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

Identification of a disulfide bridge essential for structure and function of the voltage-gated Ca(2+) channel α(2)δ-1 auxiliary subunit.

Cell calcium - 1 Jan 2012

Calderón-Rivera Aida, Andrade Arturo, Hernández-Hernández Oscar, González-Ramírez Ricardo, Sandoval Alejandro, Rivera Manuel, Gomora Juan Carlos, Felix Ricardo

Abstract excerpt

Voltage-gated calcium (Ca(V)) channels are transmembrane proteins that form Ca(2+)-selective pores gated by depolarization and are essential regulators of the intracellular Ca(2+) concentration. By providing a pathway for rapid Ca(2+) influx, Ca(V) channels couple membrane depolarization to a wide array of cellular responses including neurotransmission, muscle contraction and gene expression. Ca(V) channels fall...

Read the complete abstract on PubMed

Topics

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

Share to Calcium Channels
Share to Calcium Channels, L-Type

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine

Share to Disulfides

Share to Ion Channel Gating

Share to Mutant Proteins

Share to Protein Subunits

Share to Rabbits

Source

Open in PubMed Open full text

Identifiers

PMID: 22054663
DOI: 10.1016/j.ceca.2011.10.002
PMCID: PMC5457164

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

Identification of a disulfide bridge essential for structure and function of the voltage-gated Ca(2+) channel α(2)δ-1 auxiliary subunit.PMID 22054663Read ↗

Identification of the cysteine residue responsible for disulfide linkage of Na+ channel α and β2 subunits.Semantic proximity Read ↗

Two critical cysteine residues implicated in disulfide bond formation and proper folding of Kir2.1.Semantic proximity Read ↗

The role of a voltage-dependent Ca2+ channel intracellular linker: a structure-function analysis.Semantic proximity Read ↗

Oxidant regulated inter-subunit disulfide bond formation between ASIC1a subunits.Semantic proximity Read ↗

Identification of an intra-molecular disulfide bond in the sodium channel β1-subunit.Semantic proximity Read ↗

Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines.Semantic proximity Read ↗

Identification of the components controlling inactivation of voltage-gated Ca2+ channels.Semantic proximity Read ↗

Functional Characterization of CaVα2δ Mutations Associated with Sudden Cardiac DeathSemantic proximity Read ↗

Differential role of the alpha1C subunit tails in regulation of the Cav1.2 channel by membrane potential, beta subunits, and Ca2+ ions.Semantic proximity Read ↗

Acidic motif responsible for plasma membrane association of the voltage-dependent calcium channel beta1b subunit.Semantic proximity Read ↗

Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1.Semantic proximity Read ↗

Intra-membrane signaling between the voltage-gated Ca2+-channel and cysteine residues of syntaxin 1A coordinates synchronous release.Semantic proximity Read ↗

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