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

DYRK1B mutations associated with metabolic syndrome impair the chaperone-dependent maturation of the kinase domain.

Scientific reports - 25 Jul 2017

Abu Jhaisha Samira, Widowati Esti W, Kii Isao, Sonamoto Rie, Knapp Stefan, Papadopoulos Chrisovalantis, Becker Walter

Abstract excerpt

Two missense mutations of the DYRK1B gene have recently been found to co-segregate with a rare autosomal-dominant form of metabolic syndrome. This gene encodes a member of the DYRK family of protein kinases, which depend on tyrosine autophosphorylation to acquire the catalytically active conformation. The mutations (H90P and R102C) affect a structural element named DYRK homology (DH) box and did not directly...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Chaperonins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dyrk Kinases

Share to Metabolic Syndrome

Share to Protein Domains

Share to Protein-Tyrosine Kinases

Share to Triazoles

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 28743892
DOI: 10.1038/s41598-017-06874-w
PMCID: PMC5526990

Genes

CDC37

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

DYRK1B mutations associated with metabolic syndrome impair the chaperone-dependent maturation of the kinase domain.PMID 28743892Read ↗

Mutational analysis of two residues in the DYRK homology box of the protein kinase DYRK1A.Semantic proximity Read ↗

A form of the metabolic syndrome associated with mutations in DYRK1B.Semantic proximity Read ↗

DYRK1B variant linked to autosomal dominant metabolic syndrome.Semantic proximity Read ↗

Critical role of the CMGC insert sequence for tyrosine autophosphorylation in the protein kinase DYRK1B.Semantic proximity Read ↗

Cloning and Characterization of DYRK1B, a Novel Member of the DYRK Family of Protein KinasesSemantic proximity Read ↗

The Omnipresence of DYRK1A in Human DiseasesSemantic proximity Read ↗

A novel de novo heterozygous DYRK1A mutation causes complete loss of DYRK1A function and developmental delay.Semantic proximity Read ↗

Two novel variants in DYRK1B causative of AOMS3: expanding the clinical spectrum.Semantic proximity Read ↗

Biochemical basis of type IB (E1beta ) mutations in maple syrup urine disease. A prevalent allele in patients from the Druze kindred in Israel.Semantic proximity Read ↗

DYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 binding.Semantic proximity Read ↗

Mutational Analysis of Glycogen Synthase Kinase 3β Protein Kinase Together with Kinome-Wide Binding and Stability Studies Suggests Context-Dependent Recognition of Kinases by the Chaperone Heat Shock Protein 90.Semantic proximity Read ↗

The Q188R mutation in human galactose-1-phosphate uridylyltransferase acts as a partial dominant negative.Semantic proximity Read ↗

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