Evidence map›Paper›PMID 21784520›Full record

ReviewCell calcium2011

S100A1 and calmodulin regulation of ryanodine receptor in striated muscle.

Benjamin L Prosser, Erick O Hernández-Ochoa, Martin F Schneider

Open access · greenAbstract readReview
In one paragraph

Review in Cell calcium, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 51 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. TRPM6 N-Terminal CaM- and S100A1-Binding Domains.International journal of molecular sciences · 2019
    Article
  11. Article
  12. Loss of S100A1 expression leads to CaPhysiological reports · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. X-ray crystal structure of human calcium-bound S100A1.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  17. Article
  18. Review
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

Benjamin L ProsserCenter for Biomedical Engineering and Technology (BioMET), Department of Biochemistry and Molecular Biology, School of Medicine, University of Maryland, Baltimore, MD 21201, USA.
Erick O Hernández-Ochoa
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
Roles of voltage sensor, S100A1 and calmodulin in skeletal muscle Ca2+ signalingR37AR055099 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI SCHNEIDER, MARTIN F · 2012 to 2021
$3.5M
Control of Calcium Release in Skeletal Muscle FibersR01AR055099 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI SCHNEIDER, MARTIN F · 2007 to 2011
$1.7M
NIAMS NIH HHS R01 AR055099NIAMS NIH HHS R01AR055099NIAMS NIH HHS R37 AR055099NIAMS NIH HHS T32 AR007592
6 · The paper itself

Abstract

The release of Ca2+ ions from the sarcoplasmic reticulum through ryanodine receptor calcium release channels represents the critical step linking electrical excitation to muscular contraction in the heart and skeletal muscle (excitation-contraction coupling). Two small Ca2+ binding proteins, S100A1 and calmodulin, have been demonstrated to bind and regulate ryanodine receptor in vitro. This review focuses on recent work that has revealed new information about the endogenous roles of S100A1 and calmodulin in regulating skeletal muscle excitation-contraction coupling. S100A1 and calmodulin bind to an overlapping domain on the ryanodine receptor type 1 to tune the Ca2+ release process, and thereby regulate skeletal muscle function. We also discuss past, current and future work surrounding the regulation of ryanodine receptors by calmodulin and S100A1 in both cardiac and skeletal muscle, and the implications for excitation-contraction coupling.

Indexed as

Action PotentialsAmino Acid SequenceAnimalsBinding SitesCalciumCalmodulinExcitation Contraction CouplingHumansMiceMice, TransgenicMolecular Sequence DataMuscle ContractionMuscle, SkeletalProtein BindingProtein Structure, TertiaryRabbitsCalciumCalmodulinRyanodine Receptor Calcium Release ChannelS100A1 proteinS100 Proteins

Identifiers

PMID21784520
PMCPMC3185186
OpenAlexW1983556263

What OpenQuestion holds

Textmetadata
LicenceTDM
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.