Design of potent selective zinc-mediated serine protease inhibitors (Q27748863)

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J M Clark

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J S Finer-Moore

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T E Jenkins

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C R Johnson

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M J Ross

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C Luong

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W R Moore

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R M Stroud

A family of protein-cutting proteins

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language of work or name

English

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publication date

5 February 1998

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published in

Nature

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volume

391

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issue

6667

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page(s)

608-12

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cites work

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Structural Biology of Zinc

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Structure and specific binding of trypsin: comparison of inhibited derivatives and a model for substrate binding

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Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface

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Hydrogen bond stereochemistry in protein structure and function

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Structural basis of substrate specificity in the serine proteases

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Suppression of respiratory syncytial virus infection in cotton rats by bis(5-amidino-2-benzimidazolyl)methane

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A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease

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Engineering an interfacial zinc site to increase hormone-receptor affinity

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The X-ray structure of a growth hormone-prolactin receptor complex

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X-ray structures of a designed binding site in trypsin show metal-dependent geometry

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Aromatic amidines. Comparison of their ability to block respiratory syncytial virus induced cell fusion and to inhibit plasmin, urokinase, thrombin, and trypsin

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Production of crystallizable human chymase from a Bacillus subtilis system

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Mast cell tryptase: a new target for therapeutic intervention in asthma

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Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

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In crystals of complexes of streptavidin with peptide ligands containing the HPQ sequence the pKa of the peptide histidine is less than 3.0

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector

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