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

Identification of novel functional sites in the Cav1.3 calcium channel α1-subunit using evolutionary modeling.

Proceedings of the National Academy of Sciences of the United States of America - 11 Aug 2026

Tang Xuechen, Hermenean Horia C, Yakimchyk Alesia, Tuluc Petronel, Ortner Nadine J, Liedl Klaus R

Abstract excerpt

Voltage-gated calcium channels (VGCCs) regulate differentiation, function, and survival of excitable cells, and pathogenic variants cause diverse disorders. Most known disease-associated VGCC mutations affect well-characterized regions controlling voltage-dependent gating and channel kinetics, while many residues remain functionally unannotated. We developed an evolutionary model to predict the pathogenic...

Topics

Join the communities discussing this publication.

Amino Acid Sequence
Calcium Channels, L-Type
Evolution, Molecular
Ion Channel Gating
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Open in PubMed Open full text

Identifiers

PMID: 42546191
DOI: 10.1073/pnas.2602636123
PMCID: PMC13462451

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of novel functional sites in the Cav1.3 calcium channel α1-subunit using evolutionary modeling.PMID 42546191Read ↗

Role of a conserved glutamine in the function of voltage-gated Ca2+ channels revealed by a mutation in human CACNA1D.Semantic proximity Read ↗

Mapping Structural Distribution and Gating-Property Impacts of Disease-Associated Missense Mutations in Voltage-Gated Sodium ChannelsSemantic proximity Read ↗

CACNA1I gain-of-function mutations differentially affect channel gating and cause neurodevelopmental disorders.Semantic proximity Read ↗

Kv3.1 channelopathy: a novel loss-of-function variant and the mechanistic basis of its clinical phenotypesSemantic proximity Read ↗

Conserved patterns across ion channels correlate with variant pathogenicity and clinical phenotypes.Semantic proximity Read ↗

Voltage-Gated Ca2+-Channel α1-Subunit de novo Missense Mutations: Gain or Loss of Function – Implications for Potential TherapiesSemantic proximity Read ↗

Voltage-gated calcium channels in genetic diseases.Semantic proximity Read ↗

Conserved patterns across ion channels correlate with variant pathogenicity and clinical phenotypesSemantic proximity Read ↗

Whole Exome Sequencing Identifies a Heterozygous Variant in the Cav1.3 Gene CACNA1D Associated with Familial Sinus Node Dysfunction and Focal Idiopathic EpilepsySemantic proximity Read ↗

Gating defects of disease-causing de novo mutations in Cav1.3 Ca2+ channelsSemantic proximity Read ↗

Structure-based assessment of disease-related mutations in human voltage-gated sodium channels.Semantic proximity Read ↗

Optimizing clinical interpretability of functional evidence in epilepsy-related ion channel variantsSemantic proximity Read ↗

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