A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic stud

A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic stud

Item
http://www.wikidata.org/entity/Q28362284
A theoretical study of the active sites of papain and S195C rat trypsin: implications for the low reactivity of mutant serine proteinasesOptimizing dentin bond durability: control of collagen degradation by matrix metalloproteinases and cysteine cathepsinsThe refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificitySupracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kineticsSubstrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bondingSpatial patterns of gene expression in Brassica napus seedlings: identification of a cortex-specific gene and localization of mRNAs encoding isocitrate lyase and a polypeptide homologous to proteinases.Endolysosomal proteolysis and its regulation.Cathepsin B fraction active at physiological pH of 7.5 is of prognostic significance in squamous cell carcinoma of human lungPreparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and aChemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sitDifferences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe stuA model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolyses.Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives.
P2860

A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic stud

Item
http://www.wikidata.org/entity/Q28362284
description
1985 nî lūn-bûn
@nan
1985 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
name
A general framework of cystein ...... 65 (cathepsin H). Kinetic stud
@nl
type
label
A general framework of cystein ...... 65 (cathepsin H). Kinetic stud
@nl
prefLabel
A general framework of cystein ...... 65 (cathepsin H). Kinetic stud
@nl
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P304
P31
P407
P433
P478
P577
P698
P932