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 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.

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http://www.wikidata.org/entity/Q33199753

Q33199753

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Crystal structure of human cystatin C stabilized against amyloid formation β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages Structural characterization of V57D and V57P mutants of human cystatin C, an amyloidogenic protein The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.Self-assembly of human latexin into amyloid-like oligomers.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.Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I.Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Stabilization, characterization, and selective removal of cystatin C amyloid oligomers.An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril 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.Human cystatin C monomer, dimer, oligomer, and amyloid structures are related to health and disease.Conformational stability of the RNP domain controls fibril formation of PABPN1.Influence of point mutations on the stability, dimerization, and oligomerization of human cystatin C and its L68Q variant.Domain swapping and amyloid fibril conformation.Production of Cystatin C Wild Type and Stabilized Mutants.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.Oligomerization of ribonuclease A: two novel three-dimensional domain-swapped tetramers.The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer.Steered molecular dynamics simulation of the binding of the β2 and β3 regions in domain-swapped human cystatin C dimer.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.Fibrillogenic oligomers of human cystatin C are formed by propagated 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.Amyloid fibril formation by human stefin B: influence of pH and TFE on fibril growth and morphology

P2860

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P2860

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.

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http://www.wikidata.org/entity/Q33199753

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2004 nî lūn-bûn

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2004 թուականի Մարտին հրատարակուած գիտական յօդուած

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2004 թվականի մարտին հրատարակված գիտական հոդված

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2004年の論文

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