Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Altered dimer interface decreases stability in an amyloidogenic protein.

The Journal of biological chemistry - 6 Jun 2008

Baden Elizabeth M, Owen Barbara A L, Peterson Francis C, Volkman Brian F, Ramirez-Alvarado Marina, Thompson James R

Abstract excerpt

Amyloidoses are devastating and currently incurable diseases in which the process of amyloid formation causes fatal cellular and organ damage. The molecular mechanisms underlying amyloidoses are not well known. In this study, we address the structural basis of immunoglobulin light chain amyloidosis, which results from deposition of light chains produced by clonal plasma cells. We compare light chain amyloidosis...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid
Share to Amyloidosis
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Design

Share to Immunoglobulin kappa-Chains

Share to Mutation

Share to Plasma Cells

Share to Protein Structure, Quaternary

Source

Open in PubMed Open full text

Identifiers

PMID: 18400753
DOI: 10.1074/jbc.M705347200
PMCID: PMC2414275

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Altered dimer interface decreases stability in an amyloidogenic protein.PMID 18400753Read ↗

Structural Insights into the Role of Mutations in AmyloidogenesisSemantic proximity Read ↗

Structural alterations within native amyloidogenic immunoglobulin light chains.Semantic proximity Read ↗

A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface.Semantic proximity Read ↗

Mechanistic Insights into the Early Events in the Aggregation of Immunoglobulin Light ChainsSemantic proximity Read ↗

Tyrosine residues mediate fibril formation in a dynamic light chain dimer interface.Semantic proximity Read ↗

Immunoglobulin light chain amyloid aggregation.Semantic proximity Read ↗

Amyloid formation in light chain amyloidosis.Semantic proximity Read ↗

Preventing pathogenic dimerization in a misfolded antibody light chain through the design of an inhibitory peptideSemantic proximity Read ↗

Role of Complementarity-Determining Regions 1 and 3 in Pathologic Amyloid Formation by Human Immunoglobulin κ1 Light ChainsSemantic proximity Read ↗

Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensitySemantic proximity Read ↗

The Conformational Landscape of AlphaFold2-Predicted Amyloidogenic Light Chains and Their Correlation With VL Domain Mutations and Aggregation Propensity.Semantic proximity Read ↗

Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foeSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.