Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin
about
Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cellsCystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitorCystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatinsStructural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidasesRole of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinasesCrystal structure of the parasite inhibitor chagasin in complex with papain allows identification of structural requirements for broad reactivity and specificity determinants for target proteasesHydrophobic 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.Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C.High throughput testing of drug library substances and monoclonal antibodies for capacity to reduce formation of cystatin C dimers to identify candidates for treatment of hereditary cystatin C amyloid angiopathy.Inhibitory properties of cystatin F and its localization in U937 promonocyte cells.Olive flounder (Paralichthys olivaceus) cystatin C: cloning, mRNA expression, and enzymatic characterization of olive flounder 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 groupExpression, purification, and characterization of human cystatin C monomers and oligomers.Sparse reduced-rank regression detects genetic associations with voxel-wise longitudinal phenotypes in Alzheimer's disease.Stabilization, characterization, and selective removal of cystatin C amyloid oligomers.Modification of cystatin C activity by bacterial proteinases and neutrophil elastase in periodontitis.Cystatin SN neutralizes the inhibitory effect of cystatin C on cathepsin B activity.Identification of cystatin SN as a novel biomarker for pancreatic cancer.Cystatin C properties crucial for uptake and inhibition of intracellular target enzymes.Cystatins in health and disease.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.Local 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.Evaluation of hydrogen-bonding and enantiomeric P2-S2 hydrophobic contacts in dynamic aspects of molecular recognition by papain.Cystatin like thiol proteinase inhibitor from pancreas of Capra hircus: purification and detailed biochemical characterization.Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probImportance of the evolutionarily conserved glycine residue in the N-terminal region of human cystatin C (Gly-11) for cysteine endopeptidase inhibition.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.Delineating protein-protein interactions via biomolecular interaction analysis-mass spectrometry.Cystatin C uptake in the eye.Different cysteine proteinases involved in bone resorption and osteoclast formation.Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.Interaction of cysteine proteinases with recombinant kininogen domain 2, expressed in Escherichia coli.
P2860
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P2860
Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Interaction of recombinant hum ...... oteinases papain and actinidin
@ast
Interaction of recombinant hum ...... oteinases papain and actinidin
@en
Interaction of recombinant hum ...... oteinases papain and actinidin
@en-gb
Interaction of recombinant hum ...... oteinases papain and actinidin
@nl
type
label
Interaction of recombinant hum ...... oteinases papain and actinidin
@ast
Interaction of recombinant hum ...... oteinases papain and actinidin
@en
Interaction of recombinant hum ...... oteinases papain and actinidin
@en-gb
Interaction of recombinant hum ...... oteinases papain and actinidin
@nl
prefLabel
Interaction of recombinant hum ...... oteinases papain and actinidin
@ast
Interaction of recombinant hum ...... oteinases papain and actinidin
@en
Interaction of recombinant hum ...... oteinases papain and actinidin
@en-gb
Interaction of recombinant hum ...... oteinases papain and actinidin
@nl
P2093
P2860
P356
P1433
P1476
Interaction of recombinant hum ...... oteinases papain and actinidin
@en
P2093
P2860
P356
10.1042/BJ2810049
P407
P478
281 ( Pt 1)
P577
1992-01-01T00:00:00Z