A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
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Filming biomolecular processes by high-speed atomic force microscopyStructural Alterations within Native Amyloidogenic Immunoglobulin Light ChainsSolution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domainRational design of fiber forming supramolecular structuresMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Insights into the folding and unfolding processes of wild-type and mutated SH3 domain by molecular dynamics and replica exchange molecular dynamics simulations.A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state.Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Salts enhance both protein stability and amyloid formation of an immunoglobulin light chainBiologic and genetic characterization of the novel amyloidogenic lambda light chain-secreting human cell lines, ALMC-1 and ALMC-2.Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Abeta fibril formation pathwayAmyloid-forming peptides selected proteolytically from phage display library.Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Role of small oligomers on the amyloidogenic aggregation free-energy landscapeN-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretionProtein-folding landscapes in multichain systems.A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy.Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins.Coarse-grained strategy for modeling protein stability in concentrated solutions. II: phase behavior.Missense meanderings in sequence space: a biophysical view of protein evolution.Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.Multivalent protein polymers with controlled chemical and physical properties.Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.A brief overview of amyloids and Alzheimer's disease.The structural basis for biphasic kinetics in the folding of the WW domain from a formin-binding protein: lessons for protein design?Use of a small peptide fragment as an inhibitor of insulin fibrillation process: a study by high and low resolution spectroscopyDetermination of the second virial coefficient of bovine serum albumin under varying pH and ionic strength by composition-gradient multi-angle static light scattering.Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomersLight Chain Amyloid Fibrils Cause Metabolic Dysfunction in Human CardiomyocytesPreventing fibril formation of a protein by selective mutation.Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.Exploring amyloid formation by a de novo design.How does a simplified-sequence protein fold?Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.Mechanisms of amyloid fibril formation--focus on domain-swapping.Microbial manipulation of the amyloid fold.The fibril_one on-line database: mutations, experimental conditions, and trends associated with amyloid fibril formation.Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.
P2860
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P2860
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
description
2000 nî lūn-bûn
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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年學術文章
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name
A systematic exploration of th ...... loid fibril formation in vitro
@ast
A systematic exploration of th ...... loid fibril formation in vitro
@en
A systematic exploration of th ...... loid fibril formation in vitro
@nl
type
label
A systematic exploration of th ...... loid fibril formation in vitro
@ast
A systematic exploration of th ...... loid fibril formation in vitro
@en
A systematic exploration of th ...... loid fibril formation in vitro
@nl
prefLabel
A systematic exploration of th ...... loid fibril formation in vitro
@ast
A systematic exploration of th ...... loid fibril formation in vitro
@en
A systematic exploration of th ...... loid fibril formation in vitro
@nl
P2093
P2860
P356
P1476
A systematic exploration of th ...... loid fibril formation in vitro
@en
P2093
J S Merkel
M Ramirez-Alvarado
P2860
P304
P356
10.1073/PNAS.150091797
P407
P577
2000-08-01T00:00:00Z