Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly
about
Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectinMinimalist design of water-soluble cross-beta architecture.Trimming Down a Protein Structure to Its Bare Foldons: SPATIAL ORGANIZATION OF THE COOPERATIVE UNITStructure of an early native-like intermediate of β2-microglobulin amyloidogenesisSolubis: a webserver to reduce protein aggregation through mutationThe structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicityShort amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Selection on protein structure, interaction, and sequence.Sequence determinants of amyloid fibril formationAttraction by repulsion: compounds with like charges undergo self-assembly in water that improves in high salt and persists in real biological fluids.Protein solubility and folding enhancement by interaction with RNAAmyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesisSystematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutantsAn evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.The amyloid stretch hypothesis: recruiting proteins toward the dark sideIntrinsic disorder modulates protein self-assembly and aggregation.De novo designed peptide-based amyloid fibrils.Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.The importance of sequence diversity in the aggregation and evolution of proteins.Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid diseaseChaperoning roles of macromolecules interacting with proteins in vivo.Structural transitions and interactions in the early stages of human glucagon amyloid fibrillationIntrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.Increased Aggregation Is More Frequently Associated to Human Disease-Associated Mutations Than to Neutral Polymorphisms.Folding without charges.Thermodynamics of protein destabilization in live cellsLight-triggered disassembly of amyloid fibrils.Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.Origins of barriers and barrierless folding in BBL.Structural stability and heat-induced conformational change of two complement inhibitors: C4b-binding protein and factor HFrustration in the energy landscapes of multidomain protein misfolding.Protein aggregation in silico.Structures and free-energy landscapes of the wild type and mutants of the Abeta(21-30) peptide are determined by an interplay between intrapeptide electrostatic and hydrophobic interactions.Amyloid-a state in many guises: survival of the fittest fibril fold.Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.SLLISWD sequence in the 10FNIII domain initiates fibronectin fibrillogenesis.Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease.High-resolution imaging and nano-manipulation of biological structures on surface.
P2860
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P2860
Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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2000年の論文
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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
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2000年论文
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name
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@ast
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@en
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@nl
type
label
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@ast
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@en
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@nl
prefLabel
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@ast
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@en
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@nl
P2093
P2860
P921
P356
P1476
Designed protein tetramer zipp ...... tural clue to amyloid assembly
@en
P2093
M Oliveberg
O Kristensen
P2860
P304
P356
10.1073/PNAS.160086297
P407
P577
2000-08-29T00:00:00Z