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

Modulation of cardiac Ca(V)1.2 channels by dihydropyridine and phosphatase inhibitor requires Ser-1142 in the domain III pore loop.

Proceedings of the National Academy of Sciences of the United States of America - 4 Mar 2003

Erxleben Christian, Gomez-Alegria Claudio, Darden Thomas, Mori Yasuo, Birnbaumer Lutz, Armstrong David L

Abstract excerpt

Dihydropyridine-sensitive, voltage-activated calcium channels respond to membrane depolarization with two distinct modes of activity: short bursts of very short openings (mode 1) or repetitive openings of much longer duration (mode 2). Here we show that both the dihydropyridine, BayK8644 (BayK), and the inhibitor of SerThr protein phosphatases, okadaic acid, have identical effects on the gating of the recombinant...

Read the complete abstract on PubMed

Topics

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

Share to Okadaic Acid
Share to Calcium Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calcium Channels, L-Type

Share to Electrophysiology

Share to Phosphoric Monoester Hydrolases

Share to Rabbits

Share to Serine

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 12601159
DOI: 10.1073/pnas.2628046100
PMCID: PMC151443

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

Modulation of cardiac Ca(V)1.2 channels by dihydropyridine and phosphatase inhibitor requires Ser-1142 in the domain III pore loop.PMID 12601159Read ↗

Molecular determinants of frequency dependence and Ca2+ potentiation of verapamil block in the pore region of Cav1.2.Semantic proximity Read ↗

The guanylate kinase domain of the beta-subunit of voltage-gated calcium channels suffices to modulate gating.Semantic proximity Read ↗

Inhibition of SERCA Ca2+ pumps by 2-aminoethoxydiphenyl borate (2-APB). 2-APB reduces both Ca2+ binding and phosphoryl transfer from ATP, by interfering with the pathway leading to the Ca2+-binding sites.Semantic proximity Read ↗

Conformational changes induced in voltage-gated calcium channel Cav1.2 by BayK 8644 or FPL64176 modify the kinetics of secretion independently of Ca2+ influx.Semantic proximity Read ↗

Functional properties of the CaV1.2 calcium channel activated by calmodulin in the absence of alpha2delta subunits.Semantic proximity Read ↗

Voltage-dependent dynamics of the BK channel cytosolic gating ring are coupled to the membrane-embedded voltage sensor.Semantic proximity Read ↗

A novel molecular inactivation determinant of voltage-gated CaV1.2 L-type Ca2+ channel.Semantic proximity Read ↗

The interaction between the I-II loop and the III-IV loop of Cav2.1 contributes to voltage-dependent inactivation in a beta -dependent manner.Semantic proximity Read ↗

Several structural domains contribute to the regulation of N-type calcium channel inactivation by the beta 3 subunit.Semantic proximity Read ↗

Distinct properties of amlodipine and nicardipine block of the voltage-dependent Ca2+ channels Cav1.2 and Cav2.1 and the mutant channels Cav1.2/dihydropyridine insensitive and Cav2.1/dihydropyridine sensitive.Semantic proximity Read ↗

Ca2+-dependent gating mechanisms for dSlo, a large-conductance Ca2+-activated K+ (BK) channel.Semantic proximity Read ↗

Structural basis for inhibition of a voltage-gated Ca2+ channel by Ca2+ antagonist drugs.Semantic proximity Read ↗

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