The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B
about
Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitorsCysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probesDevelopment of calpain-specific inactivators by screening of positional scanning epoxide librariesThe identification of active forms of cysteine proteinases in Kirsten-virus-transformed mouse fibroblasts by use of a specific radiolabelled inhibitorThe use of benzyloxycarbonyl[125I]iodotyrosylalanyldiazomethane as a probe for active cysteine proteinases in human tissuesA catalytically active high-Mr form of human cathepsin B from sputumRecent developments in inhibiting cysteine and serine proteases.A cathepsin-like cysteine proteinase proaggregating activity in thrombotic thrombocytopenic purpura.Calpain 4 is not necessary for LFA-1-mediated function in CD4+ T cellsHuman cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase.The cysteine proteinase inhibitor Z-Phe-Ala-CHN2 alters cell morphology and cell division activity of Trypanosoma brucei bloodstream forms in vivo.Control of programmed cyclin destruction in a cell-free system.Proteolytic pathways of activation and degradation of a bacterial phospholipase C during intracellular infection by Listeria monocytogenes.Calpain regulates actin remodeling during cell spreading.Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulationInhibitors of cathepsins B and L induce autophagy and cell death in neuroblastoma cells.Calpain is a mediator of preservation-reperfusion injury in rat liver transplantationSpecific labeling of cysteine proteinases in pathogenic and nonpathogenic Entamoeba histolytica.Isolation of a Chinese hamster ovary cell clone possessing decreased mu-calpain content and a reduced proliferative growth rate.Biologically active monomeric and heterodimeric recombinant human calpain I produced using the baculovirus expression systemAmino acid substitutions in the N-terminal segment of cystatin C create selective protein inhibitors of lysosomal cysteine proteinases.Characterization of the active site of human multicatalytic proteinaseDesign, synthesis and biological evaluation of a library of thiocarbazates and their activity as cysteine protease inhibitors.Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit.The inactivation of the cysteinyl exopeptidases cathepsin H and C by affinity-labelling reagents.Comparative behaviour of calpain and cathepsin B toward peptidyl acyloxymethyl ketones, sulphonium methyl ketones and other potential inhibitors of cysteine proteinases.Investigation of the role of calpain as a stimulus-response mediator in human platelets using new synthetic inhibitorsReaction of proteasomes with peptidylchloromethanes and peptidyldiazomethanes.Lysosomal cysteine endopeptidases mediate interleukin 1-stimulated cartilage proteoglycan degradationDesign of a transferrin-proteinase inhibitor conjugate to probe for active cysteine proteinases in endosomes.Modulation of the in situ activity of tissue transglutaminase by calcium and GTP.Quantification of cathepsins B and L in cells.Affinity labelling of the Ca(2+)-activated neutral proteinase (calpain) in intact human platelets.Potent and selective inactivation of cysteine proteinases with N-peptidyl-O-acyl hydroxylamines.Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification.Interaction of aspartic acid-104 and proline-287 with the active site of m-calpain.Kinetics of inactivation of bovine pancreatic ribonuclease A by bromopyruvic acid.A Trypanosoma cruzi-secreted 80 kDa proteinase with specificity for human collagen types I and IV.In vitro embryotoxicity of the cysteine proteinase inhibitors benzyloxycarbonyl-phenylalanine-alanine-diazomethane (Z-Phe-Ala-CHN2) and benzyloxycarbonyl-phenylalanine-phenylalanine-diazomethane (Z-Phe-Phe-CHN2).Targeting calpain-mediated proteolysis and peptide signaling as a strategy to reduce injury in multiple sclerosis.
P2860
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P2860
The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B
description
1988 nî lūn-bûn
@nan
1988 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@ast
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@en
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@nl
type
label
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@ast
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@en
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@nl
prefLabel
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@ast
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@en
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@nl
P2093
P2860
P356
P1433
P1476
The design of peptidyldiazomet ...... I, cathepsin L and cathepsin B
@en
P2093
P2860
P356
10.1042/BJ2530751
P407
P577
1988-08-01T00:00:00Z