Kinetic characterization and molecular docking of a novel, potent, and selective slow-binding inhibitor of human cathepsin L (scientific article)

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Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein

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Cysteine protease inhibition by azapeptide esters

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A detailed comparison of current docking and scoring methods on systems of pharmaceutical relevance

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Azapeptides as inhibitors and active site titrants for cysteine proteinases.

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Triggering of apoptosis by cathepsins

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Cysteine Proteases and Their Inhibitors

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From good substrates to good inhibitors: design of inhibitors for serine and thiol proteases

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Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo

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P433

issue

P304

page(s)

34-41

P577

publication date

2008-04-10

P1433

published in

Molecular Pharmacology

Q1943386

P1476

title

Kinetic characterization and molecular docking of a novel, potent, and selective slow-binding inhibitor of human cathepsin L

P478

volume

Reverse relations

cites work (P2860)

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