Supplemental material
Journal of Enzyme Inhibition and Medicinal Chemistry
Volume 33, 2018 - Issue 1
Related Research Data
C1A cysteine-proteases and their inhibitors in plants.
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(:unav)
Molecular cloning and anti-invasive activity of cathepsin L propeptide-like protein from Calotropis procera R. Br. against cancer cells
Source:
Taylor & Francis
Drosophila CTLA-2-like protein (D/CTLA-2) inhibits cysteine proteinase 1 (CP1), a cathepsin L-like enzyme.
Source:
Zoological Society of Japan
Tight-binding inhibitors—I: Kinetic behavior☆
Source:
Elsevier BV
Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides.
Source:
American Chemical Society (ACS)
Cysteine cathepsins in human cancer.
Source:
Walter de Gruyter GmbH
Cysteine cathepsins and the cutting edge of cancer invasion.
Source:
Informa UK Limited
Purification of a novel cysteine protease, procerain B, from Calotropis procera with distinct characteristics compared to procerain
Source:
Elsevier BV
On the size of the active site in proteases. I. Papain.
Source:
Elsevier BV
Phytocystatin Purification
Source:
Wiley
Propeptide inhibition of cathepsins K, L and S
Source:
Wiley
Purification and characterization of a cystatin from the leaves of methyl jasmonate treated tomato plants.
Source:
Elsevier BV
Functions of Propeptide Parts in Cysteine Proteases
Source:
Bentham Science Publishers Ltd.
Distinct roles for cysteine cathepsin genes in multistage tumorigenesis
Source:
Cold Spring Harbor Laboratory
Bombyx cysteine proteinase inhibitor (BCPI) homologous to propeptide regions of cysteine proteinases is a strong, selective inhibitor of cathepsin L-like cysteine proteinases.
Source:
Oxford University Press (OUP)
Mechanistic studies on the inhibition of thermolysin by a peptide hydroxamic acid
Source:
American Chemical Society (ACS)
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