Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation
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Amyloid formation in light chain amyloidosisAltered Dimer Interface Decreases Stability in an Amyloidogenic ProteinStructural Insights into the Role of Mutations in AmyloidogenesisStructural Alterations within Native Amyloidogenic Immunoglobulin Light ChainsA Single Mutation Promotes Amyloidogenicity through a Highly Promiscuous Dimer InterfaceTertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formationHeterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic kappa1 immunoglobulin light chainsFree immunoglobulin light chain (FLC) promotes murine colitis and colitis-associated colon carcinogenesis by activating the inflammasome.Shoulder-pad sign of amyloidosis: structure of an Ig kappa III protein.Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycansStructures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH.Complete primary sequences of two lambda immunoglobulin light chains in myelomas with nonamyloid (Randall-type) light chain deposition disease.Effect of single point mutations in a form of systemic amyloidosis.Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.Perspectives in treatment of AL amyloidosis.Light chain amyloidosis - current findings and future prospects.ALkappa(I) (UNK) - primary structure of an AL-amyloid protein presenting an organ-limited subcutaneous nodular amyloid syndrome of long duration. Case report and review.Using empirical phase diagrams to understand the role of intramolecular dynamics in immunoglobulin G stabilityStructure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients.Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.Immunoglobulin lambda light chains are the precursors of ureteral localized amyloidosis: a micromethod for extraction of amyloidProtein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis)Four structural risk factors identify most fibril-forming kappa light chainsGlycosylation of immunoglobulin light chains associated with amyloidosisStructural analysis of the amyloidogenic k Bence Jones protein (FUR)
P2860
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P2860
Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Tertiary structure of an amylo ...... l for amyloid fibril formation
@ast
Tertiary structure of an amylo ...... l for amyloid fibril formation
@en
Tertiary structure of an amylo ...... l for amyloid fibril formation
@nl
type
label
Tertiary structure of an amylo ...... l for amyloid fibril formation
@ast
Tertiary structure of an amylo ...... l for amyloid fibril formation
@en
Tertiary structure of an amylo ...... l for amyloid fibril formation
@nl
prefLabel
Tertiary structure of an amylo ...... l for amyloid fibril formation
@ast
Tertiary structure of an amylo ...... l for amyloid fibril formation
@en
Tertiary structure of an amylo ...... l for amyloid fibril formation
@nl
P2093
P2860
P356
P1476
Tertiary structure of an amylo ...... l for amyloid fibril formation
@en
P2093
J J Liepnieks
J R Murrell
M D Benson
N Schormann
P2860
P304
P356
10.1073/PNAS.92.21.9490
P407
P577
1995-10-10T00:00:00Z