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

Dyskeratosis congenita mutations in dyskerin SUMOylation consensus sites lead to impaired telomerase RNA accumulation and telomere defects.

Human molecular genetics - 1 Sept 2013

Brault Marie Eve, Lauzon Catherine, Autexier Chantal

Abstract excerpt

Mutations in the dyskerin gene (DKC1) cause X-linked dyskeratosis congenita (DC), a rare and fatal premature aging syndrome characterized by defective telomere maintenance. Dyskerin is a highly conserved nucleolar protein, and a component of the human telomerase complex that is essential for human telomerase RNA (hTR) stability. However, its regulation remains poorly understood. Here, we report that dyskerin can...

Read the complete abstract on PubMed

Topics

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

Share to Dyskeratosis Congenita
Share to Gene Knockdown Techniques

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

Share to Protein Stability

Share to Small Ubiquitin-Related Modifier Proteins

Share to Sumoylation

Share to Telomerase

Share to Telomere

Share to Telomere Homeostasis

Source

Identifiers

PMID: 23660516
DOI: 10.1093/hmg/ddt204

Genes

DKC1

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

Dyskeratosis congenita mutations in dyskerin SUMOylation consensus sites lead to impaired telomerase RNA accumulation and telomere defects.PMID 23660516Read ↗

The C-terminal extension of dyskerin is a dyskeratosis congenita mutational hotspot that modulates interaction with telomerase RNA and subcellular localization.Semantic proximity Read ↗

Decreased dyskerin levels as a mechanism of telomere shortening in X-linked dyskeratosis congenita.Semantic proximity Read ↗

Dyskeratosis congenita: molecular insights into telomerase function, ageing and cancer.Semantic proximity Read ↗

N-terminal residues of human dyskerin are required for interactions with telomerase RNA that prevent RNA degradationSemantic proximity Read ↗

Dyskeratosis congenita -- a disease of dysfunctional telomere maintenance.Semantic proximity Read ↗

Disease mutations in the N-terminal extension and α2’-helix of dyskerin do not abolish dimerization but disrupt binding to the telomerase RNASemantic proximity Read ↗

Disease mutations in the N-terminal extension and α2’-helix of dyskerin do not abolish dimerization but disrupt binding to the telomerase RNASemantic proximity Read ↗

Dyskeratosis congenita.Semantic proximity Read ↗

Dyskeratosis congenita: a genetic disorder of many facesSemantic proximity Read ↗

SUMOylation- and GAR1-dependent regulation of dyskerin nuclear and subnuclear localizationSemantic proximity Read ↗

Domain specific mutations in dyskerin disrupt 3' end processing of scaRNA13.Semantic proximity Read ↗

Dyskeratosis CongenitaSemantic proximity Read ↗

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