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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

260 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
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  1
2021 Kholodar SA, Finer-Moore JS, Świderek K, Arafet K, Moliner V, Stroud RM, Kohen A. Caught in Action: X-ray Structure of Thymidylate Synthase with Noncovalent Intermediate Analog. Biochemistry. PMID 33829766 DOI: 10.1021/acs.biochem.1c00063  0.8
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  1
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  0.56
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  1
2020 Li F, Eriksen J, Finer-Moore J, Chang R, Nguyen P, Bowen A, Myasnikov A, Yu Z, Bulkley D, Cheng Y, Edwards RH, Stroud RM. Ion transport and regulation in a synaptic vesicle glutamate transporter. Science (New York, N.Y.). 368: 893-897. PMID 32439795 DOI: 10.1126/Science.Aba9202  0.52
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  0.52
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  0.96
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  1
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  0.72
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  1
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: 10.2210/Pdb6E1N/Pdb  0.8
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  0.8
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  0.8
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  0.32
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  0.8
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  0.36
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  0.72
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  0.88
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  1
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  0.64
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  1
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  1
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  0.44
2015 Tochowicz A, Santucci M, Saxena P, Guaitoli G, Trande M, Finer-Moore J, Stroud RM, Costi MP. Alanine mutants of the interface residues of human thymidylate synthase decode key features of the binding mode of allosteric anticancer peptides Journal of Medicinal Chemistry. 58: 1012-1018. PMID 25427005 DOI: 10.1021/Jm5011176  0.52
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  1
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  0.72
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  0.72
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  1
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  1
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  1
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  1
2014 Harris VG, Chen Y, Byers JM, Stroud RM, Browning VM, Fuller-Mora WW, Osofsky MS, Kim J, Knies D, Grabowski KS. Enhanced Jahn-Teller response induced by low-dose 10 MeV I+ irradiation of La0.7Ca0.3MnO3-δ films Applied Physics Letters. 104. DOI: 10.1063/1.4875385  0.56
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  1
2013 Tochowicz A, Dalziel S, Eidam O, O'Connell JD, Griner S, Finer-Moore JS, Stroud RM. Development and binding mode assessment of N-[4-[2-Propyn-1-yl[(6 S)-4,6,7,8-tetrahydro-2-(hydroxymethyl)-4-oxo-3H-cyclopenta[g]quinazolin-6-yl] amino]benzoyl]-L-γ-glutamyl-D-glutamic acid (BGC 945), a novel thymidylate synthase inhibitor that targets tumor cells Journal of Medicinal Chemistry. 56: 5446-5455. PMID 23710599 DOI: 10.1021/Jm400490E  1
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  1
2013 Waight AB, Pedersen BP, Schlessinger A, Bonomi M, Chau BH, Roe-Zurz Z, Risenmay AJ, Sali A, Stroud RM. Structural basis for alternating access of a eukaryotic calcium/proton exchanger Nature. 499: 107-110. PMID 23685453 DOI: 10.1038/Nature12233  1
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  1
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  1
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  1
2012 Carosati E, Tochowicz A, Marverti G, Guaitoli G, Benedetti P, Ferrari S, Stroud RM, Finer-Moore J, Luciani R, Farina D, Cruciani G, Costi MP. Inhibitor of ovarian cancer cells growth by virtual screening: a new thiazole derivative targeting human thymidylate synthase. Journal of Medicinal Chemistry. 55: 10272-6. PMID 23075414 DOI: 10.1021/Jm300850V  1
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  1
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  1
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  1
2012 Varrin-Doyer M, Spencer CM, Schulze-Topphoff U, Nelson PA, Stroud RM, Cree BA, Zamvil SS. Aquaporin 4-specific T cells in neuromyelitis optica exhibit a Th17 bias and recognize Clostridium ABC transporter. Annals of Neurology. 72: 53-64. PMID 22807325 DOI: 10.1002/Ana.23651  1
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  1
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  1
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  1
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  1
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  1
2011 Stroud RM, Schertler GFX. Membranes Current Opinion in Structural Biology. 21: 495-496. PMID 21875531 DOI: 10.1016/j.sbi.2011.08.001  1
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  1
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  1
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  1
2011 Stroud RM. New tools in membrane protein determination F1000 Biology Reports. 3. DOI: 10.3410/B3  1
2011 Stroud RM. An insoluble problem? Scientist. 25.  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2010 Stroud RM. Overview of cytokine receptors Handbook of Cell Signaling, 2/E. 1: 235-236. DOI: 10.1016/B978-0-12-374145-5.00035-8  1
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  1
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  1
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  1
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  1
2009 Alian A, DeGiovanni A, Griner SL, Finer-Moore JS, Stroud RM. Crystal structure of an RluF-RNA complex: a base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome. Journal of Molecular Biology. 388: 785-800. PMID 19298824 DOI: 10.1016/J.Jmb.2009.03.029  1
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  1
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  1
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  1
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  1
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  1
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  1
2008 Stroud RM. Michael A. Raftery (1936-2007)--the first enzyme mechanism, sequential cooperativity, and the nicotinic acetylcholine receptor defined. Protein Science : a Publication of the Protein Society. 17: 1864-6. PMID 18819191 DOI: 10.1002/Pro.171864  1
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  1
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  1
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  1
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  1
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  1
2007 Hamelberg D, Shen T, McCammon JA. A proposed signaling motif for nuclear import in mRNA processing via the formation of arginine claw. Proceedings of the National Academy of Sciences of the United States of America. 104: 14947-51. PMID 17823247 DOI: 10.1073/Pnas.0703151104  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2007 Stroud RM. Transmembrane transporters: an open and closed case. Proceedings of the National Academy of Sciences of the United States of America. 104: 1445-6. PMID 17251354 DOI: 10.1073/Pnas.0610349104  1
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  1
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  1
2007 Finer-Moore JS, Stroud RM. Preface Rsc Biomolecular Sciences. v-ix.  1
2007 Finer-Moore JS, Blaney J, Stroud RM. Facing the wall in computationally based approaches to drug discovery Rsc Biomolecular Sciences. 3-23.  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2005 Laporte SL, Forsyth CM, Cunningham BC, Miercke LJ, Akhavan D, Stroud RM. De novo design of an IL-4 antagonist and its structure at 1.9 A. Proceedings of the National Academy of Sciences of the United States of America. 102: 1889-94. PMID 15684085 DOI: 10.1073/Pnas.0408890102  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  0.52
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  1
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  0.56
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  1
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  1
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  0.52
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  0.6
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  0.72
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  1
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  0.8
2003 Stroud RM, Finer-Moore JS. Conformational dynamics along an enzymatic reaction pathway: thymidylate synthase, "the movie". Biochemistry. 42: 239-47. PMID 12525150 DOI: 10.1021/Bi020598I  0.8
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  0.92
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  1
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  1
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  1
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  0.44
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  1
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  0.72
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  1
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  1
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  0.6
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  1
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  1
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  1
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  0.72
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  1
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  1
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  1
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  0.72
2000 Kawase S, Cho SW, Rozelle J, Stroud RM, Finer-Moore J, Santi DV. Replacement set mutagenesis of the four phosphate-binding arginine residues of thymidylate synthase. Protein Engineering. 13: 557-63. PMID 10964985 DOI: 10.1093/Protein/13.8.557  0.56
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  1
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  1
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  0.8
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  1
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  0.56
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  0.56
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  1
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  1
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  1
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  0.72
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  1
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  1
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  0.56
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  1
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  0.8
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  0.8
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  1
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  1
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  1
1997 Wiener M, Freymann D, Ghosh P, Stroud RM. Crystal structure of colicin Ia. Nature. 385: 461-4. PMID 9009197 DOI: 10.1038/385461A0  1
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  1
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  0.48
1997 Rutenber EE, Stroud RM. Binding of the anticancer drug ZD1694 to E. coli thymidylate synthase: assessing specificity and affinity. Structure (London, England : 1993). 4: 1317-24. PMID 8939755 DOI: 10.1016/S0969-2126(96)00139-6  0.4
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  1
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  0.8
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  1
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  1
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  1
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  0.4
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  1
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  0.52
1995 Stroud R. An inducement to collaboration Nature Structural & Molecular Biology. 2: 619-620. DOI: 10.1038/Nsb0895-619  0.52
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  1
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  1
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  1
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  1
1993 Turner GJ, Miercke LJW, Thorgeirsson TE, Kliger DS, Betlach MC, Stroud RM. Bacteriorhodopsin D85N: Three spectroscopic species in equilibrium Biochemistry®. 32: 1332-1337. PMID 8448142 DOI: 10.1021/Bi00056A019  1
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  1
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  1
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  0.72
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  1
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  1
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  1
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  1
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  1
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  0.52
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  1
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  1
1991 Lin SW, Fodor SP, Miercke LJ, Shand RF, Betlach MC, Stroud RM, Mathies RA. Resonance Raman spectra of bacteriorhodopsin mutants with substitutions at Asp-85, Asp-96, and Arg-82 Photochemistry and Photobiology. 53: 341-346. PMID 2062880 DOI: 10.1111/J.1751-1097.1991.Tb03638.X  1
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  1
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  1
1991 Thorgeirsson TE, Milder SJ, Miercke LJ, Betlach MC, Shand RF, Stroud RM, Kliger DS. Effects of Asp-96----Asn, Asp-85----Asn, and Arg-82----Gln single-site substitutions on the photocycle of bacteriorhodopsin. Biochemistry. 30: 9133-42. PMID 1892824 DOI: 10.1021/Bi00102A003  1
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  0.8
1991 Earnest T, Fauman E, Craik CS, Stroud R. 1.59 Å structure of trypsin at 120 K: Comparison of low temperature and room temperature structures Proteins. 10: 171-187. PMID 1881877 DOI: 10.1002/Prot.340100303  0.8
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  1
1991 Ghosh P, Stroud RM. Ion channels formed by a highly charged peptide. Biochemistry. 30: 3551-7. PMID 1707312 DOI: 10.1021/Bi00228A028  0.96
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  1
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  1
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  1
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  1
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  1
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  0.48
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  1
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  1
1990 Stroud RM, McCarthy MP, Shuster M. Nicotinic acetylcholine receptor superfamily of ligand-gated ion channels. Biochemistry. 29: 11009-23. PMID 1703009 DOI: 10.1021/Bi00502A001  0.32
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  0.8
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  1
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  0.32
1989 McCarthy MP, Stroud RM. Conformational states of the nicotinic acetylcholine receptor from Torpedo californica induced by the binding of agonists, antagonists, and local anesthetics. Equilibrium measurements using tritium-hydrogen exchange. Biochemistry. 28: 40-8. PMID 2706266 DOI: 10.1021/Bi00427A007  0.32
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  1
1989 Miercke LJW, Stroud RM, Dratz EA. Preparative purification of functional bacteriorhodopsin by high-performance size-exclusion chromatography Journal of Chromatography A. 483: 331-340. PMID 2560474 DOI: 10.1016/S0021-9673(01)93132-2  1
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  1
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  1
1988 Poulter L, Earnest JP, Stroud RM, Burlingame AL. Cesium ion liquid secondary ion mass spectrometry of membrane‐bound glycoproteins: Structural and topological considerations of acetylcholine receptor from Torpedo californica Biological Mass Spectrometry. 16: 25-30. PMID 3242677 DOI: 10.1002/Bms.1200160105  1
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  1
1987 Vassarotti A, Stroud R, Douglas M. Independent mutations at the amino terminus of a protein act as surrogate signals for mitochondrial import. The Embo Journal. 6: 705-711. DOI: 10.1002/J.1460-2075.1987.Tb04811.X  0.52
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  1
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  1
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  1
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  0.52
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  1
1982 Agard DA, Stroud RM. Linking regions between helices in bacteriorhodopsin revealed. Biophysical Journal. 37: 589-602. PMID 7074187  1
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  1
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  1
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  1
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  1
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  0.68
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  1
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  1
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  1
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  1
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  1
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  1
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  0.68
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  0.4
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  0.44
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  0.68
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  0.68
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  1
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  1
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  1
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