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

Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.

PloS one - 1 Jan 2009

Poshusta Tanya L, Sikkink Laura A, Leung Nelson, Clark Raynell J, Dispenzieri Angela, Ramirez-Alvarado Marina

Abstract excerpt

BACKGROUND: The amyloidoses are protein misfolding diseases characterized by the deposition of amyloid that leads to cell death and tissue degeneration. In immunoglobulin light chain amyloidosis (AL), each patient has a unique monoclonal immunoglobulin light chain (LC) that forms amyloid deposits. Somatic mutations in AL LCs make these proteins less thermodynamically stable than their non-amyloidogenic...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Amyloidosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoglobulin Light Chains

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Multiple Myeloma

Share to Protein Structure, Secondary

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 19365555
DOI: 10.1371/journal.pone.0005169
PMCID: PMC2664898

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.PMID 19365555Read ↗

Immunoglobulin light chain amyloid aggregation.Semantic proximity Read ↗

An updated AL-base reveals ranked enrichment of immunoglobulin light chain variable genes in AL amyloidosis.Semantic proximity Read ↗

Investigating Local Sequence‐Structural Attributes of Amyloidogenic Light Chain Variable DomainsSemantic proximity Read ↗

Amyloid formation in light chain amyloidosis.Semantic proximity Read ↗

Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.Semantic proximity Read ↗

An updated AL-Base reveals ranked enrichment of immunoglobulin light chain variable genes in AL amyloidosisSemantic proximity Read ↗

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

Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains.Semantic proximity Read ↗

Identification of clonal immunoglobulin λ light-chain gene rearrangements in AL amyloidosis using next-generation sequencingSemantic proximity Read ↗

Structural Consequences of Antibody Light Chain N Glycosylation in AL AmyloidosisSemantic proximity Read ↗

Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.Semantic proximity Read ↗

Comparison of IGLV2-14 light chain sequences of patients with AL amyloidosis or multiple myeloma.Semantic proximity Read ↗

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