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 human β-III-spectrin spinocerebellar ataxia type 5 mutation causes high-affinity F-actin binding.

Scientific reports - 17 Feb 2016

Avery Adam W, Crain Jonathan, Thomas David D, Hays Thomas S

Abstract excerpt

Spinocerebellar ataxia type 5 (SCA5) is a human neurodegenerative disease that stems from mutations in the SPTBN2 gene encoding the protein β-III-spectrin. Here we investigated the molecular consequence of a SCA5 missense mutation that results in a L253P substitution in the actin-binding domain (ABD) of β-III-spectrin. We report that the L253P substitution in the isolated β-III-spectrin ABD causes strikingly high...

Read the complete abstract on PubMed

Topics

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

Share to Actins
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Protein Interaction Domains and Motifs

Share to Protein Stability

Share to Spectrin

Share to Spinocerebellar Ataxias

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 26883385
DOI: 10.1038/srep21375
PMCID: PMC4756369

Genes

SPTBN2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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 human β-III-spectrin spinocerebellar ataxia type 5 mutation causes high-affinity F-actin binding.PMID 26883385Read ↗

Increased actin binding is a shared molecular consequence of numerous spinocerebellar ataxia mutations in β-III-spectrinSemantic proximity Read ↗

Increased Actin Binding Is a Shared Molecular Consequence of Numerous SCA5 Mutations in β-III-Spectrin.Semantic proximity Read ↗

β-III-spectrin N-terminus is required for high-affinity actin binding and SCA5 neurotoxicity.Semantic proximity Read ↗

β-III-spectrin spinocerebellar ataxia type 5 mutation reveals a dominant cytoskeletal mechanism that underlies dendritic arborization.Semantic proximity Read ↗

Molecular consequences of SCA5 mutations in the spectrin-repeat domains of β-III-spectrin.Semantic proximity Read ↗

Spectrin: structure, function and disease.Semantic proximity Read ↗

Expanding the β-III Spectrin-Associated Phenotypes toward Non-Progressive Congenital Ataxias with Neurodegeneration.Semantic proximity Read ↗

-III spectrin mutation L253P associated with spinocerebellar ataxia type 5 interferes with binding to Arp1 and protein trafficking from the GolgiSemantic proximity Read ↗

Spectrin mutations in spinocerebellar ataxia (SCA).Semantic proximity Read ↗

Structural basis for spectrin recognition by ankyrin.Semantic proximity Read ↗

Spinocerebellar ataxia type 5.Semantic proximity Read ↗

Novel drug discovery platform for spinocerebellar ataxia, using fluorescence technology targeting β-III-spectrin.Semantic proximity Read ↗

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