Crystal structure of porcine cathepsin H determined at 2.1 å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
- 1 January 1998
- Vol. 6 (1) , 51-61
- https://doi.org/10.1016/s0969-2126(98)00007-0
Abstract
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This publication has 68 references indexed in Scilit:
- EMERGING ROLES FOR CYSTEINE PROTEASES IN HUMAN BIOLOGYAnnual Review of Physiology, 1997
- Enzyme-linked immunosorbent assay for the detection of total cathepsin H in human tissue cytosols and seraJournal of Immunological Methods, 1997
- IFN-γ increases cathepsin H mRNA levels in mouse macrophagesJournal of Leukocyte Biology, 1995
- Protein catabolism in fibroblasts cultured from patients with mucolipidosis II and other lysosomal disordersBiochemical Journal, 1993
- Characterization of a cathepsin‐H‐like enzyme from a human melanoma cell lineInternational Journal of Cancer, 1991
- Gene structure of rat cathepsin HFEBS Letters, 1989
- Amino acid sequences of the human kidney cathepsins H and LFEBS Letters, 1988
- INTRACELLULAR PROTEASESAnnual Review of Biochemistry, 1987
- Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogensPublished by Walter de Gruyter GmbH ,1986
- Homology of amino acid sequences of rat liver cathepsins B and H with that of papain.Proceedings of the National Academy of Sciences, 1983