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Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancerInteraction of recombinant human cystatin C with the cysteine proteinases papain and actinidinRole of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinasesHigh-molecular-weight kininogen binds two molecules of cysteine proteinases with different rate constantsHydrophobic sequences can substitute for the wild-type N-terminal sequence of cystatin A (stefin A) in tight binding to cysteine proteinases selection of high-affinity N-terminal region variants by phage display.Biochemistry and clinical role of human cystatin C.The N-terminal region of cystatin A (stefin A) binds to papain subsequent to the two hairpin loops of the inhibitor. Demonstration of two-step binding by rapid-kinetic studies of cystatin A labeled at the N-terminus with a fluorescent reporter groupThe proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain.Decreased affinity of recombinant antithrombin for heparin due to increased glycosylation.Structural and functional studies on a variant of cystatin purified from brain of Capra hircus.Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes.Evidence by chemical modification that tryptophan-104 of the cysteine-proteinase inhibitor chicken cystatin is located in or near the proteinase-binding site.Papain labelled with fluorescent thiol-specific reagents as a probe for characterization of interactions between cysteine proteinases and their protein inhibitors by competitive titrations.Interaction of chicken cystatin with inactivated papains.Kinetics of the interaction of chymotrypsin with eglin cLocal pH-dependent conformational changes leading to proteolytic susceptibility of cystatin C.Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases.Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases.Characterization by rapid-kinetic and equilibrium methods of the interaction between N-terminally truncated forms of chicken cystatin and the cysteine proteinases papain and actinidin.Quail cystatin: isolation and characterisation of a new member of the cystatin family and its hypothetical interaction with cathepsin B.Variation in the P2-S2 stereochemical selectivity towards the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin.High-affinity binding of two molecules of cysteine proteinases to low-molecular-weight kininogen.The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.AtCYS1, a cystatin from Arabidopsis thaliana, suppresses hypersensitive cell death.Interaction of cysteine proteinases with recombinant kininogen domain 2, expressed in Escherichia coli.
P2860
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P2860
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh-hant
name
Kinetics of binding of chicken cystatin to papain.
@en
Kinetics of binding of chicken cystatin to papain.
@nl
type
label
Kinetics of binding of chicken cystatin to papain.
@en
Kinetics of binding of chicken cystatin to papain.
@nl
prefLabel
Kinetics of binding of chicken cystatin to papain.
@en
Kinetics of binding of chicken cystatin to papain.
@nl
P2093
P356
P1433
P1476
Kinetics of binding of chicken cystatin to papain.
@en
P2093
Alriksson E
Ylinenjärvi K
P304
P356
10.1021/BI00430A022
P407
P577
1989-02-01T00:00:00Z