Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.
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Mechanisms of amyloid formation revealed by solution NMRAtomic Resolution Structure of Monomorphic Aβ42 Amyloid FibrilsComparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationStructural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR StudySystemic amyloidosis: lessons from β2-microglobulin.Energy landscapes of functional proteins are inherently risky.pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomersHigh resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.Distinguishing closely related amyloid precursors using an RNA aptamer.Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH.Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.Binding Interactions of Agents That Alter α-Synuclein Aggregation.A tale of two tails: The importance of unstructured termini in the aggregation pathway of β2-microglobulin.Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Atomic-Level Quality Assessment of Enzymes Encapsulated in Bioinspired Silica.Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphismStructural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T
P2860
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P2860
Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.
description
2014 nî lūn-bûn
@nan
2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
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name
Secondary structure in the cor ...... and its truncated variant ΔN6.
@en
Secondary structure in the cor ...... and its truncated variant ΔN6.
@en-gb
Secondary structure in the cor ...... and its truncated variant ΔN6.
@nl
type
label
Secondary structure in the cor ...... and its truncated variant ΔN6.
@en
Secondary structure in the cor ...... and its truncated variant ΔN6.
@en-gb
Secondary structure in the cor ...... and its truncated variant ΔN6.
@nl
prefLabel
Secondary structure in the cor ...... and its truncated variant ΔN6.
@en
Secondary structure in the cor ...... and its truncated variant ΔN6.
@en-gb
Secondary structure in the cor ...... and its truncated variant ΔN6.
@nl
P2093
P2860
P50
P356
P1154
2-s2.0-84899766632
P1476
Secondary structure in the cor ...... and its truncated variant ΔN6.
@en
P2093
Claire J Sarell
Galia T Debelouchina
Loren B Andreas
Matthew T Eddy
Robert G Griffin
P2860
P304
P356
10.1021/JA4126092
P407
P577
2014-04-16T00:00:00Z