Results 211 to 220 of about 60,305 (241)
Cathepsin K Alleviates Liver Fibrosis by Inhibiting the TGF-β/Smad Signaling Pathway and Inducing Hepatic Stellate Cell Apoptosis. [PDF]
J Clin Transl HepatolLin Z +11 more
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Structural Differences Between Rabbit Cathepsin E and Cathepsin D
Biological Chemistry Hoppe-Seyler, 1986Rabbit cathepsins D and E were isolated from bone marrow. Both enzymes were purified by affinity chromatography on pepstatin-Sepharose 4B and Con A-Sepharose 4B. Purity of the enzymes was ascertained by two-dimensional gel electrophoresis after iodination. The isoelectric point of cathepsin D was found to be 6.95.
C, Lapresle +4 more
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Biochemical and Biophysical Research Communications, 2008
Cathepsin E is a major intracellular aspartic protease which is predominantly present in the cells of immune system and is frequently implicated in antigen processing via the MHC class II pathway. In the present review some of the known features of cathepsin E such as tissue distribution, subcellular localization, enzymatic properties, intracellular ...
Nousheen, Zaidi, Hubert, Kalbacher
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Cathepsin E is a major intracellular aspartic protease which is predominantly present in the cells of immune system and is frequently implicated in antigen processing via the MHC class II pathway. In the present review some of the known features of cathepsin E such as tissue distribution, subcellular localization, enzymatic properties, intracellular ...
Nousheen, Zaidi, Hubert, Kalbacher
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Emerging functional roles of cathepsin E
Biochemical and Biophysical Research Communications, 2008Cathepsin E is an intracellular aspartic protease of the endolysosomal pathway. It has been implicated in several physiological and pathological processes however, its exact functional role is yet to be elucidated. The present review gives an account of the major physiological functions that are associated to cathepsin E by various research groups and ...
Nousheen, Zaidi +3 more
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1995
Cathepsin E is a non-lysosomal, non-secretory, intracellular aspartic proteinase. Its cellular distribution is variable between species but includes the stomach, spleen, red and white blood cells and the skin. The physiological role of this enzyme is unclear, but it has been implicated in a number of vital processes.
J, Hill, D, Montgomery, J, Kay
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Cathepsin E is a non-lysosomal, non-secretory, intracellular aspartic proteinase. Its cellular distribution is variable between species but includes the stomach, spleen, red and white blood cells and the skin. The physiological role of this enzyme is unclear, but it has been implicated in a number of vital processes.
J, Hill, D, Montgomery, J, Kay
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Cathepsin D, but not cathepsin E, degrades desmosomes during epidermal desquamation
British Journal of Dermatology, 2004We previously reported that an ambient aspartic proteinase is crucial to desquamation of the stratum corneum at pH 5. Identification of this aspartic proteinase by using enzyme inhibitors suggested it to be cathepsin D, although we could not exclude cathepsin E.To determine the identity of this aspartic proteinase and its distribution within the ...
S, Igarashi +10 more
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Archives of Biochemistry and Biophysics, 1987
An extract of rat neutrophils was found to contain a high hemoglobin-hydrolyzing activity at pH 3.2, about 70% of which does not cross-react with anti-rat liver cathepsin D antibody. A neutrophil non-cathepsin D acid proteinase was successfully isolated from cathepsin D and characterized in comparison with the properties of rat liver cathepsin D.
S, Yonezawa, T, Tanaka, T, Miyauchi
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An extract of rat neutrophils was found to contain a high hemoglobin-hydrolyzing activity at pH 3.2, about 70% of which does not cross-react with anti-rat liver cathepsin D antibody. A neutrophil non-cathepsin D acid proteinase was successfully isolated from cathepsin D and characterized in comparison with the properties of rat liver cathepsin D.
S, Yonezawa, T, Tanaka, T, Miyauchi
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Grassystatin-derived peptides selectively inhibit cathepsin E and have low affinity to cathepsin D
Biochemical and Biophysical Research Communications, 2020Aspartic proteases are important biomarkers of human disease and interesting targets for modulation of immune response via MHC class II antigen processing inhibition. The lack of inhibitors with sufficient selectivity hampers precise analysis of the role of cathepsin E and napsin A in samples containing the ubiquitous and highly abundant homolog ...
Sophie Stotz +3 more
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1999
Aspartic proteinases are produced by a number of cells and tissues. These enzymes share a high degree of similarity which involves primary structures, and most of them are active predominantly in the acidic pH range. Eukaryotic aspartic proteinases (i.e.
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Aspartic proteinases are produced by a number of cells and tissues. These enzymes share a high degree of similarity which involves primary structures, and most of them are active predominantly in the acidic pH range. Eukaryotic aspartic proteinases (i.e.
openaire +1 more source