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

Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment.

Biochemistry - 1 May 2018

Janke Abigail M, Seo Da Hee, Rahmanian Vahid, Conicella Alexander E, Mathews Kaylee L, Burke Kathleen A, Mittal Jeetain, Fawzi Nicolas L

Abstract excerpt

Many cancer-causing chromosomal translocations result in transactivating protein products encoding FET family (FUS, EWSR1, TAF15) low-complexity (LC) domains fused to a DNA binding domain from one of several transcription factors. Recent work demonstrates that higher-order assemblies of FET LC domains bind the carboxy-terminal domain of the large subunit of RNA polymerase II (RNA pol II CTD), suggesting FET...

Read the complete abstract on PubMed

Topics

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

Share to Heterogeneous-Nuclear Ribonucleoprotein Group A-B
Share to Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Multiprotein Complexes

Share to Protein Domains

Share to RNA Polymerase II

Share to TATA-Binding Protein Associated Factors

Share to Translocation, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 28945358
DOI: 10.1021/acs.biochem.7b00310
PMCID: PMC5975632

Genes

TAF15
EWSR1
FUS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment.PMID 28945358Read ↗

Insights into Molecular Diversity within the FET Family: Unraveling Phase Separation of the N-Terminal Low Complexity Domain from RNA-Binding Protein EWSSemantic proximity Read ↗

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain.Semantic proximity Read ↗

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA binding domainSemantic proximity Read ↗

FUS and TAF15 safeguard the critical functions of the ribonucleoprotein network formed by EWSR1 and newly synthesized RNASemantic proximity Read ↗

Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation.Semantic proximity Read ↗

Real-Time Observation of Structure and Dynamics during the Liquid-to-Solid Transition of FUS LCSemantic proximity Read ↗

A ubiquitous disordered protein interaction module orchestrates transcription elongation.Semantic proximity Read ↗

Mutant huntingtin causes defective actin remodeling during stress: defining a new role for transglutaminase 2 in neurodegenerative disease.Semantic proximity Read ↗

Targeted ATAC-see (tATAC-see): A Visual Assay for Target-Specific Chromatin ProfilingSemantic proximity Read ↗

The Low Complexity Domain of the FUS RNA Binding Protein Self-assembles via the Mutually Exclusive Use of Two Distinct Cross-β CoresSemantic proximity Read ↗

ALS mutations in the TIA1 RNA granule protein have differing effect on low complexity domain fibril formationSemantic proximity Read ↗

Dynamic and Selective Low-Complexity Domain Interactions Revealed by Live-Cell Single-Molecule ImagingSemantic proximity Read ↗

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