Evidence map›Paper›PMID 12885639›Full record

ArticleBiophysical journal2003

Calmodulin modulates initiation but not termination of spontaneous Ca2+ sparks in frog skeletal muscle.

George G Rodney, Martin F Schneider

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 36% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Duplex signaling by CaM and Stac3 enhances CaThe Journal of general physiology · 2018
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  3. Dantrolene requires MgProceedings of the National Academy of Sciences of the United States of America · 2017
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

George G RodneyDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
Martin F Schneider
University of Maryland, Baltimore · US

Funding

Interdisciplinary Training Program Muscle BiologyT32AR007592 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI Aikaterini Kontrogianni-Konstantopoulos · 1996 to 2026
$11.7M
Training Program in Cellular &Integrative NeuroscienceT32NS007375 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI KELLER, ASAF · 1994 to 2013
$4.2M
EXCITATION-CONTRACTION COUPLING IN CUT MUSCLE FIBERSR01NS023346 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI SCHNEIDER, MARTIN F · 1985 to 2006
$2.2M
Regulation of Calcium Release by Calmodulin in MuscleF32NS044636 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI RODNEY, GEORGE G · 2002 to 2002
$38k
NIAMS NIH HHS T32 AR007592NIAMS NIH HHS T32 AR07592NINDS NIH HHS F32 NS044636NINDS NIH HHS F32 NS44636NINDS NIH HHS R01 NS023346NINDS NIH HHS R01-NS23346NINDS NIH HHS T32 NS007375
6 · The paper itself

Abstract

Calmodulin is a ubiquitous Ca(2+) sensing protein that binds to and modulates the sarcoplasmic reticulum Ca(2+) release channel, ryanodine receptor (RYR). Here we assessed the effects of calmodulin on the local Ca(2+) release properties of RYR in permeabilized frog skeletal muscle fibers. Fluorescently labeled recombinant calmodulin in the internal solution localized at the Z-line/triad region. Calmodulin (0.05-5.0 micro M) in the internal solution (free [Ca(2+)](i) approximately 50-100 nM) initiated a highly cooperative dose-dependent increase in Ca(2+) spark frequency, with a half-maximal activation (K) of 1.1 micro M, a Hill coefficient (n) of 4.2 and a fractional maximal increase in frequency (R) of 17-fold. A non-Ca(2+) binding mutant of calmodulin elicited a similar highly cooperative dose-dependent increase in spark frequency (K = 1.0 micro M; n = 3.7; R = 12-fold). Spatiotemporal properties of Ca(2+) sparks were essentially unaffected by either wild-type or mutant calmodulin. An N-terminal extension of calmodulin, (N+3)calmodulin, that binds to but does not activate RYR at nM [Ca(2+)] in sarcoplasmic reticulum vesicles, prevented the calmodulin-induced increase in spark frequency. These data suggest that exogenous Ca(2+)-free calmodulin cooperatively sensitizes the Ca(2+) release channel to open, but that Ca(2+) binding to the added calmodulin does not play a significant role in the termination of Ca(2+) sparks.

Indexed as

AnimalsCalciumCalcium SignalingCalmodulinCells, CulturedDose-Response Relationship, DrugMembrane PotentialsMuscle, SkeletalRana pipiensSaponinsSarcoplasmic ReticulumCalciumCalmodulinSaponins

Identifiers

PMID12885639
PMCPMC1303213
OpenAlexW2063253489

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.