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

Structural Analysis and Conformational Dynamics of STN1 Gene Mutations Involved in Coat Plus Syndrome

12 Jun 2019

Abstract excerpt

The human CST complex (CTC1-STN1-TEN1) is associated with telomere functions including genome stability. We have systemically analyzed the sequence of STN and performed structure analysis to establish its association with the Coat Plus (CP) syndrome. Many deleterious non-synonymous SNPs have been identified and subjected for structure analysis to find their pathogenic association and aggregation propensity. A...

Read the complete abstract on PubMed

Topics

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

Share to Cancer-related gene regulation
Share to Genetics and Neurodevelopmental Disorders
Share to Neurogenetic and Muscular Disorders Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 31245382
DOI: 10.3389/fmolb.2019.00041

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural Analysis and Conformational Dynamics of STN1 Gene Mutations Involved in Coat Plus SyndromePMID 31245382Read ↗

Structural genomics approach to investigate deleterious impact of nsSNPs in conserved telomere maintenance component 1.Semantic proximity Read ↗

An Indian child with Coats plus syndrome due to mutations in STN1.Semantic proximity Read ↗

Structural and functional impact of non- synonymous SNPs in the CST complex subunit TEN1: Structural genomics approachSemantic proximity Read ↗

Mutations in STN1 cause Coats plus syndrome and are associated with genomic and telomere defects.Semantic proximity Read ↗

Functional characterization of human CTC1 mutations reveals novel mechanisms responsible for the pathogenesis of the telomere disease Coats plus.Semantic proximity Read ↗

Structural analysis of <i>de novo</i> STXBP1 mutation in complex with syntaxin 1A reveals a major alteration in the interaction interface in a child with developmental delay and spasticitySemantic proximity Read ↗

Novel compound heterozygous STN1 variants are associated with Coats Plus syndrome.Semantic proximity Read ↗

Structural and functional analysis of an OB-fold in human Ctc1 implicated in telomere maintenance and bone marrow syndromes.Semantic proximity Read ↗

A Novel Biallelic STN1 Mutation Is Associated With Adult-Onset Multisystemic Involvement: Broadening the Mutational Spectrum in Coats Plus Syndrome.Semantic proximity Read ↗

Structural Characterization of Carbonic Anhydrase VIII and Effects of Missense Single Nucleotide Variations to Protein Structure and Function.Semantic proximity Read ↗

Molecular basis of telomere syndrome caused by CTC1 mutations.Semantic proximity Read ↗

The cryo-EM structure of human CST reveals a two-megadalton decameric assembly bound to telomeric DNASemantic proximity Read ↗

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