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Structural plasticity broadens the specificity of an engineered protease
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title
Structural plasticity broadens the specificity of an engineered protease
(English)
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author name string
R Bone
series ordinal
1
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J L Silen
series ordinal
2
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D A Agard
series ordinal
3
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language of work or name
English
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publication date
18 May 1989
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published in
Nature
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volume
339
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issue
6221
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page(s)
191-5
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cites work
Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering
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Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering
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A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework
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Redesigning trypsin: alteration of substrate specificity
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Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.
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Refined structure of alpha-lytic protease at 1.7 A resolution. Analysis of hydrogen bonding and solvent structure
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Molecular structure of the α-lytic protease from Myxobacter 495 at 2·8 Å resolution
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Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer
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Catalytic mechanism of serine proteases: reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease
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High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors.
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Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid
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On the size of the active site in proteases. I. Papain
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Active site of alpha-lytic protease: enzyme-substrate interactions
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Kinetic properties of the binding of alpha-lytic protease to peptide boronic acids
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The influence of the geometric properties of the active centre on the specificity of α‐chymotrypsin catalysis
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Active site mapping of the serine proteases human leukocyte elastase, cathepsin G, porcine pancreatic elastase, rat mast cell proteases I and II. Bovine chymotrypsin A alpha, and Staphylococcus aureus protease V-8 using tripeptide thiobenzyl ester s
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Analytical molecular surface calculation
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Solvent-accessible surfaces of proteins and nucleic acids
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Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity
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Cassette mutagenesis: an efficient method for generation of multiple mutations at defined sites
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Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases.
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17 The kinetics of reversible tight-binding inhibition
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Identifiers
DOI
10.1038/339191A0
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Dimensions Publication ID
1024065236
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PubMed publication ID
2716847
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ResearchGate publication ID
20439083
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