The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
about
Deficiency of disulfide bonds facilitating fibrillogenesis of endostatinPauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid diseaseβ2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkagesNMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain.Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchangePolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Disulfide bridges remain intact while native insulin converts into amyloid fibrils3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR.A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrilsbeta(2)-microglobulin: from physiology to amyloidosis.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Investigation into the role of macrophages in the formation and degradation of beta2-microglobulin amyloid fibrils.Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy.Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta2-microglobulin.Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry.Small molecule-mediated inhibition of β-2-microglobulin-based amyloid fibril formation.Dynamics and dimension of an amyloidogenic disordered state of human β(2)-microglobulin.Reduction of conformational mobility and aggregation in W60G β2-microglobulin: assessment by 15N NMR relaxation.
P2860
Q24293595-6B0453F5-91A6-4715-B39D-C9AC2A6C0617Q24564070-FD60301F-8C5B-4D6B-8484-1D7D9F1BC3B5Q27666185-D228826D-0E08-4E5E-8BAA-742BF78598E3Q30159629-8BBF299B-E3E9-4C9A-97D3-2AA7A4E5B436Q33373955-093AB8FF-4689-4B37-B355-371B1B26ED45Q34059772-9C2FE1B4-BF24-4A35-B188-E9A1B3349C1DQ34295554-0DAE81C8-3B6C-4DBC-8BE8-E22CE9778D06Q35722137-1620B1F7-6805-4D1D-94EA-2F3B31518623Q36719294-A8CFAFE4-50B0-4B8F-9E7A-113EE2A771FCQ37573510-B7C2DD6B-CF57-435B-BD47-0C8600F56AEDQ37877295-BE766906-47FB-4127-B15F-D638509F27FDQ38051908-C44F9AFD-4AAC-4AC5-AF55-E805B264FEEBQ39494899-4C27C196-4E2E-4B54-BB08-2CC03993771FQ40096568-B3095531-0472-4449-85F9-292AFA9B791AQ41085989-53B08E5B-2D1A-42B7-9BAF-AB195DD5EB67Q41454157-1558ED93-8348-4B2F-A021-1A0732E291C0Q41849521-707462CD-0E4C-4A8E-BF57-79D9D0C57639Q42550081-6F989749-B85C-40D2-9D79-DFAEF340170DQ43076154-0E2D3ADE-3548-42FB-B2D0-EDDE4B32CC5EQ43197716-CAD1DD0D-D53A-41BA-B27F-92AAABA3C871Q44575256-24271219-5DD6-4F06-B94D-15B005FDCFFAQ44853349-90125061-6D9B-445B-BFEF-EFC1AE7BAB20Q46372407-7C04FDDF-BF62-4954-B1E2-8FB236494A44Q47708157-7B67A420-EE31-4AAB-8FB0-DC52A51DC153Q54735249-C29A4EC7-2CCE-41BB-8594-600381629F24
P2860
The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
The role of disulfide bond in ...... studied by heteronuclear NMR.
@en
type
label
The role of disulfide bond in ...... studied by heteronuclear NMR.
@en
prefLabel
The role of disulfide bond in ...... studied by heteronuclear NMR.
@en
P2093
P2860
P356
P1433
P1476
The role of disulfide bond in ...... studied by heteronuclear NMR.
@en
P2093
Hidenori Katou
Hironobu Naiki
Hiroyuki Tanaka
Kazuhiro Hasegawa
Masaru Hoshino
Takashi Kanno
Tomoji Kawai
Yoshihisa Hagihara
P2860
P304
P356
10.1110/PS.0213202
P577
2002-09-01T00:00:00Z