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

Novel mutations in the DYNC1H1 tail domain refine the genetic and clinical spectrum of dyneinopathies.

Human mutation - 1 Mar 2015

Peeters Kristien, Bervoets Sven, Chamova Teodora, Litvinenko Ivan, De Vriendt Els, Bichev Stoyan, Kancheva Dahlia, Mitev Vanyo, Kennerson Marina, Timmerman Vincent, De Jonghe Peter, Tournev Ivailo, MacMillan John, Jordanova Albena

Abstract excerpt

The heavy chain 1 of cytoplasmic dynein (DYNC1H1) is responsible for movement of the motor complex along microtubules and recruitment of dynein components. Mutations in DYNC1H1 are associated with spinal muscular atrophy (SMA), hereditary motor and sensory neuropathy (HMSN), cortical malformations, or a combination of these. Combining linkage analysis and whole-exome sequencing, we identified a novel dominant...

Read the complete abstract on PubMed

Topics

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

Share to Charcot-Marie-Tooth Disease
Share to Cytoplasmic Dyneins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dyneins

Share to Microtubule-Associated Proteins

Share to Muscular Atrophy, Spinal

Share to Mutation

Share to Protein Structure, Tertiary

Share to RNA Research and Splicing

Source

Identifiers

PMID: 25512093
DOI: 10.1002/humu.22744

Genes

BICD2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel mutations in the DYNC1H1 tail domain refine the genetic and clinical spectrum of dyneinopathies.PMID 25512093Read ↗

Mutations in the tail domain of DYNC1H1 cause dominant spinal muscular atrophy.Semantic proximity Read ↗

Mutation screen reveals novel variants and expands the phenotypes associated with DYNC1H1.Semantic proximity Read ↗

Exome Sequencing Identifies De Novo DYNC1H1 Mutations Associated With Distal Spinal Muscular Atrophy and Malformations of Cortical Development.Semantic proximity Read ↗

Exome sequencing identifies a DYNC1H1 mutation in a large pedigree with dominant axonal Charcot-Marie-Tooth disease.Semantic proximity Read ↗

The clinical-phenotype continuum in DYNC1H1-related disorders-genomic profiling and proposal for a novel classification.Semantic proximity Read ↗

Expanding the phenotypic spectrum associated with mutations of DYNC1H1.Semantic proximity Read ↗

DYNC1H1-related disorders: A description of four new unrelated patients and a comprehensive review of previously reported variants.Semantic proximity Read ↗

Novel dynein DYNC1H1 neck and motor domain mutations link distal spinal muscular atrophy and abnormal cortical development.Semantic proximity Read ↗

Exome Sequencing Identifies DYNC1H1 Variant Associated With Vertebral Abnormality and Spinal Muscular Atrophy With Lower Extremity Predominance.Semantic proximity Read ↗

A recurrent de novo DYNC1H1 tail domain mutation causes spinal muscular atrophy with lower extremity predominance, learning difficulties and mild brain abnormality.Semantic proximity Read ↗

<i>DYNC1H1</i> mutations associated with neurological diseases compromise processivity of dynein-dynactin-cargo adaptor complexesSemantic proximity Read ↗

Mutations in DYNC1H1 cause severe intellectual disability with neuronal migration defectsSemantic proximity Read ↗

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