Results 81 to 90 of about 623 (108)
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Anti-Cathepsin L Monoclonal Antibodies That Distinguish Cathepsin L from Cathepsin V

Biological Chemistry, 2001
Cathepsin L is a lysosomal cysteine protease involved in intracellular protein degradation. Recently, several new cysteine proteases have been identified. Human cathepsin V, a thymus- and testis-specific human cysteine protease, shares 78% sequence identity with human cathepsin L.
Darja Barlič-Maganja   +4 more
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Cathepsin S inhibitors

Expert Opinion on Therapeutic Patents, 2004
Cysteine proteases have attracted considerable interest over the past decade. Lysosomal cysteine protease cathepsin S plays an important role in antigen presentation and matrix degradation. Interest for this enzyme has recently grown and ~ 70 patents have appeared over the last 3 years, targeting cathepsin S either solely or among other related ...
Sukanthini Thurairatnam, Vincent Leroy
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Cathepsin B in osteoblasts

Biochimica et Biophysica Acta (BBA) - General Subjects, 2003
Active cathepsin B has been found in cell extract and medium of human osteoblast-like cells and MG-63 cells. The released form is stable at neutral and alkaline pH and, in both cell types, intracellular and extracellular cathepsin B activities are increased by interleukin-1 beta (IL-1beta) and parathyroid hormone (PTH).
Aisa M. C.   +3 more
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CATHEPSIN B, CATHEPSIN C AND ARYLAMIDASE IN RABBIT CORNEA

Acta Ophthalmologica, 1982
The 3 peptide hydrolases cathepsin B, cathepsin C and arylamidase have been assayed in rabbit cornea with the use of fluorigenic derivatives of β‐naphthylamine. The optimal reaction conditions and kinetic properties are described. The assay procedures which are simple and very sensitive can be used for studying the release of these enzymes from corneal
Kirsti Schive, G. Volden
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Cathepsin L in glioma progression: Comparison with cathepsin B

Cancer Detection and Prevention, 2005
Lysosomal cysteine cathepsins have been implicated in tumor progression. This study is aimed to reveal differential expression and compare the prognostic significance of cathepsins B and L in glioma patients.The histological slides of 82 patients with primary astrocytic tumors were reviewed.
Tadej Strojnik   +3 more
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Human Cathepsins F and W: A New Subgroup of Cathepsins

Biochemical and Biophysical Research Communications, 1999
Human cathepsin F is a recently described papain-like cysteine protease of unknown function. To investigate the evolutionary relatedness to other human cathepsins, we determined the genomic organization and the chromosomal localization of cathepsin F and isolated its putative promoter region.
H. Wex   +3 more
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Cathepsin E and cathepsin D

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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Cathepsin-regulated apoptosis

Apoptosis, 2006
Apoptosis can be mediated by different mechanisms. There is growing evidence that different proteolytic enzymes are involved in the regulation of apoptosis. Cathepsins are proteases which, under physiologic conditions, are localized intralysosomally.
Tobias Welte   +2 more
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Crystallization of cathepsin D

Biochemical and Biophysical Research Communications, 1976
Summary Cathepsin D from chicken liver purified to apparent homogeneity by the method of affinity chromatography on pepstatin-Sepharose, was crystallized, upn gradual precipitation with ethanol, from 1.5% protein solution in slightly acid media corresponding to the isoelectric point of the enzyme.
O.V. Kazakova, V.N. Orokhovich
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Cathepsin X

2013
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 800 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
Nägler, Dorit K.   +2 more
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