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

C. elegans expressing human β2-microglobulin: a novel model for studying the relationship between the molecular assembly and the toxic phenotype.

PloS one - 1 Jan 2012

Diomede Luisa, Soria Cristina, Romeo Margherita, Giorgetti Sofia, Marchese Loredana, Mangione Patrizia Palma, Porcari Riccardo, Zorzoli Irene, Salmona Mario, Bellotti Vittorio, Stoppini Monica

Abstract excerpt

Availability of living organisms to mimic key step of amyloidogenesis of human protein has become an indispensable tool for our translation approach aiming at filling the deep gap existing between the biophysical and biochemical data obtained in vitro and the pathological features observed in patients. Human β(2)-microglobulin (β(2)-m) causes systemic amyloidosis in haemodialysed patients. The structure,...

Read the complete abstract on PubMed

Topics

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

Share to Animals, Genetically Modified
Share to beta 2-Microglobulin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Caenorhabditis elegans

Share to Fluorescent Antibody Technique

Share to Genotype

Share to Microscopy, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 23284985
DOI: 10.1371/journal.pone.0052314
PMCID: PMC3528749

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

C. elegans expressing human β2-microglobulin: a novel model for studying the relationship between the molecular assembly and the toxic phenotype.PMID 23284985Read ↗

Global Proteotoxicity Caused by Human β2 Microglobulin Variants Impairs the Unfolded Protein Response in C. elegans.Semantic proximity Read ↗

C. elegans expressing D76N β2-microglobulin: a model for in vivo screening of drug candidates targeting amyloidosis.Semantic proximity Read ↗

Caenorhabditis elegans Models to Investigate the Mechanisms Underlying Tau Toxicity in TauopathiesSemantic proximity Read ↗

Utility of an improved model of amyloid-beta (Aβ1-42) toxicity in Caenorhabditis elegans for drug screening for Alzheimer’s diseaseSemantic proximity Read ↗

Modeling immunoglobulin light chain amyloidosis in <i>Caenorhabditis elegans</i>Semantic proximity Read ↗

Modeling immunoglobulin light chain amyloidosis in Caenorhabditis elegansSemantic proximity Read ↗

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in <i>C. elegans</i>Semantic proximity Read ↗

Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans.Semantic proximity Read ↗

Expression of A2V-mutated Aβ in Caenorhabditis elegans results in oligomer formation and toxicity.Semantic proximity Read ↗

Hsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes Treatment.Semantic proximity Read ↗

Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan.Semantic proximity Read ↗

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegansSemantic proximity Read ↗

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