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

A CK1 FRET biosensor reveals that DDX3X is an essential activator of CK1ε.

Journal of cell science - 4 Jan 2018

Dolde Christine, Bischof Joachim, Grüter Simon, Montada Anna, Halekotte Jakob, Peifer Christian, Kalbacher Hubert, Baumann Ulrich, Knippschild Uwe, Suter Beat

Abstract excerpt

Casein kinase 1 (CK1) plays central roles in various signal transduction pathways and performs many cellular activities. For many years CK1 was thought to act independently of modulatory subunits and in a constitutive manner. Recently, DEAD box RNA helicases, in particular DEAD box RNA helicase 3 X-linked (DDX3X), were found to stimulate CK1 activity in vitro In order to observe CK1 activity in living cells and...

Read the complete abstract on PubMed

Topics

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

Share to Biosensing Techniques
Share to Casein Kinase I

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cerebellar Neoplasms

Share to DEAD-box RNA Helicases

Share to Fluorescence Resonance Energy Transfer

Share to Medulloblastoma

Share to RNA Helicases

Share to Wnt Signaling Pathway

Source

Open in PubMed Open full text

Identifiers

PMID: 29222110
DOI: 10.1242/jcs.207316
PMCID: PMC5818060

Genes

SHH

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A CK1 FRET biosensor reveals that DDX3X is an essential activator of CK1ε.PMID 29222110Read ↗

Analog sensitive chemical inhibition of the DEAD-box protein DDX3.Semantic proximity Read ↗

Development of a chemical probe to enable characterization of the casein kinase 1γ subfamilySemantic proximity Read ↗

Mutant forms of DDX3X with diminished catalysis form hollow condensates that exhibit sex-specific regulationSemantic proximity Read ↗

Identification of a DYRK1A Inhibitor that Induces Degradation of the Target Kinase using Co-chaperone CDC37 fused with Luciferase nanoKAZ.Semantic proximity Read ↗

Specific catalytically impaired DDX3X mutants form sexually dimorphic hollow condensates.Semantic proximity Read ↗

Autoinhibitory Interdomain Interactions and Subfamily-specific Extensions Redefine the Catalytic Core of the Human DEAD-box Protein DDX3.Semantic proximity Read ↗

Cancer-associated mutants of RNA helicase DDX3X are defective in RNA-stimulated ATP hydrolysis.Semantic proximity Read ↗

A comprehensive proteomics-based interaction screen that links DYRK1A to RNF169 and to the DNA damage responseSemantic proximity Read ↗

Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the Ku70 subunit of the DNA-dependent protein kinase complex.Semantic proximity Read ↗

CK1δ kinase activity is modulated by Chk1-mediated phosphorylation.Semantic proximity Read ↗

DYRK1A regulates the recruitment of 53BP1 to the sites of DNA damage in part through interaction with RNF169Semantic proximity Read ↗

CK2 and protein kinases of the CK1 superfamily as targets for neurodegenerative disordersSemantic proximity Read ↗

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