Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 279

The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.

Ca2+-induced inhibition of the cardiac Ca2+channel depends on calmodulin

Open access
Qin, Ning, Olcese, Riccardo, Bransby, Michael, Lin, Tony, Birnbaumer, Lutz·1999·Proceedings of the National Academy of Sciences

Abstract

Ca 2+-induced inhibition of α 1C voltage-gated Ca 2+channels is a physiologically important regulatory mechanism that shortens the mean open time of these otherwise long-lasting high-voltage-activated channels. The mechanism of action of Ca 2+has been a matter of some controversy, as previous studies have proposed the involvement of a putative Ca 2+-binding EF hand in the C terminus of α 1C and/or a sequence downstream from this EF-hand motif containing a putative calmodulin (CaM)-binding IQ motif. Previously, using site directed mutagenesis, we have shown that disruption of the EF-hand motif does not remove Ca 2+inhibition. We now show that the IQ motif binds CaM and that disruption of this binding activity prevents Ca 2+inhibition. We propose that Ca 2+entering through the voltage-gated pore binds to CaM and that the Ca/CaM complex is the mediator of Ca 2+inhibition.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1073/pnas.96.5.2435

Cites

14 of 14 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 14 references

Cited by

See all 279

Metadata

Authors
Qin, N., Olcese, R., Bransby, M., Lin, T., & Birnbaumer, L.
Venue
Proceedings of the National Academy of Sciences
Published
1999-03-02
Volume
96
Issue
5
Pages
2435-2438
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2055098453
Cited by
279
References
14
FWCI
8.92
Type
journal article
Language
en
Open access
green

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Ca2+-induced inhibition of the cardiac Ca2+channel depends on calmodulin. https://app.cochat.ai/papers/10.1073/pnas.96.5.2435
The paper
Qin, N., Olcese, R., Bransby, M., Lin, T., & Birnbaumer, L. (1999). Ca2+-induced inhibition of the cardiac Ca2+channel depends on calmodulin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.5.2435

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.