about
The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillizationInnate Immune Response in Brain, NF-Kappa B Signaling and CystatinsCrystal structure of human cystatin C stabilized against amyloid formationStructural characterization of V57D and V57P mutants of human cystatin C, an amyloidogenic proteinPressure as a denaturing agent in studies of single-point mutants of an amyloidogenic protein human cystatin c.The cerebral hemorrhage-producing cystatin C variant (L68Q) in extracellular fluids.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.Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site-specific glycosylation in yeast.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.Biochemistry and clinical role of human cystatin C.Targeted quantitative mass spectrometric immunoassay for human protein variants.Expression, purification, and characterization of human cystatin C monomers and oligomers.Stabilization, characterization, and selective removal of cystatin C amyloid oligomers.Chemical chaperone and inhibitor discovery: potential treatments for protein conformational diseases.Application of amide hydrogen/deuterium exchange mass spectrometry for epitope mapping in human cystatin C.Cystatin SN neutralizes the inhibitory effect of cystatin C on cathepsin B activity.Cystatins in immune system.Internalization of exogenous cystatin F supresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms.Regions which are Responsible for Swapping are also Responsible for Folding and Misfolding.Molecular dynamics simulations of human cystatin C and its L68Q varient to investigate the domain swapping mechanism.Structural and dynamic properties of a new amyloidogenic chicken cystatin mutant I108T.Molecular dynamics simulation to investigate the impact of disulfide bond formation on conformational stability of chicken cystatin I66Q mutant.Oligomerization and transglutaminase cross-linking of the cystatin CRES in the mouse epididymal lumen: potential mechanism of extracellular quality control.Identification and characterization of antibodies elicited by human cystatin C fragment.Appendant structure plays an important role in amyloidogenic cystatin dimerization prior to domain swapping.Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.Isolation and characterization of autoantibodies against human cystatin C.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մարտին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Hereditary cystatin C amyloid angiopathy.
@ast
Hereditary cystatin C amyloid angiopathy.
@en
type
label
Hereditary cystatin C amyloid angiopathy.
@ast
Hereditary cystatin C amyloid angiopathy.
@en
prefLabel
Hereditary cystatin C amyloid angiopathy.
@ast
Hereditary cystatin C amyloid angiopathy.
@en
P2860
P1433
P1476
Hereditary cystatin C amyloid angiopathy.
@en
P2093
P2860
P356
10.3109/13506120009146827
P577
2000-03-01T00:00:00Z