Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.
about
Converting the Highly Amyloidogenic Human Calcitonin into a Powerful Fibril Inhibitor by Three-dimensional Structure Homology with a Non-amyloidogenic AnalogueN-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneityComparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationInsights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometryElongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry.Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR studyA simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.Early folding events protect aggregation-prone regions of a β-rich protein.K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscapePrediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.Ligand binding to distinct states diverts aggregation of an amyloid-forming protein.Comparative Analyses of the Relative Effects of Various Mutations in Major Histocompatibility Complex I-a Way to Predict Protein-Protein Interactions.The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein.Size distribution of amyloid nanofibrils.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril FormationPhosphorylation as a tool to modulate aggregation propensity and to predict fibril architecture.Multiple competing pathways for chemical reaction: drastic reaction shortcut for the self-catalytic double-helix formation of helicene oligomers.Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.Structural and dynamical characterization of the pH-dependence of the pectin methylesterase-pectin methylesterase inhibitor complex.Assessing the effect of D59P mutation in the DE loop region in amyloid aggregation propensity of β2-microglobulin: A molecular dynamics simulation study.
P2860
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P2860
Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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name
Competition between intramolec ...... in an amyloid-forming protein.
@en
Competition between intramolec ...... in an amyloid-forming protein.
@en-gb
Competition between intramolec ...... in an amyloid-forming protein.
@nl
type
label
Competition between intramolec ...... in an amyloid-forming protein.
@en
Competition between intramolec ...... in an amyloid-forming protein.
@en-gb
Competition between intramolec ...... in an amyloid-forming protein.
@nl
prefLabel
Competition between intramolec ...... in an amyloid-forming protein.
@en
Competition between intramolec ...... in an amyloid-forming protein.
@en-gb
Competition between intramolec ...... in an amyloid-forming protein.
@nl
P2860
P50
P1476
Competition between intramolec ...... in an amyloid-forming protein.
@en
P2093
Geoffrey W Platt
Katy E Routledge
P2860
P304
P356
10.1016/J.JMB.2009.04.042
P407
P577
2009-04-23T00:00:00Z