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

Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.

Scientific reports - 27 Jan 2017

Hora Manuel, Carballo-Pacheco Martin, Weber Benedikt, Morris Vanessa K, Wittkopf Antje, Buchner Johannes, Strodel Birgit, Reif Bernd

Abstract excerpt

Antibody light chain amyloidosis is a rare disease caused by fibril formation of secreted immunoglobulin light chains (LCs). The huge variety of antibody sequences puts a serious challenge to drug discovery. The green tea polyphenol epigallocatechin-3-gallate (EGCG) is known to interfere with fibril formation in general. Here we present solution- and solid-state NMR studies as well as MD simulations to...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Catechin

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Immunoglobulin Light Chains

Share to Kinetics

Share to Magnetic Resonance Spectroscopy

Share to Proline

Share to Protein Aggregates

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 28128355
DOI: 10.1038/srep41515
PMCID: PMC5269747

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.PMID 28128355Read ↗

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

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

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

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

(-)-epigallocatechin-3-gallate inhibits fibrillogenesis of chicken cystatin.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 ↗

Rational design of antibodies targeting specific epitopes within intrinsically disordered proteinsSemantic proximity Read ↗

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

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

Inherent Biophysical Properties Modulate the Toxicity of Soluble Amyloidogenic Light Chains.Semantic proximity Read ↗

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

Chemical mutagenesis for the modulation and study of protein function and dysfunction within Alzheimer's diseaseSemantic proximity Read ↗

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