The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
about
Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregatesAmyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSESNovel Zn2+-binding Sites in Human Transthyretin: IMPLICATIONS FOR AMYLOIDOGENESIS AND RETINOL-BINDING PROTEIN RECOGNITIONSwitch region for pathogenic structural change in conformational disease and its predictionPotentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy.Initial conformational changes of human transthyretin under partially denaturing conditionsPresence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: an escape from ERADExposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants.Biomarkers in the assessment of therapies for familial amyloidotic polyneuropathy.Why is Leu55-->Pro55 transthyretin variant the most amyloidogenic: insights from molecular dynamics simulations of transthyretin monomersFTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils.Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.4'-Iodo-4'-deoxydoxorubicin disrupts the fibrillar structure of transthyretin amyloid.Human transthyretin in complex with iododiflunisal: structural features associated with a potent amyloid inhibitor.Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative.Designing transthyretin mutants affecting tetrameric structure: implications in amyloidogenicity.The molecular interaction of 4'-iodo-4'-deoxydoxorubicin with Leu-55Pro transthyretin 'amyloid-like' oligomer leading to disaggregation.Structural and dynamics evidence for scaffold asymmetric flexibility of the human transthyretin tetramer.NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations
P2860
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P2860
The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The crystal structure of amylo ...... erization into amyloid fibrils
@ast
The crystal structure of amylo ...... erization into amyloid fibrils
@en
The crystal structure of amylo ...... erization into amyloid fibrils
@nl
type
label
The crystal structure of amylo ...... erization into amyloid fibrils
@ast
The crystal structure of amylo ...... erization into amyloid fibrils
@en
The crystal structure of amylo ...... erization into amyloid fibrils
@nl
prefLabel
The crystal structure of amylo ...... erization into amyloid fibrils
@ast
The crystal structure of amylo ...... erization into amyloid fibrils
@en
The crystal structure of amylo ...... erization into amyloid fibrils
@nl
P2093
P1476
The crystal structure of amylo ...... erization into amyloid fibrils
@en
P2093
M J Saraiva
M P Sebastião
P304
P407
P577
1998-09-18T00:00:00Z