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

Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assembly

1 Jan 2013

Abstract excerpt

Approximately 1% of human proteins harbor a prion-like domain (PrLD) of similar low complexity sequence and amino acid composition to domains that drive prionogenesis of yeast proteins like Sup35. PrLDs are over-represented in human RNA-binding proteins and mediate phase transitions underpinning RNP granule assembly. This modality renders PrLDs prone to misfold into conformers that accrue in pathological...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis Research
Share to Prion Diseases and Protein Misfolding
Share to RNA Research and Splicing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25002999
DOI: 10.4161/rdis.25200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assemblyPMID 25002999Read ↗

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.Semantic proximity Read ↗

Mutations in human prion-like domains: pathogenic but not always amyloidogenic.Semantic proximity Read ↗

Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseSemantic proximity Read ↗

RNA-binding proteins with prion-like domains in health and disease.Semantic proximity Read ↗

Role of RNA Binding Proteins with prion-like domains in muscle and neuromuscular diseasesSemantic proximity Read ↗

Characterization of HNRNPA1 mutations defines diversity in pathogenic mechanisms and clinical presentation.Semantic proximity Read ↗

Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.Semantic proximity Read ↗

Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein.Semantic proximity Read ↗

DEFINING THE DIVERSITY OF HNRNPA1 MUTATIONS IN CLINICAL PHENOTYPE AND PATHOMECHANISMSemantic proximity Read ↗

Stress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrumSemantic proximity Read ↗

Manipulating the aggregation activity of human prion-like proteins.Semantic proximity Read ↗

Aggregation prone regions and gatekeeping residues in protein sequences.Semantic proximity Read ↗

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