Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin.
about
The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transitionA regulatable switch mediates self-association in an immunoglobulin foldThe two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressureSystemic amyloidosis: lessons from β2-microglobulin.Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchangeApproach to characterization of the higher order structure of disulfide-containing proteins using hydrogen/deuterium exchange and top-down mass spectrometrySequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.Carnosine's effect on amyloid fibril formation and induced cytotoxicity of lysozyme.Energy landscapes of functional proteins are inherently risky.A New Folding Kinetic Mechanism for Human Transthyretin and the Influence of the Amyloidogenic V30M Mutation.Molecular interactions in the formation and deposition of beta2-microglobulin-related amyloid fibrils.An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibrilStructure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin.beta(2)-microglobulin: from physiology to amyloidosis.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Fast real-time NMR methods for characterizing short-lived molecular states.The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.Topological investigation of amyloid fibrils obtained from beta2-microglobulin.Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis.Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril FormationMetal binding sheds light on mechanisms of amyloid assembly.Delineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin.Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR.DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded formA Population Shift between Sparsely Populated Folding Intermediates Determines AmyloidogenicityNMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system.Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.A novel system for continuous protein refolding and on-line capture by expanded bed adsorption.Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis.Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I.Capillary electrophoresis investigation of a partially unfolded conformation of beta(2)-microglobulin.Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond.Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry.Conformational stability of amyloid fibrils of beta2-microglobulin probed by guanidine-hydrochloride-induced unfolding.Cleaved beta 2-microglobulin partially attains a conformation that has amyloidogenic features.Optimized fast mixing device for real-time NMR applications.
P2860
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P2860
Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Detection of two partially str ...... protein beta 2-microglobulin.
@ast
Detection of two partially str ...... protein beta 2-microglobulin.
@en
type
label
Detection of two partially str ...... protein beta 2-microglobulin.
@ast
Detection of two partially str ...... protein beta 2-microglobulin.
@en
prefLabel
Detection of two partially str ...... protein beta 2-microglobulin.
@ast
Detection of two partially str ...... protein beta 2-microglobulin.
@en
P2093
P356
P1476
Detection of two partially str ...... protein beta 2-microglobulin.
@en
P2093
A Andreola
C M Dobson
P Mangione
S Giorgetti
V Bellotti
P304
P356
10.1006/JMBI.2000.4478
P407
P577
2001-03-01T00:00:00Z