1968–1989

1989

Preparative purification of functional bacteriorhodopsin by high-performance size-exclusion chromatography.
Miercke, LJW; Stroud, RM; and Dratz, EA. (1989)
Journal of Chromatography 483, 331-340.
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Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
Hurley, JH; Thorsness, PE; Ramalingam, V; Helmers, NH; Koshland, DE; and Stroud, RM. (1989)
Proceedings of the National Academy of Sciences (USA) 86, 8635-9.
PDB Accession No. 3ICD
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Structure, oligosaccharide structures, and posttranslationally modified sites of the nicotinic acetylcholine receptor.
Poulter, L; Earnest, JP; Stroud, RM; and Burlingame, AL. (1989)
Proceedings of the National Academy of Sciences (USA) 86, 6645-6649.
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Three-dimensional structure of nicotinic acetylcholine receptor and location of the major associated 43-kD cytoskeletal protein, determined at 22 Å by low dose electron microscopy and x-ray diffraction to 12.5 Å
Mitra, AK; McCarthy, MP; Stroud, RM. (1989) 
Journal of Cell Biology 109, 755-774.
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Changes in conformation upon agonist binding, and nonequivalent labeling, of the membrane-spanning regions of the nicotinic acetylcholine receptor subunits.
McCarthy, MP; and Stroud RM. (1989)
Journal of Biological Chemistry 264, 10911-10916.
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Purification of bacteriorhodopsin and characterization of mature and partially processed forms.
Miercke, LJW; Ross, PE; Stroud, RM; and Dratz, EA. (1989)
Journal of Biological Chemistry 264, 7531-7535.
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Molecular biology of the acetylcholine receptor.
Stroud, RM; McCarthy, MP; Earnest, JP; Schuster, M; Ghosh, P;and Mitra, AR. (1989)
Fernstrom Series on Neuromuscular Junction,LC Sellin, R Libelius and S Thesleff, eds., Elsevier Science Publishers,The Netherlands, pp 209-216.
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Identification of membrane proteins and soluble protein secondary structural elements, domain structure, and packing arrangements by Fourier-transform amphipathic analysis.
Finer-Moore, J; Bazan, JF; Rubin, J; and Stroud, RM. (1989)
Prediction of Protein Structure and the Principles of Protein Conformation
G. Fasman, ed., Plenum Press, New York, pp 719-759.
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Conformational states of the nicotinic acetylcholine receptorfrom Torpedo californica induced by the binding of agonists, antagonists and local anaesthetics.  Equilibrium measurements using tritium-hydrogen exchange.
McCarthy, MP; and Stroud, RM. (1989)
Biochemistry 28, 40-48.

1988

Structural studies of α-bungarotoxin. 1. Sequence-specific 1H NMR resonance assignments.
Basus, VJ; Billeter, M; Love, RA; Stroud, RM; Kuntz, ID. (1988)
Biochemistry 27, 2763-2771.
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Cesium ion liquid secondary ion mass spectometry of membrane-bound glycoproteins:  Structural and topological considerations of acetylcholine receptor from Torpedo californica.
Poulter, L; Earnest, JP; Stroud, RM; Burlingame, AL. (1988)
Biomedical and Environmental Mass Spectometry 16, 25-30.
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A new strategy for mapping the topography of a transmembrane protein using mass spectometry.
Falick, AM; Mel, SF; Stroud, RM; Burlingame, AL. (1988)
Techniques in Protein Chemistry, Academic Press, pp 152-159.
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Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis.
Basson, ME; Thorsness, M; Finer-Moore, J; Stroud, RM; Kuntz, ID.(1988)
Molecular and Cellular Biology 8, 3797-3808.
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Terbium-calcium binding sites on the acetylcholine receptor.
Fairclough, RH; Stroud, RM; Miake-Lye, RC; Hodgson, KO; Doniach, S. (1988)
Myasthenia Gravis: Biology and Treatment (Annals of the New York Academy of Sciences 505, 752-755).
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1987

Independent mutations at the amino terminus of a protein act as surrogate signals for mitochondrial import.
Vassarotti, A; Stroud, RM; and Douglas, M. (1987)
EMBO Journal 6, 705-711.
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Atomic structure of thymidylate synthase: Target for rational drug design.
Hardy, LW; Finer-Moore, JS; Montfort, WR; Jones, MO; Santi, DV;and Stroud, RM. (1987)
Science 235, 448-455.
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The three-dimensional structure of Asn102 mutant of trypsin: Role of Asp102 in serine protease catalysis.
Sprange, S; Standing, T; Fletterick, RJ; Stroud, RM; Finer-Moore, J;
Xuong, NH; Hamlin, R; Rutter, WJ; and Craik, CS. (1987)
Science 237, 905-909.
PDB Accession Nos. 1TRM & 2TRM 
View PDB structure 1TRM, 2TRM
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An archetypal molecular transducer of the nervous system: The acetylcholine receptor.
Stroud, RM. (1987)
Molecular Neurobiology in Neurology and Psychiatry,
E Kandel, ed., Raven Press, New York 65, 51-63.
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Effects of the functional state of the acetylcholine receptoron reconstitution into lipid vesicles.
Earnest, JP; Stroud, RM; and McNamee, MG. (1987)
Membrane Proteins: Proceedings of the Membrane Protein Symposium, 
SC Goheen, ed., Bio-Rad Laboratories, Richmond, California, pp 117-130.

The acetylcholine receptor: What the three-dimensional structure tells us about ion conductance.
Stroud, RM; and Finer-Moore, J. (1987)
Biological Organization: Macromolecular Interactions at High Resolution, RM Burnett and HJ Vogel, eds., Academic Press Inc,  Orlando, pp 307-318.
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1986

Family of G protein α chains: amphipathic analysis and predicted structure of functional domains.
Masters, SB; Stroud, RM; and Bourne, HR. (1986)
Protein Engineering 1, 47-54.
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The crystal structure of a-bungarotoxin at 2.5 Å resolution: relation to solution structure and binding to acetylcholine receptor.
Love, RA; and Stroud, RM. (1986)
Protein Engineering 1, 37-46.
PDB Accession No. 2ABX
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Lack of the transition state stabilization site is a factor in the inactivity of trypsinogen, a serine protease zymogen. Structure of /Dfp inhibited bovine trypsinogen at 2.1 Å resolution.
Jones, MO; and Stroud, RM.  (1986)
Not published
PDB Accession No. 2TGD
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Evidence for conformational differences in aqueous and crystalline structures of a-bungarotoxin and cobratoxin. Thomas, GJ Jr; Prescott, B; Love, R; and Stroud, RM. (1986)
Spectrochimica Acta 42A, 215-222.
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Cation binding sites on the projected structure of bacteriorhodopsin.
Katre, NV; Kimura, Y; and Stroud, RM. (1986)
Biophysical Journal 50, 277-284.
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Topological mapping and the ionic channel in an acetylcholine receptor.
Stroud, RM. (1986)
Proteins of Excitable Membranes, B Hille and D Fambrough, eds.,
Society of General Physiologists Series Vol 41, pp 67-75.
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Purification and crystallization of creatine kinase from rabbit skeletal muscle.
Hershenson, S; Helmers, N; Desmueles, P; and Stroud, RM. (1986)
Journal of Biological Chemistry261, 3732-3736.
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The molecular neurobiology of the acetylcholine receptor.
McCarthy, MP; Earnest, JP; Young, EF; Choe, S; Stroud, RM. (1986)
Annual Review of Neuroscience 9, 383-413.
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Location of terbium binding sites on acetylcholine receptor-enriched membranes.
Fairclough, RH; Miake-Lye, RC; Stroud, RM; Hodgson, KO;and Doniach, S. (1986)
Journal of Molecular Biology 189, 673-680.
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1980–1985

Acetylcholine receptor structure, function, and evolution.
Stroud, RM; and Finer-Moore, J. (1985)
Annual Review of Cell Biology 1, 317-351.
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Topological mapping of acetylcholine receptor: Evidence fora model with five transmembrane segments and a cytoplasmic COOH-terminal peptide.
Young, EF; Ralston, E; Blake, J; Ramachandran, J; Hall, ZW; and Stroud, RM. (1985)
Proc. National Academy of Sciences USA 82, 626-630.
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Domain structure of 3-Hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum.
Liscum, L; Finer-Moore, J; Stroud, RM; Luskey, KL; Brown, MS; and Goldstein, JL. (1985)
Journal of Biological Chemistry 260, 522-530.
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Location of an extrinsic label in the primary and tertiary structure of bacteriorhodopsin.
Katre, NV; Finer-Moore, J; Stroud, RM; Hayward, SB. (1984)
Biophysical Journal 46, 195-203.
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Subunit secondary structure in filamentous viruses: Predictions and observations.
Finer-Moore, J; Stroud, RM; Prescott, B; and Thomas, GJ, Jr. (1984)
Journal of Biomolecular Structure and Dynamics 2, 93-100.
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Acetylcholine receptor structure and function.
Stroud, RM. (1984)
Biological Membranes  5 (6),221-239, D Chapman, ed.,
Academic Press Inc. (London) Ltd, London.
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Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor.
Finer-Moore, J; and Stroud, RM. (1984)
Proc. National Academy of Sciences USA 81, 155-159.
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Acetylcholine receptor structure.
Stroud, RM. (1983)
Neuroscience Commentaries 1, 124-138.
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Subunit organization and structure of an acetylcholine receptor.
Fairclough, RH; Finer-Moore, J; Love, RA; Kristofferson, D; Desmueles, PJ; and Stroud, RM. (1983)
Cold Spring Harbor Symposia on Quantitative Biology 48, 9-20.
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The structure of acetylcholine receptor and of bacteriorhodopsin.
Stroud, RM. (1983)
Frontiers in Biochemical and Biophysical Studies of Proteinsand Membranes,
TY Liu, et al, eds., Elsevier Science Publishing Co. Inc, New York, pp 331-349.

Structure-function studies on human alpha interferon.
Wetzel, R; Levine, HL; Estell, DA; Shire, S; Finer-Moore, J; Stroud, RM; and Bewley, TA. (1982)
Interferons,  Academic Press, New York, NY, pp 365-376.

Linking regions between helices in bacteriorhodopsin revealed. Agard, DA; and Stroud, RM. (1982)
Biophysical Journal 37, 589-602.
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α-bungarotoxin structure revealed by a rapid method for averaging electron density of non-crystallographically, translationally related molecules.
Agard, DA; and Stroud, RM. (1982)
Acta Crystallographica A38, 186-194.
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Structure and function of an acetylcholine receptor.
Kistler, J; Stroud, RM; Klymkowsky, MW; Lalancette, RA; and Fairclough, RH. (1982)
Biophysical Journal 37, 371-383.
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A probable linking sequence between two transmembrane components of bacteriorhodopsin.
Katre, NV; Stroud, RM. (1981)
FEBS Letters 136, 170-174.

Structure of an acetylcholine receptor, a hypothesis for a dynamic mechanism of its action. Stroud, RM. (1981) Biomolecular Stereodynamics 1, 55-73, RH Sarma, ed., Adenine Press,New York.  (Proceedings of the Second SUNYA Conversation in the Discipline Biomolecular Stereodynamics, Vol. II.)
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Assembly of bacteriophage T7: Dimensions of the bacteriophage and its capsids.
Stroud, RM; Serwer, P; Ross, MJ. (1981)
Biophysical Journal 36, 743-757.
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Projected structure of purple membrane determined to 3.7 Å resolution by low temperature electron microscopy.
Hayward, SB; Stroud, RM. (1981)
J. Molecular Biology 151, 491-517.
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Quantitative analyses of electrophoretograms: A mathematical approach to super-resolution.
Agard, DA; Steinberg, RA; Stroud, RM. (1981)
Analytical Biochemistry 111, 257-268.
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Attachment site(s) of retinal in bacteriorhodopsin.
Katre, NV; Wolber, PK; Stoeckenius, W; Stroud, RM. (1981)
Proc. National Academy of Sciences USA 78, 4068-4072.
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Crystalline arrays of membrane-bound acetylcholine receptor.
Kistler, J; Stroud, RM. (1981)
Proc. National Academy of Sciences USA 78, 3678-3682.
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The binding and processing of plasminogen by Balb/c 3T3 and SV3T3 cells.
Tobler, J; Krieger, M; Stroud, RM. (1981)
Journal of Cellular Physiology 108, 277-290
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Protease effects on the structure of acetylcholine receptor membranes from Torpedo californica.
Klymkowsky, MW; Heuser, JE; Stroud, RM. (1980)
Journal of Cell Biology 85, 823-838. 
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1973–1979

Immunospecific identification and three-dimensional structure ofa membrane-bound acetylcholine receptor from Torpedo californica.
Klymkowsky, MW; Stroud, RM. (1979) 
Journal of Molecular Biology 128, 319-334.
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The accuracy of refined protein structures: Comparison of two independently refined models of bovine trypsin.
Chambers, JL; Stroud, RM. (1979)
Acta Crystallographica B35,1861-8174.
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Structure determination of asymmetric membrane profiles using an iterative Fourier method.
Stroud, RM; Agard, DA. (1979)
Biophysical Journal 25, 495-512.
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Preliminary crystallization and x-ray diffraction studies of human thrombin.
McKay, DB; Kay, LM; Stroud, RM. (1977)
Chemistry and Biology of Thrombin, RL Lundblad, JW Fenton II, and KG Mann eds., pp 113-121, Ann Arbor Science Publishers Inc, Ann Arbor, Michigan.
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Mechanisms of zymogen activation.
Stroud, RM; Kossiakoff, AA; Chambers, JL. (1977)
Annual Review of Biophysics and Bioengineering 6, 177-193.
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Structural studies of a membrane-bound acetylcholine receptor from Torpedo californica.
Ross, MJ; Klymkowsky, MW; Agard, DA; Stroud, RM. (1977)
J. Molecular Biology 116, 635-659.
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Error analysis in the biophysical applications of a flatbed autodensitometer.
Ross, MJ; Stroud, RM. (1977)
Acta Crystallographica A33, 500-508.
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Difference Fourier refinement of the structure of DIP-trypsinat 1.5 Å with a minicomputer technique.
Chambers, JL; Stroud, RM. (1977)
Acta Crystallographica B33, 1824-1837.
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Structure of bovine trypsinogen at 1.9 Å resolution.
Kossiakoff, AA; Chambers, JL; Kay, LM; Stroud, RM. (1977)
Biochemistry 16, 654-664.
PDB Accession No. 1TGN
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The effect of pre-incubation on trypsin kinetics at low pH.
Koeppe, RE II; Krieger, M; Stroud, RM. (1977)
Biochimica et Biophysica Acta 481, 617-621.
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A focusing monochromator for small-angle diffraction studies with synchrotron radiation.
Webb, NG; Samson, S; Stroud, RM; Gamble, RC; Baldeschwieler, JD. (1977)
Journal of Applied Crystallography 10, 104-110.
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Remotely controlled mirror of variable geometry for small-angle x-ray diffraction with synchrotron radiation.
Webb, NG; Samson, S; Stroud, RM; Gamble, RC; Baldeschwieler, JD. (1976)
Rev. Sci. Instrum. 47, 836-839.
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Data collection in protein crystallography: Experimental methods for reducing background radiation.
Krieger, M; Stroud, RM. (1976)
Acta Crystallographica A32, 653-656.
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pH dependence of tritium exchange with the C-2 protons of the histidines in bovine trypsin.
Krieger, M; Koeppe, RE II; Stroud, RM. (1976)
Biochemistry 15, 3458-3464.
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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.
Koeppe, RE II; Stroud, RM. (1976)
Biochemistry 15, 3450-3458.
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A pulsed diffusion technique for the growth of protein crystals for x-ray diffraction.
Koeppe, RE II; Stroud, RM; Pena, VA; Santi, DV.  (1975)
Journal of Molecular Biology 98, 155-160.
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Structural and functional studies of an acetylcholine receptor.
Raftery, MA; Bode, J; Vandlen, R; Michaelson, D; Deutsch, J; Moody, T;Ross, MJ; Stroud, RM. (1975)
Protein-Ligand Interactions, pp. 328-355, Walter de Gruyter & Co,
Berlin, Germany.
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Structure-function relationships in the serine proteases.
Stroud, RM; Krieger, M; Koeppe, RE, II; Kossiakoff, AA; Chambers, JL. (1975)
Cold Spring Harbor Symposium on Proteases and Biological Control,
Proteases and Biological Control, pp 13-32, Cold Spring Harbor Laboratory.
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Data collection in protein crystallography: Capillary effects and background corrections.
Krieger, M; Chambers, JL; Christoph, GG; Stroud, RM; Trus, BL. (1974)
Acta Crystallographica A30, 740-748.
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A family of protein-cutting proteins.
Stroud, RM. (1974)
Scientific American 231, 74-88.
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Molecular properties of Torpedo californica acetylcholine receptors.
Raftery, MA; Bode, J; Vandlen, R; Michaelson, D; Deutsch, J; Moody, T; Ross, MJ; Stroud, RM. (1974)
FEBS Proceedings 9, 9.

Silver ion inhibition of serine proteases: Crystallographic study of silver-trypsin.
Chambers, JL; Christoph, GG; Krieger, M; Kay, L; Stroud, RM. (1974)
Biochemical and Biophysical Research Communications 59, 70-74.
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Structure and specific binding of trypsin: Comparison of inhibited derivatives and a model for substrate binding.
Krieger, M; Kay, LM; Stroud, RM. (1974)
Journal of Molecular Biology 83, 209-230.
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The structure of bovine trypsin: Electron density maps of the inhibited enzyme at 5Å and at 2.7Å resolution.
Stroud, RM; Kay, LM; Dickerson, RE. (1974)
Journal of Molecular Biology 83, 185-208.
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The high resolution structure of trypsin.
Stroud, RM. (1973)
Stockholm Symposium on Structure of Biological Molecules.

The crystal and molecular structure of tubercidin, C₁₁H₁₄N₄O₄.
Stroud, RM. (1973)
Acta Crystallographica B29, 690-696.
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1968–1972

A single-crystal structure determination of DL-6-Thioctic acid, C₈H₁₄O₂S₂.
Stroud, RM; Carlisle, CH. (1972)
Acta Crystallographica B28, 304-307.
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The crystal and molecular structure of DIP-inhibited bovine trypsin at 2.7Å resolution.
Stroud, RM; Kay, LM; Dickerson, RE. (1971)
Cold Spring Harbor Symposia on Quantitative Biology 36, 125-140.
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The crystal structure of DIP-trypsin at 2.7Å resolution.
Stroud, RM; Kay, L; Stanford, RH; Battfay, O; Corey, RB;
Dickerson, RE. (1969)
Acta Crystallographica A25, S182.
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An optical illusion.
MacKay, AL; Stroud, RM. (1968)
Journal of Perception and Psychophysics 4, 90.
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