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Article

Conserved RNA helicase FRH acts nonenzymatically to support the intrinsically disordered neurospora clock protein FRQ.

Molecular cell - 26 Dec 2013

Hurley Jennifer M, Larrondo Luis F, Loros Jennifer J, Dunlap Jay C

Abstract excerpt

Protein conformation dictates a great deal of protein function. A class of naturally unstructured proteins, termed intrinsically disordered proteins (IDPs), demonstrates that flexibility in structure can be as important mechanistically as rigid structure. At the core of the circadian transcription/translation feedback loop in Neurospora crassa is the protein FREQUENCY (FRQ), shown here shown to share many...

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Share to Circadian Rhythm
Share to CLOCK Proteins
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Neurospora crassa

Share to Protein Interaction Domains and Motifs

Share to Protein Stability

Share to Proteolysis

Share to RNA Helicases

Source

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Identifiers

PMID: 24316221
DOI: 10.1016/j.molcel.2013.11.005
PMCID: PMC3900029

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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.

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