: 10.1128/Mcb.8.9.3797  0.446
1989 Poulter L, Earnest JP, Stroud RM, Burlingame AL. Structure, oligosaccharide structures, and posttranslationally modified sites of the nicotinic acetylcholine receptor Proceedings of the National Academy of Sciences of the United States of America. 86: 6645-6649. PMID 2771948 DOI: 10.1073/Pnas.86.17.6645  0.467
1989 Mitra AK, McCarthy MP, Stroud RM. Three-dimensional structure of the nicotinic acetylcholine receptor and location of the major associated 43-kD cytoskeletal protein, determined at 22 A by low dose electron microscopy and x-ray diffraction to 12.5 A. The Journal of Cell Biology. 109: 755-74. PMID 2760111 DOI: 10.1083/Jcb.109.2.755  0.502
1989 Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE, Stroud RM. Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase Proceedings of the National Academy of Sciences of the United States of America. 86: 8635-8639. PMID 2682654 DOI: 10.1073/Pnas.86.22.8635  0.629
1989 Falick AM, Mel SF, Stroud RM, Burlingame AL. 15 – A New Strategy For Mapping The Topography Of A Transmembrane Protein Using Mass Spectrometry1 Techniques in Protein Chemistry. 152-159. DOI: 10.1016/B978-0-12-682001-0.50022-1  0.771
1988 Basus VJ, Billeter M, Love RA, Stroud RM, Kuntz ID. Structural studies of alpha-bungarotoxin. 1. Sequence-specific 1H NMR resonance assignments. Biochemistry. 27: 2763-71. PMID 3401447 DOI: 10.1021/Bi00408A016  0.424
1987 Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS. The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis. Science (New York, N.Y.). 237: 905-9. PMID 3112942 DOI: 10.1126/Science.3112942  0.448
1987 Hardy LW, Finer-Moore JS, Montfort WR, Jones MO, Santi DV, Stroud RM. Atomic structure of thymidylate synthase: target for rational drug design. Science (New York, N.Y.). 235: 448-55. PMID 3099389 DOI: 10.1126/Science.3099389  0.704
1987 Stroud RM, Finer-Moore J. Acetylcholine receptor structure, function, and evolution. Annual Review of Cell Biology. 1: 317-51. PMID 2435309 DOI: 10.1146/Annurev.Cb.01.110185.001533  0.403
1986 Fairclough RH, Miake-Lye RC, Stroud RM, Hodgson KO, Doniach S. Location of terbium binding sites on acetylcholine receptor-enriched membranes. Journal of Molecular Biology. 189: 673-80. PMID 3783687 DOI: 10.1016/0022-2836(86)90497-3  0.418
1986 Katre NV, Kimura Y, Stroud RM. Cation binding sites on the projected structure of bacteriorhodopsin. Biophysical Journal. 50: 277-84. PMID 3741984 DOI: 10.1016/S0006-3495(86)83461-0  0.43
1986 McCarthy MP, Earnest JP, Young EF, Choe S, Stroud RM. The molecular neurobiology of the acetylcholine receptor. Annual Review of Neuroscience. 9: 383-413. PMID 2423008 DOI: 10.1146/Annurev.Ne.09.030186.002123  0.612
1986 Masters SB, Stroud RM, Bourne HR. Family of G protein α chains: amphipathic analysis and predicted structure of functional domains "Protein Engineering, Design and Selection". 1: 47-54. DOI: 10.1093/Protein/1.1.47  0.409
1986 Thomas GJ, Prescott B, Love R, Stroud RM. Evidence for conformational differences in aqueous and crystalline structures of α-bungarotoxin and cobratoxin Spectrochimica Acta Part a: Molecular Spectroscopy. 42: 215-222. DOI: 10.1016/0584-8539(86)80182-9  0.431
1985 Young EF, Ralston E, Blake J, Ramachandran J, Hall ZW, Stroud RM. Topological mapping of acetylcholine receptor: evidence for a model with five transmembrane segments and a cytoplasmic COOH-terminal peptide. Proceedings of the National Academy of Sciences of the United States of America. 82: 626-30. PMID 3881770 DOI: 10.1073/Pnas.82.2.626  0.422
1984 Katre NV, Finer-Moore J, Stroud RM, Hayward SB. Location of an extrinsic label in the primary and tertiary structure of bacteriorhodopsin. Biophysical Journal. 46: 195-203. PMID 6478034 DOI: 10.1016/S0006-3495(84)84013-8  0.424
1984 Finer-Moore J, Stroud RM, Prescott B, Thomas GJ. Subunit secondary structure in filamentous viruses: predictions and observations. Journal of Biomolecular Structure & Dynamics. 2: 93-100. PMID 6400935 DOI: 10.1080/07391102.1984.10507549  0.412
1984 Finer-Moore J, Stroud RM. Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor. Proceedings of the National Academy of Sciences of the United States of America. 81: 155-9. PMID 6320162 DOI: 10.1073/Pnas.81.1.155  0.449
1983 Fairclough RH, Finer-Moore J, Love RA, Kristofferson D, Desmeules PJ, Stroud RM. Subunit organization and structure of an acetylcholine receptor Cold Spring Harbor Symposia On Quantitative Biology. 48: 9-20. PMID 6586365 DOI: 10.1101/Sqb.1983.048.01.004  0.427
1982 Agard DA, Stroud RM. Linking regions between helices in bacteriorhodopsin revealed. Biophysical Journal. 37: 589-602. PMID 7074187  0.54
1982 Kistler J, Stroud RM, Klymkowsky MW, Lalancette RA, Fairclough RH. Structure and function of an acetylcholine receptor. Biophysical Journal. 37: 371-83. PMID 7055628 DOI: 10.1016/S0006-3495(82)84685-7  0.675
1982 Agard DA, Stroud RM. α-Bungaratoxin structure revealed by a rapid method for averaging electron density of non-crystallographically translationally related molecules Acta Crystallographica Section A. 38: 186-194. DOI: 10.1107/S0567739482000436  0.567
1981 Stroud RM, Serwer P, Ross MJ. Assembly of bacteriophage T7. Dimensions of the bacteriophage and its capsids. Biophysical Journal. 36: 743-57. PMID 7326332 DOI: 10.1016/S0006-3495(81)84763-7  0.577
1981 Agard DA, Steinberg RA, Stroud RM. Quantitative analysis of electrophoretograms: a mathematical approach to super-resolution. Analytical Biochemistry. 111: 257-68. PMID 7247021 DOI: 10.1016/0003-2697(81)90562-5  0.503
1981 Kistler J, Stroud RM. Crystalline arrays of membrane-bound acetylcholine receptor. Proceedings of the National Academy of Sciences of the United States of America. 78: 3678-82. PMID 6943572 DOI: 10.1073/Pnas.78.6.3678  0.438
1981 Katre NV, Wolber PK, Stoeckenius W, Stroud RM. Attachment site(s) of retinal in bacteriorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 78: 4068-72. PMID 6794028 DOI: 10.1073/Pnas.78.7.4068  0.405
1981 Tobler J, Krieger M, Stroud RM. The binding and processing of plasminogen by Balb/c 3T3 and SV3T3 cells. Journal of Cellular Physiology. 108: 277-90. PMID 6267086 DOI: 10.1002/Jcp.1041080217  0.553
1980 Klymkowsky MW, Heuser JE, Stroud RM. Protease effects on the structure of acetylcholine receptor membranes from Torpedo californica. The Journal of Cell Biology. 85: 823-38. PMID 6993498 DOI: 10.1083/Jcb.85.3.823  0.638
1979 Klymkowsky MW, Stroud RM. Immunospecific identification and three-dimensional structure of a membrane-bound acetylcholine receptor from Torpedo californica. Journal of Molecular Biology. 128: 319-34. PMID 439138 DOI: 10.1016/0022-2836(79)90091-3  0.632
1979 Stroud RM, Agard DA. Structure determination of asymmetric membrane profiles using an iterative Fourier method. Biophysical Journal. 25: 495-512. PMID 318062 DOI: 10.1016/S0006-3495(79)85319-9  0.565
1979 Chambers JL, Stroud RM. The accuracy of refined protein structures: comparison of two independently refined models of bovine trypsin Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 35: 1861-1874. DOI: 10.1107/S0567740879007925  0.464
1977 Ross MJ, Klymkowsky MW, Agard DA, Stroud RM. Structural studies of a membrane-bound acetylcholine receptor from Torpedo californica. Journal of Molecular Biology. 116: 635-59. PMID 563472 DOI: 10.1016/0022-2836(77)90264-9  0.716
1977 Kossiakoff AA, Chambers JL, Kay LM, Stroud RM. Structure of bovine trypsinogen at 1.9 A resolution. Biochemistry. 16: 654-64. PMID 556951 DOI: 10.1021/Bi00623A016  0.731
1977 Stroud RM, Kossiakoff AA, Chambers JL. Mechanisms of zymogen activation. Annual Review of Biophysics and Bioengineering. 6: 177-93. PMID 17350 DOI: 10.1146/annurev.bb.06.060177.001141  0.648
1977 Koeppe RE, Krieger M, Stroud RM. The effect of pre-incubation on trypsin kinetics at low pH. Biochimica Et Biophysica Acta. 481: 617-21. PMID 15615 DOI: 10.1016/0005-2744(77)90294-7  0.643
1977 Chambers JL, Stroud RM. Difference Fourier refinement of the structure of DIP-trypsin at 1.5 Å with a minicomputer technique Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 33: 1824-1837. DOI: 10.1107/S0567740877007146  0.413
1976 Koeppe RE, Stroud RM. A pulsed diffusion technique for the growth of protein crystals for x-ray diffraction. Journal of Molecular Biology. 98: 155-60. PMID 1195375 DOI: 10.1016/S0022-2836(75)80106-9  0.577
1976 Koeppe RE, Stroud RM. Mechanism of hydrolysis by serine proteases: direct determination of the pKa's of aspartyl-102 and aspartyl-194 in bovine trypsin using difference infrared spectroscopy. Biochemistry. 15: 3450-8. PMID 986162 DOI: 10.1021/Bi00661A009  0.592
1976 Krieger M, Koeppe RE, Stroud RM. pH dependence of tritium exchange with the C-2 protons of the histidines in bovine trypsin. Biochemistry. 15: 3458-64. PMID 8090 DOI: 10.1021/Bi00661A010  0.656
1976 Krieger M, Stroud RM. Data collection in protein crystallography: experimental methods for reducing background radiation Acta Crystallographica Section A. 32: 653-656. DOI: 10.1107/S0567739476001356  0.534
1975 Volanakis JE, Stroud RM. Rabbit C1q: purification, functional and structural studies. Journal of Immunological Methods. 2: 25-34. PMID 4139208 DOI: 10.1016/0022-1759(72)90014-2  0.42
1974 Chambers JL, Christoph GG, Krieger M, Kay L, Stroud RM. Silver ion inhibition of serine proteases: crystallographic study of silver-trypsin. Biochemical and Biophysical Research Communications. 59: 70-4. PMID 4842294 DOI: 10.1016/S0006-291X(74)80175-0  0.564
1974 Krieger M, Kay LM, Stroud RM. Structure and specific binding of trypsin: comparison of inhibited derivatives and a model for substrate binding. Journal of Molecular Biology. 83: 209-30. PMID 4821871 DOI: 10.1016/0022-2836(74)90388-X  0.618
1974 Stroud RM, Kay LM, Dickerson RE. The structure of bovine trypsin: electron density maps of the inhibited enzyme at 5 Angstrom and at 2-7 Angstron resolution. Journal of Molecular Biology. 83: 185-208. PMID 4821870 DOI: 10.1016/0022-2836(74)90387-8  0.635
1974 Krieger M, Chambers JL, Christoph GG, Stroud RM, Trus BL. Data collection in protein crystallography: capillary effects and background corrections Acta Crystallographica Section A. 30: 740-748. DOI: 10.1107/S0567739474001811  0.538
1973 Stroud RM. The crystal and molecular structure of tubercidin, C11H14N4O4 Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 29: 690-696. DOI: 10.1107/S0567740873003183  0.439
1972 Stroud RM, Kay LM, Dickerson RE. The crystal and molecular structure of DIP-inhibited bovine trypsin at2.7Angstrom resolution. Cold Spring Harbor Symposia On Quantitative Biology. 36: 125-40. PMID 4508129 DOI: 10.1101/Sqb.1972.036.01.018  0.629
1972 Stroud RM, Carlisle CH. A single-crystal structure determination of DL-6-thioctic acid, C8H14O2S2 Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 28: 304-307. DOI: 10.1107/S0567740872002225  0.421
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