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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.
Highly Cited
2009
Highly Cited
2009
Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation.
In our efforts to explore marine cyanobacteria as a source of novel bioactive compounds, we discovered a statine unit-containing… 
Highly Cited
2007
Highly Cited
2007
Cathepsin E prevents tumor growth and metastasis by catalyzing the proteolytic release of soluble TRAIL from tumor cell surface.
The aspartic proteinase cathepsin E is expressed predominantly in cells of the immune system and highly secreted by activated… 
Highly Cited
2007
Highly Cited
2007
Cathepsin E Deficiency Induces a Novel Form of Lysosomal Storage Disorder Showing the Accumulation of Lysosomal Membrane Sialoglycoproteins and the Elevation of Lysosomal pH in Macrophages*
Cathepsin E, an endolysosomal aspartic proteinase predominantly expressed in cells of the immune system, has an important role in… 
Highly Cited
1999
Highly Cited
1999
Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D.
Cathepsin E and cathepsin D are two major intracellular aspartic proteinases implicated in the physiological and pathological… 
Highly Cited
1998
Highly Cited
1998
Identification of Cellular Compartments Involved in Processing of Cathepsin E in Primary Cultures of Rat Microglia
Abstract: Cathepsin E is a major nonlysosomal, intracellular aspartic proteinase that localizes in various cellular compartments… 
Highly Cited
1992
Highly Cited
1992
Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E
Proteolytic degradation (processing) of antigen by antigen‐presenting cells is a major regulatory step in the activation of a T… 
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
1991
Highly Cited
1991
An immunocytochemical study on distinct intracellular localization of cathepsin E and cathepsin D in human gastric cells and various rat cells.
Immunocytochemical localization of two distinct intracellular aspartic proteinases, cathepsins E and D, in human gastric mucosal… 
1988
1988
Characteristic distribution of cathepsin E which immunologically cross-reacts with the 86-kDa acid proteinase from rat gastric mucosa.
The antiserum raised against the high-molecular-weight acid proteinase from rat gastric mucosa, termed 86-kDa acid proteinase… 
Highly Cited
1987
Highly Cited
1987
Slow moving proteinase. Isolation, characterization, and immunohistochemical localization in gastric mucosa.
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