Trypsin

Design of potent selective zinc-mediated serine protease inhibitors.
Katz, BA; Clark, JM; Finer-Moore, JS; Jenkins, TE; Johnson, CR; Ross, MJ; Luong, C; Moore, WR; Stroud, RM. (1998)
Nature 391, 608-612.
PDB Accession Nos.: 1XUF, 1XUG, 1XUH, 1XUI, 1XUJ , 1XUK.
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View PDB structure 1XUF, 1XUG, 1XUH, 1XUI, 1XUJ, 1XUK

Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface.
Katz, BA; Finer-Moore, J; Mortezaei, R; Rich, DH; Stroud, RM. (1995)
Biochemistry 34, 8264-8280.
PDB Accession Numbers: 1BTX, 1BTW, 1BTY, and 1BTZ.
View PDB structure 1BTX, 1BTW, 1BTY 1BTZ
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Solvent structure in crystals of trypsin determined by x-ray and neutron diffraction.
Finer-Moore, JS; Kossiakoff, AA; Hurley, JH; Earnest, T; Stroud, RM. (1992)
Proteins 12, 203-222.
PDB Accession No. 5PTP
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1.59 Å structure of trypsin at 120 K: comparison of low temperature and room temperature structures.
Earnest, T; Fauman, E; Craik, CS; Stroud, R. (1991)
Proteins 10, 171-187.
PDB Accession No. 1DPO
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Structure of an acyl-enzyme intermediate during catalysis: (guanidinobenzoyl) trypsin.
Mangel, WF; Singer, PT; Cyr, DM; Umland, TC; Toledo, DL; Stroud, RM; Pflugrath, JW; Sweet, RM. (1990)
Biochemistry 29, 8351-8357.
PDB Accession No. 1GBT
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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; Craik, CS. (1987)
Science 237, 905-909.
PDB Accession Nos. 1TRM , 2TRM
View PDB structure 1TRM, 2TRM
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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; Stroud, RM. (1986)
Not published
PDB Accession No. 2TGD
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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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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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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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Difference Fourier refinement of the structure of DIP-trypsin at 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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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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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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A family of protein-cutting proteins.
Stroud, RM. (1974)
Scientific American 231, 74-88.
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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)
J. 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)
J. 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 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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