Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping. - Test2 - elhamkhani - TriplyDB

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

http://www.wikidata.org/entity/Q48182955

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The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillization Ubiquitous amyloids Crystal structure of human cystatin C stabilized against amyloid formation β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages Self-assembly of human latexin into amyloid-like oligomers.Functional repertoire, molecular pathways and diseases associated with 3D domain swapping in the human proteome Molecular determinants of improved cathepsin B inhibition by new cystatins obtained by DNA shuffling.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.Nonpathological extracellular amyloid is present during normal epididymal sperm maturation.Double domain swapping in bovine seminal RNase: formation of distinct N- and C-swapped tetramers and multimers with increasing biological activities Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands.A Single Spherical Assembly of Protein Amyloid Fibrils Formed by Laser Trapping.Expression, purification, and characterization of human cystatin C monomers and oligomers.Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein Stabilization, characterization, and selective removal of cystatin C amyloid oligomers.The method of purifying bioengineered spider silk determines the silk sphere properties.Application of amide hydrogen/deuterium exchange mass spectrometry for epitope mapping in human cystatin C.Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.Animal models of human amyloidoses: are transgenic mice worth the time and trouble?Fertility defects in mice expressing the L68Q variant of human cystatin C: a role for amyloid in male infertility.Developmental regulation of synthesis and dimerization of the amyloidogenic protease inhibitor cystatin C in the hematopoietic system.Mechanisms of amyloid fibril formation--focus on domain-swapping.Cystatin C is a disease-associated protein subject to multiple regulation.Functional Amyloids in Reproduction.Cystatin-related epididymal spermatogenic subgroup members are part of an amyloid matrix and associated with extracellular vesicles in the mouse epididymal lumen.Influence of point mutations on the stability, dimerization, and oligomerization of human cystatin C and its L68Q variant.A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies.Production of Cystatin C Wild Type and Stabilized Mutants.Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions.Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1.The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.Understanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies.Steered molecular dynamics simulation of the binding of the β2 and β3 regions in domain-swapped human cystatin C dimer.Oligomerization and transglutaminase cross-linking of the cystatin CRES in the mouse epididymal lumen: potential mechanism of extracellular quality control.A mechanistic model to predict effects of cathepsin B and cystatin C on β-amyloid aggregation and degradation.Identification and characterization of antibodies elicited by human cystatin C fragment.Steered molecular dynamics simulations on the binding of the appendant structure and helix-β2 in domain-swapped human cystatin C dimer.Appendant structure plays an important role in amyloidogenic cystatin dimerization prior to domain swapping.Isolation and characterization of autoantibodies against human cystatin C.Insights into the mechanism of cystatin C oligomer and amyloid formation and its interaction with β-amyloid.

P2860

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P2860

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

http://www.wikidata.org/entity/Q48182955

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

@zh

2007年學術文章

@zh-hant

name

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

@en

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

@nl

type

label

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

@en

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

@nl

prefLabel

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

@en

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

@nl

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P1433

Journal of Biological Chemistry

P1476

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

@en

P2093

Eric Carlemalm

http://www.w3.org/2001/XMLSchema#string

Maria Wahlbom

http://www.w3.org/2001/XMLSchema#string

Veronica Lindström

http://www.w3.org/2001/XMLSchema#string

Xin Wang

http://www.w3.org/2001/XMLSchema#string

P2860

Amyloid fibrils from the viewpoint of protein folding

Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin

3D domain swapping: a mechanism for oligomer assembly

Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping

Crystal structure of the human prion protein reveals a mechanism for oligomerization

XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

Common mechanisms of amyloid oligomer pathogenesis in degenerative disease

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.

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18318-18326

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scholarly article

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10.1074/JBC.M611368200

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25

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P478

282

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Mariusz Jaskolski

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2007-04-29T00:00:00Z

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17470433

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