Cathepsin H: Molecular characteristics and clues to function and mechanism
Y Wang, J Zhao, Y Gu, H Wang, M Jiang, S Zhao… - Biochemical …, 2023 - Elsevier
Cathepsin H (CatH) is a lysosomal cysteine protease with a unique aminopeptidase activity
that is extensively expressed in the lung, pancreas, thymus, kidney, liver, skin, and brain …
that is extensively expressed in the lung, pancreas, thymus, kidney, liver, skin, and brain …
Theearly andlate processing of lysosomal enzymes: Proteolysis and compartmentation
A Hasilik - Experientia, 1992 - Springer
Lysosomal enzymes are subjected to a number of modifications including carbohydrate
restructuring and proteolytic maturation. Some of these reactions support lysosomal …
restructuring and proteolytic maturation. Some of these reactions support lysosomal …
[图书][B] Enzyme handbook
D Schomburg, M Salzmann, D Schomburg… - 1991 - Springer
Enzyme Handbook | SpringerLink Skip to main content Advertisement SpringerLink Account
Menu Find a journal Publish with us Track your research Search Cart Book cover Enzyme …
Menu Find a journal Publish with us Track your research Search Cart Book cover Enzyme …
[PDF][PDF] Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H …
G Guncar, M Podobnik, J Pungercar, B Strukelj, V Turk… - Structure, 1998 - academia.edu
Background: Cathepsin H is a lysosomal cysteine protease, involved in intracellular protein
degradation. It is the only known mono-aminopeptidase in the papain-like family and is …
degradation. It is the only known mono-aminopeptidase in the papain-like family and is …
[HTML][HTML] Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location
We have identified and characterized a novel human cysteine proteinase of the papain
family. A full-length cDNA for this enzyme was cloned from a human brain cDNA library …
family. A full-length cDNA for this enzyme was cloned from a human brain cDNA library …
[HTML][HTML] Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide …
A cDNA encoding a new cysteine proteinase belonging to the papain family and called
cathepsin F has been cloned from a human prostate cDNA library. This cDNA encodes a …
cathepsin F has been cloned from a human prostate cDNA library. This cDNA encodes a …
Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in human tissues.
G Velasco, AA Ferrando, XS Puente… - Journal of Biological …, 1994 - ASBMB
A cDNA encoding a novel member of the cysteine proteinase family of proteins has been
cloned from a human breast carcinoma cDNA library, by using a polymerase chain reaction …
cloned from a human breast carcinoma cDNA library, by using a polymerase chain reaction …
In vitro processing of aleurain, a barley vacuolar thiol protease.
BC Holwerda, NJ Galvin, TJ Baranski… - The Plant Cell, 1990 - academic.oup.com
Aleurain, originally described from its cDNA as a thiol protease [Rogers, JC, Dean, D., and
Heck, GR (1985). Proc. Natl. Acad. Sci. USA 82, 6512-6516], is characterized here as a …
Heck, GR (1985). Proc. Natl. Acad. Sci. USA 82, 6512-6516], is characterized here as a …
Molecular cloning and sequence analysis of human preprocathepsin C
A Pariš, B Štrukelj, J Pungerčar, M Renko, I Dolenc… - FEBS letters, 1995 - Elsevier
A cDNA clone (C1) coding for human preprocathepsin C was isolated from a human ileum
cDNA library using a rat kidney-derived RT-PCR probe and its complete nucleotide …
cDNA library using a rat kidney-derived RT-PCR probe and its complete nucleotide …
Purification and characterization of aleurain: a plant thiol protease functionally homologous to mammalian cathepsin H
BC Holwerda, JC Rogers - Plant physiology, 1992 - academic.oup.com
Barley (Hordeum vulgare L. cv Himilaya) aleurain is a vacuolar thiol protease originally
isolated as a cDNA with 65% derived amino acid sequence identity with cathepsin H (JC …
isolated as a cDNA with 65% derived amino acid sequence identity with cathepsin H (JC …