Conformational constraints for amyloid fibrillation: the importance of being unfolded.
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Fluorescent Proteins as Biomarkers and Biosensors: Throwing Color Lights on Molecular and Cellular ProcessesA partially folded structure of amyloid-beta(1-40) in an aqueous environmentProtein folding: then and nowPrediction of "hot spots" of aggregation in disease-linked polypeptidesMolecular signaling involving intrinsically disordered proteins in prostate cancerPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Misfolding and amyloid aggregation of apomyoglobinFibrillogenesis of huntingtin and other glutamine containing proteinsExploring the accessible conformations of N-terminal acetylated α-synucleinWrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulatorsWhat macromolecular crowding can do to a proteinInhibition of IAPP Aggregation and Toxicity by Natural Products and DerivativesHydrogen sulfide inhibits amyloid formationSecondary Structure of Huntingtin Amino-Terminal RegionStructure of an early native-like intermediate of β2-microglobulin amyloidogenesisMechanism of Protein Kinetic Stabilization by Engineered Disulfide CrosslinksUV-light exposed prion protein fails to form amyloid fibrilsThe effect of a DeltaK280 mutation on the unfolded state of a microtubule-binding repeat in TauAggregation propensity of the human proteomeSDS can be utilized as an amyloid inducer: a case study on diverse proteinsCovalent defects restrict supramolecular self-assembly of homopolypeptides: case study of β2-fibrils of poly-L-glutamic acidDirect detection of transient alpha-helical states in islet amyloid polypeptideMisfolding of proteins with a polyglutamine expansion is facilitated by proteasomal chaperonesA decade and a half of protein intrinsic disorder: biology still waits for physicsOrdered self-assembly mechanism of a spherical oncoprotein oligomer triggered by zinc removal and stabilized by an intrinsically disordered domainMicrocanonical thermostatistics of coarse-grained proteins with amyloidogenic propensity.Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Truncation of a β-barrel scaffold dissociates intrinsic stability from its propensity to aggregation.Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria.High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form.A quasi-spontaneous amyloid route in a DNA binding gene regulatory domain: The papillomavirus HPV16 E2 protein.Status quo of annotation of human disease variants.The glaucoma-associated olfactomedin domain of myocilin forms polymorphic fibrils that are constrained by partial unfolding and peptide sequenceSensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillationStepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.Self-assembly of human latexin into amyloid-like oligomers.Conformational changes of alpha-chymotrypsin in a fibrillation-promoting condition: a molecular dynamics study.Differential effects of glycation on protein aggregation and amyloid formation.
P2860
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P2860
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
@ast
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
@en
type
label
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
@ast
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
@en
prefLabel
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
@ast
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
@en
P1476
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
@en
P2093
Anthony L Fink
P304
P356
10.1016/J.BBAPAP.2003.12.008
P407
P577
2004-05-01T00:00:00Z