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

Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity

27 Nov 2017

Abstract excerpt

Light chain amyloidosis (AL), the most common systemic amyloidosis, is caused by the overproduction and the aggregation of monoclonal immunoglobulin light chains (LC) in target organs. Due to genetic rearrangement and somatic hypermutation, virtually, each AL patient presents a different amyloidogenic LC. Because of such complexity, the fine molecular determinants of LC aggregation propensity and proteotoxicity...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidosis: Diagnosis, Treatment, Outcomes
Share to Drug Transport and Resistance Mechanisms
Share to Protein Kinase Regulation and GTPase Signaling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 29196671
DOI: 10.1038/s41598-017-16953-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensityPMID 29196671Read ↗

Immunoglobulin light chain amyloid aggregation.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 ↗

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

Computational evidences of a misfolding event in an aggregation-prone light chain preceding the formation of the non-native pathogenic dimer.Semantic proximity Read ↗

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

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

Exploring the sequence features determining amyloidosis in human antibody light chainsSemantic proximity Read ↗

Driving forces in amyloidosis: How does a light chain make a heavy heart?Semantic proximity Read ↗

Four structural risk factors identify most fibril-forming kappa light chainsSemantic proximity Read ↗

Role of complementarity-determining regions 1 and 3 in pathologic amyloid formation by human immunoglobulin κ1 light chainsSemantic proximity Read ↗

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

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