A regulatable switch mediates self-association in an immunoglobulin fold
about
D-strand perturbation and amyloid propensity in beta-2 microglobulinProtein-induced photophysical changes to the amyloid indicator dye thioflavin TAssessing the causes and consequences of co-polymerization in amyloid formationStructural basis for regulation of the Crk signaling protein by a proline switch.β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkagesAtomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic 2-microglobulin variantConformational Conversion during Amyloid Formation at Atomic ResolutionBslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.Structure of the preamyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry.Structural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometryCalcium binding to beta-2-microglobulin at physiological pH drives the occurrence of conformational changes which cause the protein to precipitate into amorphous forms that subsequently transform into amyloid aggregates.A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.Wild type beta-2 microglobulin and DE loop mutants display a common fibrillar architectureDynamic Clustering of the Bacterial Sensory Kinase BaeSZinc-Induced Polymerization of Killer-Cell Ig-like Receptor into Filaments Promotes Its Inhibitory Function at Cytotoxic Immunological Synapses.Molecular insights into cell toxicity of a novel familial amyloidogenic variant of β2-microglobulin.Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils.Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate β2-microglobulin amyloid assembly.Copper binding to beta-2-microglobulin and its pre-amyloid oligomers.beta(2)-microglobulin: from physiology to amyloidosis.NMR reveals novel mechanisms of protein activity regulation.Mechanisms of amyloid fibril formation--focus on domain-swapping.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Structural, morphological, and functional diversity of amyloid oligomers.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Increased β-Sheet Dynamics and D-E Loop Repositioning Are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin.A covalent homodimer probing early oligomers along amyloid aggregation.Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-{beta} from Alzheimer disease.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.DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded formA Population Shift between Sparsely Populated Folding Intermediates Determines AmyloidogenicityAssessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.Role of zinc in human islet amyloid polypeptide aggregation.A tale of two tails: The importance of unstructured termini in the aggregation pathway of β2-microglobulin.Incomplete Refolding of Antibody Light Chains to Non-Native, Protease-Sensitive Conformations Leads to Aggregation: A Mechanism of Amyloidogenesis in Patients?Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients.Characterization of β2-microglobulin conformational intermediates associated to different fibrillation conditions
P2860
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P2860
A regulatable switch mediates self-association in an immunoglobulin fold
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A regulatable switch mediates self-association in an immunoglobulin fold
@ast
A regulatable switch mediates self-association in an immunoglobulin fold
@en
A regulatable switch mediates self-association in an immunoglobulin fold
@nl
type
label
A regulatable switch mediates self-association in an immunoglobulin fold
@ast
A regulatable switch mediates self-association in an immunoglobulin fold
@en
A regulatable switch mediates self-association in an immunoglobulin fold
@nl
prefLabel
A regulatable switch mediates self-association in an immunoglobulin fold
@ast
A regulatable switch mediates self-association in an immunoglobulin fold
@en
A regulatable switch mediates self-association in an immunoglobulin fold
@nl
P2093
P2860
P3181
P356
P1476
A regulatable switch mediates self-association in an immunoglobulin fold
@en
P2093
Andrew D Miranker
Catherine M Eakin
Jimin M Wang
Matthew F Calabrese
P2860
P2888
P304
P3181
P356
10.1038/NSMB.1483
P577
2008-09-01T00:00:00Z
P5875
P6179
1044111236