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Cathepsin E

Known as: Cathepsin E [Chemical/Ingredient], Moving Proteinase, Slow, Slow Moving Proteinase 
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a… 
National Institutes of Health

Related topics

Related topics

11 relations

Broader (2)

Aspartic Acid EndopeptidasesCathepsins
CTSE geneIn BloodProcess of secretionantagonists & inhibitors

Narrower (1)

procathepsin E

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2006
2006
Cathepsin E-deficient mice show increased susceptibility to bacterial infection associated with the decreased expression of multiple cell surface Toll-like receptors.
Cathepsin E, an intracellular aspartic proteinase, is predominantly localized in the endosomal compartments of immune system… 
Highly Cited
2004
Highly Cited
2004
Cathepsin D, but not cathepsin E, degrades desmosomes during epidermal desquamation
Background  We previously reported that an ambient aspartic proteinase is crucial to desquamation of the stratum corneum at pH 5… 
1996
1996
Regulation of cathepsin E expression during human B cell differentiation in vitro
Cathepsin E is an aspartic proteinase which has been implicated in antigen processing in the class II major histocompatibility… 
1995
1995
Isolation and sequencing of two cDNA clones encoding rat spleen cathepsin E and analysis of the activation of purified procathepsin E.
Cathepsin E (CE) is an intracellular, nonlysosomal aspartic proteinase consisting of two identical subunits with a molecular mass… 
1995
1995
Specific immunocytochemical localization of cathepsin E at the ruffled border membrane of active osteoclasts
The immunocytochemical localization of cathepsin E, a non-lysosomal aspartic proteinase, was investigated in rat osteoclasts… 
1995
1995
Exploring the binding preferences/specificity in the active site of human cathepsin E
Aspartic proteinases are produced in the human body by a variety of cells. Some of these proteins, examples of which are pepsin… 
1993
1993
Rabbit procathepsin E and cathepsin E. Nucleotide sequence of cDNA, hydrolytic specificity for biologically active peptides and gene expression during development.
The structure of rabbit procathepsin E was determined by molecular cloning of its cDNA. The proenzyme consisted of 379 amino… 
Highly Cited
1992
Highly Cited
1992
Gastric procathepsin E and progastricsin from guinea pig. Purification, molecular cloning of cDNAs, and characterization of enzymatic properties, with special reference to procathepsin E.
Highly Cited
1987
Highly Cited
1987
Slow moving proteinase. Isolation, characterization, and immunohistochemical localization in gastric mucosa.
1986
1986
An aspartic proteinase from human erythrocytes is immunochemically indistinguishable from a non-pepsin, electrophoretically slow moving proteinase from gastric mucosa.
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