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

Inherent Biophysical Properties Modulate the Toxicity of Soluble Amyloidogenic Light Chains.

Journal of molecular biology - 14 Feb 2020

Maritan Martina, Romeo Margherita, Oberti Luca, Sormanni Pietro, Tasaki Masayoshi, Russo Rosaria, Ambrosetti Arianna, Motta Paolo, Rognoni Paola, Mazzini Giulia, Barbiroli Alberto, Palladini Giovanni, Vendruscolo Michele, Diomede Luisa, Bolognesi Martino, Merlini Giampaolo, Lavatelli Francesca, Ricagno Stefano

Abstract excerpt

In light chain amyloidosis (AL), fibrillar deposition of monoclonal immunoglobulin light chains (LCs) in vital organs, such as heart, is associated with their severe dysfunction. In addition to the cellular damage caused by fibril deposition, direct toxicity of soluble prefibrillar amyloidogenic proteins has been reported, in particular, for cardiotoxicity. However, the molecular bases of proteotoxicity by...

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biophysics

Share to Immunoglobulin Light Chains

Share to Mutation

Share to Protein Folding

Source

Identifiers

PMID: 31874151
DOI: 10.1016/j.jmb.2019.12.015

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

Inherent Biophysical Properties Modulate the Toxicity of Soluble Amyloidogenic Light Chains.PMID 31874151Read ↗

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

Driving amyloid toxicity in a yeast model by structural changes: a molecular approach.Semantic proximity Read ↗

The Critical Role of the Variable Domain in Driving Proteotoxicity and Aggregation in Full-length Light ChainsSemantic proximity Read ↗

Polymorphic IGLV6-57 AL amyloid fibrils and features of a shared folding pathwaySemantic proximity Read ↗

Conserved features of intermediates in amyloid assembly determine their benign or toxic statesSemantic proximity Read ↗

The Amyloid Phenomenon and Its Links with Human Disease.Semantic proximity Read ↗

Protein misfolding, aggregation and mechanism of amyloid cytotoxicity: An overview and therapeutic strategies to inhibit aggregationSemantic proximity Read ↗

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

In vitro and in vivo disease models of cardiac amyloidosis: progress, pitfalls, and potential.Semantic proximity Read ↗

A mouse model of cardiac immunoglobulin light chain amyloidosis reveals insights into tissue accumulation and toxicity of amyloid fibrilsSemantic proximity Read ↗

Unfolding and Aggregation Pathways of Variable Domains from Immunoglobulin Light Chains.Semantic proximity Read ↗

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

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