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    Robert Stroud, MA, PhD

    TitleProfessor
    SchoolUCSF School of Medicine
    DepartmentBiochemistry and Biophysics
    Address600 16th Street
    San Francisco CA 94143
    Phone415-476-4224

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       Publications
      Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Researchers can login to make corrections and additions, or contact us for help.
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      1. 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. Proc Natl Acad Sci U S A. 2014 Jul 22; 111(29):10404-10.
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      2. Monk BC, Tomasiak TM, Keniya MV, Huschmann FU, Tyndall JD, 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. Proc Natl Acad Sci U S A. 2014 Mar 11; 111(10):3865-70.
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      3. Kumar H, Kasho V, Smirnova I, Finer-Moore JS, Kaback HR, Stroud RM. Structure of sugar-bound LacY. Proc Natl Acad Sci U S A. 2014 Feb 4; 111(5):1784-8.
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      4. 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 Res. 2014 Feb 1; 42(3):2037-48.
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      5. 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. Proc Natl Acad Sci U S A. 2013 Nov 12; 110(46):18484-9.
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      6. 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[(6S)-4,6,7,8-tetrahydro-2-(hydroxymethyl)-4-oxo-3H-cyclopenta[g]quinazolin-6-yl]amino]benzoyl]-l-?-glutamyl-d-glutamic Acid (BGC 945), a Novel Thymidylate Synthase Inhibitor That Targets Tumor Cells. J Med Chem. 2013 Jul 11; 56(13):5446-55.
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      7. 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. J Mol Biol. 2013 Oct 23; 425(20):3875-87.
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      8. 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. 2013 Jul 4; 499(7456):107-10.
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      9. 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. J Am Chem Soc. 2013 May 22; 135(20):7583-92.
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      10. 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. 2013 Apr 25; 496(7446):533-6.
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      11. 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, Stevens RC, Sali A. Coordinating the impact of structural genomics on the human a-helical transmembrane proteome. Nat Struct Mol Biol. 2013 Feb; 20(2):135-8.
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      12. 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. J Med Chem. 2012 Nov 26; 55(22):10272-6.
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      13. 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. J Am Chem Soc. 2012 Oct 24; 134(42):17722-30.
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      14. Metzger LE, Lee JK, Finer-Moore JS, Raetz CR, Stroud RM. LpxI structures reveal how a lipid A precursor is synthesized. Nat Struct Mol Biol. 2012 Nov; 19(11):1132-8.
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      15. 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 Crystallogr D Biol Crystallogr. 2012 Sep; 68(Pt 9):1232-41.
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      16. 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. Ann Neurol. 2012 Jul; 72(1):53-64.
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      17. 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. 2012; 7(4):e34918.
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      18. 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, Tampé R, Edwards RH, Stroud RM, Craik CS, Cheng Y. Fabs enable single particle cryoEM studies of small proteins. Structure. 2012 Apr 4; 20(4):582-92.
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      19. Chaudhary S, Pak JE, Gruswitz F, Sharma V, Stroud RM. Overexpressing human membrane proteins in stably transfected and clonal human embryonic kidney 293S cells. Nat Protoc. 2012 Mar; 7(3):453-66.
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      20. Kim J, Stroud RM, Craik CS. Rapid identification of recombinant Fabs that bind to membrane proteins. Methods. 2011 Dec; 55(4):303-9.
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      21. Chaudhary S, Pak JE, Pedersen BP, Bang LJ, Zhang LB, Ngaw SM, Green RG, Sharma V, Stroud RM. Efficient expression screening of human membrane proteins in transiently transfected Human Embryonic Kidney 293S cells. Methods. 2011 Dec; 55(4):273-80.
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      22. Stroud RM, Schertler GF. Membranes. Curr Opin Struct Biol. 2011 Aug; 21(4):495-6.
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      23. 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. Proc Natl Acad Sci U S A. 2011 Aug 16; 108(33):13450-5.
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      24. 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 Biol. 2011; 9:48.
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      25. 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 Biol. 2011; 9:47.
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      26. Stroud RM. New tools in membrane protein determination. F1000 Biol Rep. 2011; 3:8.
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      27. 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. 2010; 5(11):e15050.
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      28. Egea PF, Stroud RM. Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proc Natl Acad Sci U S A. 2010 Oct 5; 107(40):17182-7.
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      29. Savage DF, O'Connell JD, Miercke LJ, Finer-Moore J, Stroud RM. Structural context shapes the aquaporin selectivity filter. Proc Natl Acad Sci U S A. 2010 Oct 5; 107(40):17164-9.
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      30. Lee JK, Stroud RM. Unlocking the eukaryotic membrane protein structural proteome. Curr Opin Struct Biol. 2010 Aug; 20(4):464-70.
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      31. 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. Proc Natl Acad Sci U S A. 2010 Jun 15; 107(24):11038-43.
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      32. 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. Proc Natl Acad Sci U S A. 2010 May 25; 107(21):9638-43.
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      33. Hays FA, Roe-Zurz Z, Stroud RM. Overexpression and purification of integral membrane proteins in yeast. Methods Enzymol. 2010; 470:695-707.
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      34. 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 Sci. 2010 Mar; 19(3):412-28.
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      35. 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. J Struct Funct Genomics. 2009 Dec; 10(4):269-80.
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      36. 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. Proc Natl Acad Sci U S A. 2009 May 19; 106(20):8192-7.
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      37. 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. Proc Natl Acad Sci U S A. 2009 May 5; 106(18):7437-42.
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      38. 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. J Mol Biol. 2009 May 15; 388(4):785-800.
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      39. 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. J Struct Funct Genomics. 2009 Apr; 10(2):193-208.
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      40. 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. Nat Protoc. 2009; 4(5):619-37.
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      41. 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. 2009 Feb 5; 457(7230):687-93.
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      42. 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. J Mol Biol. 2009 Jan 23; 385(3):820-30.
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      43. 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. J Struct Funct Genomics. 2009 Mar; 10(1):9-16.
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      44. 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. 2008; 3(11):e3619.
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      45. 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. 2008; 3(10):e3528.
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      46. Stroud RM. Michael A. Raftery (1936-2007)--the first enzyme mechanism, sequential cooperativity, and the nicotinic acetylcholine receptor defined. Protein Sci. 2008 Oct; 17(10):1864-6.
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      47. Lee JK, Belogrudov GI, Stroud RM. Crystal structure of bovine mitochondrial factor B at 0.96-A resolution. Proc Natl Acad Sci U S A. 2008 Sep 9; 105(36):13379-84.
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      48. 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. Nat Struct Mol Biol. 2008 Jun; 15(6):619-25.
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      49. 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. Proc Natl Acad Sci U S A. 2008 May 13; 105(19):6876-81.
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      50. 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. Proc Natl Acad Sci U S A. 2008 Feb 19; 105(7):2391-6.
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      51. Menuz K, Stroud RM, Nicoll RA, Hays FA. TARP auxiliary subunits switch AMPA receptor antagonists into partial agonists. Science. 2007 Nov 2; 318(5851):815-7.
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      52. Reyes CL, Rutenber E, Walter P, Stroud RM. X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates. PLoS One. 2007; 2(7):e607.
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      53. 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. 2007 Jul; 13(7):1043-51.
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      54. Savage DF, Anderson CL, Robles-Colmenares Y, Newby ZE, Stroud RM. Cell-free complements in vivo expression of the E. coli membrane proteome. Protein Sci. 2007 May; 16(5):966-76.
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      55. Hur S, Stroud RM. How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Mol Cell. 2007 Apr 27; 26(2):189-203.
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      56. 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 Res. 2007; 35(8):2651-60.
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      57. Savage DF, Stroud RM. Structural basis of aquaporin inhibition by mercury. J Mol Biol. 2007 May 4; 368(3):607-17.
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      58. Pan H, Ho JD, Stroud RM, Finer-Moore J. The crystal structure of E. coli rRNA pseudouridine synthase RluE. J Mol Biol. 2007 Apr 13; 367(5):1459-70.
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      59. Stroud RM. Transmembrane transporters: an open and closed case. Proc Natl Acad Sci U S A. 2007 Jan 30; 104(5):1445-6.
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      60. 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. Proc Natl Acad Sci U S A. 2007 Jan 2; 104(1):42-7.
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      61. Khademi S, Stroud RM. The Amt/MEP/Rh family: structure of AmtB and the mechanism of ammonia gas conduction. Physiology (Bethesda). 2006 Dec; 21:419-29.
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      62. Hur S, Stroud RM, Finer-Moore J. Substrate recognition by RNA 5-methyluridine methyltransferases and pseudouridine synthases: a structural perspective. J Biol Chem. 2006 Dec 22; 281(51):38969-73.
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      63. 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. J Med Chem. 2006 Oct 19; 49(21):6308-23.
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      64. 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. 2006 Jun 20; 45(24):7415-28.
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      65. Keatinge-Clay AT, Stroud RM. The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases. Structure. 2006 Apr; 14(4):737-48.
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      66. Credle JJ, Finer-Moore JS, Papa FR, Stroud RM, Walter P. On the mechanism of sensing unfolded protein in the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2005 Dec 27; 102(52):18773-84.
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      67. 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. Proc Natl Acad Sci U S A. 2005 Dec 27; 102(52):18932-7.
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      68. 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 Crystallogr D Biol Crystallogr. 2005 Oct; 61(Pt 10):1320-34.
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      69. 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. J Biol Chem. 2005 Nov 18; 280(46):38823-30.
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      70. Egea PF, Stroud RM, Walter P. Targeting proteins to membranes: structure of the signal recognition particle. Curr Opin Struct Biol. 2005 Apr; 15(2):213-20.
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      71. 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. 2005 Mar 11; 120(5):599-611.
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      72. 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. Proc Natl Acad Sci U S A. 2005 Feb 8; 102(6):1889-94.
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      73. 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. Proc Natl Acad Sci U S A. 2004 Nov 23; 101(47):16454-9.
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      74. Shan SO, Stroud RM, Walter P. Mechanism of association and reciprocal activation of two GTPases. PLoS Biol. 2004 Oct; 2(10):e320.
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      75. Harries WE, Akhavan D, Miercke LJ, Khademi S, Stroud RM. The channel architecture of aquaporin 0 at a 2.2-A resolution. Proc Natl Acad Sci U S A. 2004 Sep 28; 101(39):14045-50.
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      76. 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. 2004 Sep 10; 305(5690):1587-94.
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      77. Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM. An antibiotic factory caught in action. Nat Struct Mol Biol. 2004 Sep; 11(9):888-93.
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      78. Agarwalla S, Stroud RM, Gaffney BJ. Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies. J Biol Chem. 2004 Aug 13; 279(33):34123-9.
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      79. Stroud RM, Wells JA. Mechanistic diversity of cytokine receptor signaling across cell membranes. Sci STKE. 2004 May 4; 2004(231):re7.
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      80. Lee TT, Agarwalla S, Stroud RM. Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase. Structure. 2004 Mar; 12(3):397-407.
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      81. Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM. Substrate twinning activates the signal recognition particle and its receptor. Nature. 2004 Jan 15; 427(6971):215-21.
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      82. 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 Biol. 2003 Dec; 1(3):E72.
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      83. 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. 2003 Dec; 11(12):1609-20.
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      84. 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. J Mol Biol. 2003 Nov 28; 334(3):435-44.
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      85. 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. J Synchrotron Radiat. 2004 Jan 1; 11(Pt 1):86-8.
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      86. 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 Lett. 2003 Nov 27; 555(1):79-84.
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      87. 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. Proc Natl Acad Sci U S A. 2003 Oct 28; 100(22):12648-53.
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      88. 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. J Biol Chem. 2003 Dec 26; 278(52):52980-7.
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      89. 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. Curr Opin Struct Biol. 2003 Aug; 13(4):424-31.
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      90. 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 Eng. 2003 Aug; 16(8):607-14.
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      91. Jez JM, Chen JC, Rastelli G, Stroud RM, Santi DV. Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chem Biol. 2003 Apr; 10(4):361-8.
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      92. 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. 2003 Mar 11; 42(9):2616-24.
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      93. 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 Eng. 2003 Mar; 16(3):229-40.
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      94. 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. 2003 Feb; 11(2):147-54.
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      95. 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. 2003 Jan 21; 42(2):248-56.
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      96. Stroud RM, Finer-Moore JS. Conformational dynamics along an enzymatic reaction pathway: thymidylate synthase, "the movie". Biochemistry. 2003 Jan 21; 42(2):239-47.
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      97. Stroud RM, Nollert P, Miercke L. The glycerol facilitator GlpF its aquaporin family of channels, and their selectivity. Adv Protein Chem. 2003; 63:291-316.
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      98. 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. J Eukaryot Microbiol. 2003; 50 Suppl:555-6.
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      99. 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. 2002 Nov; 10(11):1559-68.
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      100. 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. 2002 Oct 22; 41(42):12598-606.
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      101. 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. J Mol Biol. 2002 Jul 19; 320(4):783-99.
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      102. 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. Biochim Biophys Acta. 2002 Jul 18; 1587(2-3):206-14.
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      103. 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. 2002 Jun 4; 41(22):7021-9.
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      104. 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. 2002 Apr 19; 296(5567):525-30.
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      105. 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. 2002 Apr 9; 41(14):4582-94.
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      106. Agarwalla S, Kealey JT, Santi DV, Stroud RM. Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli. J Biol Chem. 2002 Mar 15; 277(11):8835-40.
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      107. Fu D, Libson A, Stroud R. The structure of GlpF, a glycerol conducting channel. Novartis Found Symp. 2002; 245:51-61; discussion 61-5, 165-8.
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      108. 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. Proc Natl Acad Sci U S A. 2001 Dec 18; 98(26):14808-13.
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      109. 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. J Mol Biol. 2001 Nov 2; 313(4):813-29.
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      110. 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. Chem Biol. 2001 Oct; 8(10):981-95.
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      111. 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 Lett. 2001 Aug 31; 504(3):112-7.
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      112. Morse RJ, Yamamoto T, Stroud RM. Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure. 2001 May 9; 9(5):409-17.
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      113. 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. Chem Biol. 2001 May; 8(5):445-57.
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      114. Lackey DB, Groziak MP, Sergeeva M, Beryt M, Boyer C, Stroud RM, Sayre P, Park JW, Johnston P, Slamon D, Shepard HM, Pegram M. Enzyme-catalyzed therapeutic agent (ECTA) design: activation of the antitumor ECTA compound NB1011 by thymidylate synthase. Biochem Pharmacol. 2001 Jan 15; 61(2):179-89.
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      115. Keenan RJ, Freymann DM, Stroud RM, Walter P. The signal recognition particle. Annu Rev Biochem. 2001; 70:755-75.
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      116. 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. 2000 Oct 24; 39(42):12796-803.
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      117. 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. 2000 Oct 20; 290(5491):481-6.
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      118. Erlanson DA, Braisted AC, Raphael DR, Randal M, Stroud RM, Gordon EM, Wells JA. Site-directed ligand discovery. Proc Natl Acad Sci U S A. 2000 Aug 15; 97(17):9367-72.
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      119. 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 Eng. 2000 Aug; 13(8):557-63.
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      120. 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. Proc Natl Acad Sci U S A. 2000 Jul 18; 97(15):8233-8.
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      121. Wiener MC, Verkman AS, Stroud RM, van Hoek AN. Mesoscopic surfactant organization and membrane protein crystallization. Protein Sci. 2000 Jul; 9(7):1407-9.
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      122. 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. J Mol Biol. 2000 Mar 31; 297(3):645-57.
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      123. Variath P, Liu Y, Lee TT, Stroud RM, Santi DV. Effects of subunit occupancy on partitioning of an intermediate in thymidylate synthase mutants. Biochemistry. 2000 Mar 14; 39(10):2429-35.
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      124. 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. 2000 Feb 8; 39(5):1011-20.
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      125. 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. J Mol Biol. 2000 Jan 21; 295(3):377-85.
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      126. Foster PG, Huang L, Santi DV, Stroud RM. The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nat Struct Biol. 2000 Jan; 7(1):23-7.
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      127. Stroud RM, Walter P. Signal sequence recognition and protein targeting. Curr Opin Struct Biol. 1999 Dec; 9(6):754-9.
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      128. 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 Expr Purif. 1999 Nov; 17(2):324-38.
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      129. 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. 1999 Oct 19; 38(42):13829-36.
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      130. Freymann DM, Keenan RJ, Stroud RM, Walter P. Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat Struct Biol. 1999 Aug; 6(8):793-801.
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      131. 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. J Med Chem. 1999 Jun 17; 42(12):2112-24.
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      132. 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, Matthews DJ, Cheetham JC, Egrie J, Giebel LB, Stroud RM. Engineering a soluble extracellular erythropoietin receptor (EPObp) in Pichia pastoris to eliminate microheterogeneity, and its complex with erythropoietin. Protein Eng. 1999 Jun; 12(6):505-13.
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      133. 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. 1999 Feb 2; 38(5):1607-17.
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      134. 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. J Mol Biol. 1998 Dec 4; 284(3):699-712.
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      135. Stout TJ, Schellenberger U, Santi DV, Stroud RM. Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis. Biochemistry. 1998 Oct 20; 37(42):14736-47.
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      136. 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, Wendoloski JJ, Egrie J, Stroud RM. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature. 1998 Oct 1; 395(6701):511-6.
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      137. 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. 1998 Sep 29; 37(39):13893-901.
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      138. Stroud RM, Reiling K, Wiener M, Freymann D. Ion-channel-forming colicins. Curr Opin Struct Biol. 1998 Aug; 8(4):525-33.
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      139. Schafmeister CE, Stroud RM. Helical protein design. Curr Opin Biotechnol. 1998 Aug; 9(4):350-3.
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      140. Keenan RJ, Freymann DM, Walter P, Stroud RM. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell. 1998 Jul 24; 94(2):181-91.
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      141. Stout TJ, Sage CR, Stroud RM. The additivity of substrate fragments in enzyme-ligand binding. Structure. 1998 Jul 15; 6(7):839-48.
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      142. 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. 1998 Apr 14; 37(15):5107-17.
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      143. 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 Eng. 1998 Mar; 11(3):171-83.
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      144. Rose RB, Craik CS, Stroud RM. Domain flexibility in retroviral proteases: structural implications for drug resistant mutations. Biochemistry. 1998 Feb 24; 37(8):2607-21.
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      145. 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. J Mol Biol. 1998 Feb 13; 276(1):113-29.
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      146. 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. 1998 Feb 5; 391(6667):608-12.
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      147. Agarwalla S, LaPorte S, Liu L, Finer-Moore J, Stroud RM, Santi DV. A novel dCMP methylase by engineering thymidylate synthase. Biochemistry. 1997 Dec 16; 36(50):15909-17.
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      148. Schafmeister CE, LaPorte SL, Miercke LJ, Stroud RM. A designed four helix bundle protein with native-like structure. Nat Struct Biol. 1997 Dec; 4(12):1039-46.
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      149. Finer-Moore J, Tsutakawa SE, Cherbavaz DR, LaPorte DC, Koshland DE, Stroud RM. Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting. Biochemistry. 1997 Nov 11; 36(45):13890-6.
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      150. 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. Bioorg Med Chem. 1997 Jul; 5(7):1311-20.
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      151. Wiener M, Freymann D, Ghosh P, Stroud RM. Crystal structure of colicin Ia. Nature. 1997 Jan 30; 385(6615):461-4.
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      152. Freymann DM, Keenan RJ, Stroud RM, Walter P. Structure of the conserved GTPase domain of the signal recognition particle. Nature. 1997 Jan 23; 385(6614):361-4.
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      153. 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. 1996 Dec 17; 35(50):16270-81.
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      154. Rutenber EE, Stroud RM. Binding of the anticancer drug ZD1694 to E. coli thymidylate synthase: assessing specificity and affinity. Structure. 1996 Nov 15; 4(11):1317-24.
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      155. Rose RB, Craik CS, Douglas NL, Stroud RM. Three-dimensional structures of HIV-1 and SIV protease product complexes. Biochemistry. 1996 Oct 1; 35(39):12933-44.
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      156. 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. Bioorg Med Chem. 1996 Sep; 4(9):1545-58.
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      157. Stroud RM. Balancing ATP in the cell. Nat Struct Biol. 1996 Jul; 3(7):567-9.
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      158. 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. 1996 Apr 23; 35(16):5125-36.
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      159. 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. 1996 Apr 2; 35(13):3944-9.
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      160. 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. J Mol Biol. 1996 Jan 26; 255(3):522-35.
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      161. 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. 1996 Jan 15; 4(1):67-77.
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      162. 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 Eng. 1996 Jan; 9(1):69-75.
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      163. 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. 1995 Dec 19; 34(50):16279-87.
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      164. Stroud RM, Fauman EB. Significance of structural changes in proteins: expected errors in refined protein structures. Protein Sci. 1995 Nov; 4(11):2392-404.
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      165. Katz BA, Stroud RM, Collins N, Liu B, Arze R. Topochemistry for preparing ligands that dimerize receptors. Chem Biol. 1995 Sep; 2(9):591-600.
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      166. Stroud R. Ion channel forming colicins. Curr Opin Struct Biol. 1995 Aug; 5(4):514-20.
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      167. 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. 1995 Jul 4; 34(26):8264-80.
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      168. 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. 1994 Dec 27; 33(51):15459-68.
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      169. Ghosh P, Mel SF, Stroud RM. The domain structure of the ion channel-forming protein colicin Ia. Nat Struct Biol. 1994 Sep; 1(9):597-604.
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      170. Stroud RM. An electrostatic highway. Nat Struct Biol. 1994 Mar; 1(3):131-4.
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      171. 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. 1994 Feb 15; 33(6):1502-11.
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      172. 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. 1993 Nov 23; 32(46):12498-507.
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      173. Schafmeister CE, Miercke LJ, Stroud RM. Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins. Science. 1993 Oct 29; 262(5134):734-8.
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      174. Mel SF, Falick AM, Burlingame AL, Stroud RM. Mapping a membrane-associated conformation of colicin Ia. Biochemistry. 1993 Sep 14; 32(36):9473-9.
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      175. Mitra AK, Miercke LJ, 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. Biophys J. 1993 Sep; 65(3):1295-306.
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      176. 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. J Mol Biol. 1993 Aug 20; 232(4):1101-16.
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      177. 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. 1993 Jul 20; 32(28):7116-25.
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      178. Ghosh P, Mel SF, Stroud RM. A carboxy-terminal fragment of colicin Ia forms ion channels. J Membr Biol. 1993 Jun; 134(2):85-92.
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      179. Stroud RM, Finer-Moore JS. Stereochemistry of a multistep/bipartite methyl transfer reaction: thymidylate synthase. FASEB J. 1993 May; 7(8):671-7.
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      180. Shoichet BK, Stroud RM, Santi DV, Kuntz ID, Perry KM. Structure-based discovery of inhibitors of thymidylate synthase. Science. 1993 Mar 5; 259(5100):1445-50.
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      181. Mel SF, Stroud RM. Colicin Ia inserts into negatively charged membranes at low pH with a tertiary but little secondary structural change. Biochemistry. 1993 Mar 2; 32(8):2082-9.
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      182. Turner GJ, Miercke LJ, Thorgeirsson TE, Kliger DS, Betlach MC, Stroud RM. Bacteriorhodopsin D85N: three spectroscopic species in equilibrium. Biochemistry. 1993 Feb 9; 32(5):1332-7.
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      183. Kamb A, Finer-Moore JS, Stroud RM. Cofactor triggers the conformational change in thymidylate synthase: implications for an ordered binding mechanism. Biochemistry. 1992 Dec 29; 31(51):12876-84.
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      184. Kamb A, Finer-Moore J, Calvert AH, Stroud RM. Structural basis for recognition of polyglutamyl folates by thymidylate synthase. Biochemistry. 1992 Oct 20; 31(41):9883-90.
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      185. Perry KM, Pookanjanatavip M, Zhao J, Santi DV, Stroud RM. Reversible dissociation and unfolding of the dimeric protein thymidylate synthase. Protein Sci. 1992 Jun; 1(6):796-800.
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      186. 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. 1992 Mar; 12(3):203-22.
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      187. Schiffer CA, Caldwell JW, Stroud RM, Kollman PA. Inclusion of solvation free energy with molecular mechanics energy: alanyl dipeptide as a test case. Protein Sci. 1992 Mar; 1(3):396-400.
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      188. 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. 1991 Sep 24; 30(38):9133-42.
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      189. 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. 1991 Sep 3; 30(35):8671-8.
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      190. Lax I, Mitra AK, Ravera C, Hurwitz DR, Rubinstein M, Ullrich A, Stroud RM, Schlessinger J. Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor. A low resolution projection structure of the ligand-binding domain. J Biol Chem. 1991 Jul 25; 266(21):13828-33.
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      191. Schiffer CA, Davisson VJ, Santi DV, Stroud RM. Crystallization of human thymidylate synthase. J Mol Biol. 1991 May 20; 219(2):161-3.
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      192. Ghosh P, Stroud RM. Ion channels formed by a highly charged peptide. Biochemistry. 1991 Apr 9; 30(14):3551-7.
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      193. Miercke LJ, 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. 1991 Mar 26; 30(12):3088-98.
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      194. Shand RF, Miercke LJ, Mitra AK, Fong SK, Stroud RM, Betlach MC. Wild-type and mutant bacterioopsins D85N, D96N, and R82Q: high-level expression in Escherichia coli. Biochemistry. 1991 Mar 26; 30(12):3082-8.
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      195. 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. Photochem Photobiol. 1991 Mar; 53(3):341-6.
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      196. Milder SJ, Thorgeirsson TE, Miercke LJ, Stroud RM, Kliger DS. Effects of detergent environments on the photocycle of purified monomeric bacteriorhodopsin. Biochemistry. 1991 Feb 19; 30(7):1751-61.
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      197. Earnest T, Fauman E, Craik CS, Stroud R. 1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures. Proteins. 1991; 10(3):171-87.
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      198. Stroud RM, McCarthy MP, Shuster M. Nicotinic acetylcholine receptor superfamily of ligand-gated ion channels. Biochemistry. 1990 Dec 18; 29(50):11009-23.
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      199. Climie S, Ruiz-Perez L, Gonzalez-Pacanowska D, Prapunwattana P, Cho SW, Stroud R, Santi DV. Saturation site-directed mutagenesis of thymidylate synthase. J Biol Chem. 1990 Nov 5; 265(31):18776-9.
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      200. 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)trypsin. Biochemistry. 1990 Sep 11; 29(36):8351-7.
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      201. Hurley JH, Dean AM, Sohl JL, Koshland DE, Stroud RM. Regulation of an enzyme by phosphorylation at the active site. Science. 1990 Aug 31; 249(4972):1012-6.
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      202. 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. 1990 Jul 31; 29(30):6964-77.
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      203. Finer-Moore JS, Montfort WR, Stroud RM. Pairwise specificity and sequential binding in enzyme catalysis: thymidylate synthase. Biochemistry. 1990 Jul 31; 29(30):6977-86.
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      204. 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. J Biol Chem. 1990 Mar 5; 265(7):3599-602.
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      205. Mitra AK, Stroud RM. High sensitivity electron diffraction analysis. A study of divalent cation binding to purple membrane. Biophys J. 1990 Feb; 57(2):301-11.
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      206. Schiffer CA, Caldwell JW, Kollman PA, Stroud RM. Prediction of homologous protein structures based on conformational searches and energetics. Proteins. 1990; 8(1):30-43.
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      207. 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. 1990; 8(4):315-33.
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      208. Miercke LJ, Stroud RM, Dratz EA. Preparative purification of functional bacteriorhodopsin by high-performance size-exclusion chromatography. J Chromatogr. 1989 Dec 8; 483:331-40.
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      209. Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE, Stroud RM. Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proc Natl Acad Sci U S A. 1989 Nov; 86(22):8635-9.
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      210. Poulter L, Earnest JP, Stroud RM, Burlingame AL. Structure, oligosaccharide structures, and posttranslationally modified sites of the nicotinic acetylcholine receptor. Proc Natl Acad Sci U S A. 1989 Sep; 86(17):6645-9.
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      211. 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. J Cell Biol. 1989 Aug; 109(2):755-74.
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      212. McCarthy MP, Stroud RM. Changes in conformation upon agonist binding, and nonequivalent labeling, of the membrane-spanning regions of the nicotinic acetylcholine receptor subunits. J Biol Chem. 1989 Jun 25; 264(18):10911-6.
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      213. Miercke LJ, Ross PE, Stroud RM, Dratz EA. Purification of bacteriorhodopsin and characterization of mature and partially processed forms. J Biol Chem. 1989 May 5; 264(13):7531-5.
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      214. 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. 1989 Jan 10; 28(1):40-8.
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      215. 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. Biomed Environ Mass Spectrom. 1988 Oct; 16(1-12):25-30.
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      216. 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. Mol Cell Biol. 1988 Sep; 8(9):3797-808.
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      217. Basus VJ, Billeter M, Love RA, Stroud RM, Kuntz ID. Structural studies of alpha-bungarotoxin. 1. Sequence-specific 1H NMR resonance assignments. Biochemistry. 1988 Apr 19; 27(8):2763-71.
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      218. 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. 1987 Aug 21; 237(4817):905-9.
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      219. Vassarotti A, Stroud R, Douglas M. Independent mutations at the amino terminus of a protein act as surrogate signals for mitochondrial import. EMBO J. 1987 Mar; 6(3):705-11.
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      220. Hardy LW, Finer-Moore JS, Montfort WR, Jones MO, Santi DV, Stroud RM. Atomic structure of thymidylate synthase: target for rational drug design. Science. 1987 Jan 23; 235(4787):448-55.
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      221. Stroud RM. An archetypal molecular transducer of the nervous system: the acetylcholine receptor. Res Publ Assoc Res Nerv Ment Dis. 1987; 65:51-63.
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      222. Stroud RM. Topological mapping and the ionic channel in an acetylcholine receptor. Soc Gen Physiol Ser. 1987; 41:67-75.
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      223. Masters SB, Stroud RM, Bourne HR. Family of G protein alpha chains: amphipathic analysis and predicted structure of functional domains. Protein Eng. 1986 Oct-Nov; 1(1):47-54.
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      224. 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 Eng. 1986 Oct-Nov; 1(1):37-46.
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      225. Katre NV, Kimura Y, Stroud RM. Cation binding sites on the projected structure of bacteriorhodopsin. Biophys J. 1986 Aug; 50(2):277-84.
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      226. Fairclough RH, Miake-Lye RC, Stroud RM, Hodgson KO, Doniach S. Location of terbium binding sites on acetylcholine receptor-enriched membranes. J Mol Biol. 1986 Jun 20; 189(4):673-80.
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      227. Hershenson S, Helmers N, Desmueles P, Stroud R. Purification and crystallization of creatine kinase from rabbit skeletal muscle. J Biol Chem. 1986 Mar 15; 261(8):3732-6.
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      228. McCarthy MP, Earnest JP, Young EF, Choe S, Stroud RM. The molecular neurobiology of the acetylcholine receptor. Annu Rev Neurosci. 1986; 9:383-413.
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      229. Liscum L, Finer-Moore J, Stroud RM, Luskey KL, Brown MS, Goldstein JL. Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. J Biol Chem. 1985 Jan 10; 260(1):522-30.
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      230. 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. Proc Natl Acad Sci U S A. 1985 Jan; 82(2):626-30.
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      231. Stroud RM, Finer-Moore J. Acetylcholine receptor structure, function, and evolution. Annu Rev Cell Biol. 1985; 1:317-51.
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      232. Finer-Moore J, Stroud RM, Prescott B, Thomas GJ. Subunit secondary structure in filamentous viruses: predictions and observations. J Biomol Struct Dyn. 1984 Aug; 2(1):93-100.
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      233. Katre NV, Finer-Moore J, Stroud RM, Hayward SB. Location of an extrinsic label in the primary and tertiary structure of bacteriorhodopsin. Biophys J. 1984 Aug; 46(2):195-203.
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      234. Finer-Moore J, Stroud RM. Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor. Proc Natl Acad Sci U S A. 1984 Jan; 81(1):155-9.
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      235. Fairclough RH, Finer-Moore J, Love RA, Kristofferson D, Desmeules PJ, Stroud RM. Subunit organization and structure of an acetylcholine receptor. Cold Spring Harb Symp Quant Biol. 1983; 48 Pt 1:9-20.
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      236. Agard DA, Stroud RM. Linking regions between helices in bacteriorhodopsin revealed. Biophys J. 1982 Mar; 37(3):589-602.
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      237. Kistler J, Stroud RM, Klymkowsky MW, Lalancette RA, Fairclough RH. Structure and function of an acetylcholine receptor. Biophys J. 1982 Jan; 37(1):371-83.
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      238. Stroud RM, Serwer P, Ross MJ. Assembly of bacteriophage T7. Dimensions of the bacteriophage and its capsids. Biophys J. 1981 Dec; 36(3):743-57.
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      239. Hayward SB, Stroud RM. Projected structure of purple membrane determined to 3.7 A resolution by low temperature electron microscopy. J Mol Biol. 1981 Sep 25; 151(3):491-517.
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      240. Katre NV, Wolber PK, Stoeckenius W, Stroud RM. Attachment site(s) of retinal in bacteriorhodopsin. Proc Natl Acad Sci U S A. 1981 Jul; 78(7):4068-72.
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      241. Kistler J, Stroud RM. Crystalline arrays of membrane-bound acetylcholine receptor. Proc Natl Acad Sci U S A. 1981 Jun; 78(6):3678-82.
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      242. Nagasawa S, Stroud RM. Purification and characterization of a macromolecular weight cofactor for C3b-inactivator, C4bC3bINA-cofactor, of human plasma. Mol Immunol. 1980 Nov; 17(11):1365-72.
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      243. Klymkowsky MW, Heuser JE, Stroud RM. Protease effects on the structure of acetylcholine receptor membranes from Torpedo californica. J Cell Biol. 1980 Jun; 85(3):823-38.
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      244. Klymkowsky MW, Stroud RM. Immunospecific identification and three-dimensional structure of a membrane-bound acetylcholine receptor from Torpedo californica. J Mol Biol. 1979 Mar 5; 128(3):319-34.
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      245. Stroud RM, Agard DA. Structure determination of asymmetric membrane profiles using an iterative Fourier method. Biophys J. 1979 Mar; 25(3):495-512.
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      246. Ross MJ, Klymkowsky MW, Agard DA, Stroud RM. Structural studies of a membrane-bound acetylcholine receptor from Torpedo californica. J Mol Biol. 1977 Nov; 116(4):635-59.
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      247. Kossiakoff AA, Chambers JL, Kay LM, Stroud RM. Structure of bovine trypsinogen at 1.9 A resolution. Biochemistry. 1977 Feb 22; 16(4):654-64.
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      248. Stroud RM, Kossiakoff AA, Chambers JL. Mechanisms of zymogen activation. Annu Rev Biophys Bioeng. 1977; 6:177-93.
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      249. Krieger M, Koeppe RE, Stroud RM. pH dependence of tritium exchange with the C-2 protons of the histidines in bovine trypsin. Biochemistry. 1976 Aug 10; 15(16):3458-64.
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      250. 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. 1976 Aug 10; 15(16):3450-8.
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      251. Koeppe RE, Stroud RM. A pulsed diffusion technique for the growth of protein crystals for x-ray diffraction. J Mol Biol. 1975 Oct 15; 98(1):155-60.
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      252. Hurst MM, Volanakis JE, Hester RB, Stroud RM, Bennett JC. The structural basis for binding of complement by immunoglobulin M. J Exp Med. 1974 Oct 1; 140(4):1117-21.
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      253. Chambers JL, Christoph GG, Krieger M, Kay L, Stroud RM. Silver ion inhibition of serine proteases: crystallographic study of silver-trypsin. Biochem Biophys Res Commun. 1974 Jul 10; 59(1):70-4.
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      254. Krieger M, Kay LM, Stroud RM. Structure and specific binding of trypsin: comparison of inhibited derivatives and a model for substrate binding. J Mol Biol. 1974 Feb 25; 83(2):209-30.
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      255. 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. J Mol Biol. 1974 Feb 25; 83(2):185-208.
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      256. Stroud RM, Kay LM, Dickerson RE. The crystal and molecular structure of DIP-inhibited bovine trypsin at2.7Angstrom resolution. Cold Spring Harb Symp Quant Biol. 1972; 36:125-40.
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