Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants. - Wikidata - awgldk - TriplyDB

Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants.

Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants.

http://www.wikidata.org/entity/Q35066532

about

Phage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitope Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Conformational Abs recognizing a generic amyloid fibril epitope.Transthyretin mutations in hyperthyroxinemia and amyloid diseases.Transthyretin amyloidosis: a tale of weak interactions.Presence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: an escape from ERAD Inhibition of TTR aggregation-induced cell death--a new role for serum amyloid P component.Transthyretin is dysregulated in preeclampsia, and its native form prevents the onset of disease in a preclinical mouse model.A monoclonal antibody against synthetic Aβ dimer assemblies neutralizes brain-derived synaptic plasticity-disrupting Aβ.Lactoferrin Glu561Asp facilitates secondary amyloidosis in the cornea.Localization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains.Evidence for early cytotoxic aggregates in transgenic mice for human transthyretin Leu55Pro Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.Novel conformation-specific monoclonal antibodies against amyloidogenic forms of transthyretin One mutation, two distinct disease variants: unravelling the impact of transthyretin amyloid fibril composition.An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-type protein.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Novel Antibody for the Treatment of Transthyretin Amyloidosis.Insights into the potential aggregation liabilities of the b12 Fab fragment via elevated temperature molecular dynamics.Deposition and passage of transthyretin through the blood-nerve barrier in recipients of familial amyloid polyneuropathy livers.Antibody therapy for familial amyloidotic polyneuropathy.Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy

P2860

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P2860

Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants.

http://www.wikidata.org/entity/Q35066532

description

1999 nî lūn-bûn

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1999 թուականի Մարտին հրատարակուած գիտական յօդուած

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1999 թվականի մարտին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Exposure of cryptic epitopes o ...... and in amyloidogenic mutants.

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Exposure of cryptic epitopes o ...... and in amyloidogenic mutants.

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Exposure of cryptic epitopes o ...... and in amyloidogenic mutants.

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Exposure of cryptic epitopes o ...... and in amyloidogenic mutants.

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prefLabel

Exposure of cryptic epitopes o ...... and in amyloidogenic mutants.

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Exposure of cryptic epitopes o ...... and in amyloidogenic mutants.

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P1433

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Exposure of cryptic epitopes o ...... and in amyloidogenic mutants.

@en

P2093

Andersson K

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Dacklin I

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Edvinsson A

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Goldsteins G

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Lundgren E

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Olofsson A

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Persson H

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Saraiva MJ

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P2860

Fibril in senile systemic amyloidosis is derived from normal transthyretin

Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A

The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils

Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation

Rapid and efficient site-specific mutagenesis without phenotypic selection

Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid

Topological mapping of complement component C9 by recombinant DNA techniques suggests a novel mechanism for its insertion into target membranes.

Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro.

Transthyretin mutations in health and disease.

The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid.

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3108-3113

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scholarly article

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10.1073/PNAS.96.6.3108

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P433

6

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96

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1999-03-01T00:00:00Z

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235614673

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10077645

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P932

15903

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