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

TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells.

The Journal of biological chemistry - 4 May 2012

Colombrita Claudia, Onesto Elisa, Megiorni Francesca, Pizzuti Antonio, Baralle Francisco E, Buratti Emanuele, Silani Vincenzo, Ratti Antonia

Abstract excerpt

The RNA-binding proteins TDP-43 and FUS form abnormal cytoplasmic aggregates in affected tissues of patients with amyotrophic lateral sclerosis and frontotemporal lobar dementia. TDP-43 and FUS localize mainly in the nucleus where they regulate pre-mRNA splicing, but they are also involved in mRNA transport, stability, and translation. To better investigate their cytoplasmic activities, we applied an RNA...

Read the complete abstract on PubMed

Topics

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

Share to Immunoprecipitation
Share to Motor Neurons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nucleotide Motifs

Share to Progranulins

Share to RNA-Binding Protein FUS

Share to RNA Stability

Share to TATA-Binding Protein Associated Factors

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22427648
DOI: 10.1074/jbc.M111.333450
PMCID: PMC3346140

Genes

FUS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells.PMID 22427648Read ↗

TDP‐43 and FUS/TLS: cellular functions and implications for neurodegenerationSemantic proximity Read ↗

Conjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS.Semantic proximity Read ↗

The ALS/FTLD‐related RNA‐binding proteins TDP‐43 and FUS have common downstream RNA targets in cortical neuronsSemantic proximity Read ↗

Hu antigen R (HuR) is a positive regulator of the RNA-binding proteins TDP-43 and FUS/TLS: implications for amyotrophic lateral sclerosis.Semantic proximity Read ↗

The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulationSemantic proximity Read ↗

How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other?Semantic proximity Read ↗

Understanding age-related pathologic changes in TDP-43 functions and the consequence on RNA splicing and signalling in health and diseaseSemantic proximity Read ↗

Dysregulation of Translation in TDP-43 Proteinopathies: Deficits in the RNA Supply Chain and Local Protein ProductionSemantic proximity Read ↗

Connecting RNA-Modifying Similarities of TDP-43, FUS, and SOD1 with MicroRNA Dysregulation Amidst A Renewed Network Perspective of Amyotrophic Lateral Sclerosis Proteinopathy.Semantic proximity Read ↗

Novel and known transcriptional targets of ALS/FTD protein TDP-43: Meta-analysis and interactive graphical databasesSemantic proximity Read ↗

Progranulin transcripts with short and long 5' untranslated regions (UTRs) are differentially expressed via posttranscriptional and translational repression.Semantic proximity Read ↗

Familial ALS/FTD-associated RNA-binding deficient TDP-43 mutants cause neuronal and synaptic transcript dysregulation in vitroSemantic proximity Read ↗

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