Unfolding and Aggregation Pathways of Variable Domains from Immunoglobulin Light Chains.

doi:10.1021/acs.biochem.2c00704

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

Back to search

Article

Unfolding and Aggregation Pathways of Variable Domains from Immunoglobulin Light Chains.

Biochemistry - 7 Mar 2023

Meunier-Carmenate Yadira, Valdés-García Gilberto, Maya-Martinez Roberto, French-Pacheco Leidys, Fernández-Silva Arline, González-Onofre Yoselin, Millan-Pacheco Cesar, Pastor Nina, Amero Carlos

Abstract excerpt

Light chain amyloidosis is the most common form of systemic amyloidosis. This disease is caused by the formation and deposition of amyloid fibers made from immunoglobulin light chains. Environmental conditions such as pH and temperature can affect protein structure and induce the development of these fibers. Several studies have shed light on the native state, stability, dynamics, and final amyloid state of these...

Topics

Humans
Immunoglobulin Light Chains
Amyloid
Amyloidosis
Amyloidogenic Proteins
Mutation

Source

Open in PubMed

Identifiers

PMID: 36802343
DOI: 10.1021/acs.biochem.2c00704

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics