ReviewJournal of muscle research and cell motility2007
Bridging the myoplasmic gap: recent developments in skeletal muscle excitation-contraction coupling.
Review in Journal of muscle research and cell motility, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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.
Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
- A bridge from the endoplasmic reticulum to the plasma membrane comes into view.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Transcriptomic characterization of the molecular mechanisms induced by RGMa during skeletal muscle nuclei accretion and hypertrophy.BMC genomics · 2022Article
- Excitation-contraction coupling in skeletal muscle: recent progress and unanswered questions.Biophysical reviews · 2020Review
- Orai1 and STIM1 in ER/PM junctions: roles in pancreatic cell function and dysfunction.American journal of physiology. Cell physiology · 2016Review
- Bridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics.The Journal of cell biology · 2014Article
- Analysis of embryonic and larval zebrafish skeletal myofibers from dissociated preparations.Journal of visualized experiments : JoVE · 2013Article
- Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channel.Biochimica et biophysica acta · 2013Review
- Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy.Nature communications · 2013Article
- Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Journal of muscle research and cell motility · 2011Review
- The β(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tail.Biophysical journal · 2011Article
- In vivo expression of G-protein beta1gamma2 dimer in adult mouse skeletal muscle alters L-type calcium current and excitation-contraction coupling.The Journal of physiology · 2010Article
- Excitation-contraction coupling and minor triadic proteins in low-frequency fatigue.Exercise and sport sciences reviews · 2010Review
- Looking for answers to EC coupling's persistent questions.The Journal of general physiology · 2010Article
- New factors contributing to dynamic calcium regulation in the skeletal muscle triad-a crowded place.Biophysical reviews · 2010Review
- Molecular basis for zinc transporter 1 action as an endogenous inhibitor of L-type calcium channels.The Journal of biological chemistry · 2009Article
- Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.The Journal of general physiology · 2009Article
- The alpha(1S) III-IV loop influences 1,4-dihydropyridine receptor gating but is not directly involved in excitation-contraction coupling interactions with the type 1 ryanodine receptor.The Journal of biological chemistry · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational coupling between the L-type voltage-gated Ca(2+) channel (or 1,4-dihydropyridine receptor; DHPR) and the ryanodine-sensitive Ca(2+) release channel of the sarcoplasmic reticulum (RyR1) is the mechanistic basis for excitation-contraction (EC) coupling in skeletal muscle. In this article, recent findings regarding the roles of the individual cytoplasmic domains (the amino- and carboxyl-termini, cytoplasmic loops I-II, II-III, and III-IV) of the DHPR alpha(1S) subunit in bi-directional communication with RyR1 will be discussed.
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What OpenQuestion holds
Registered trials
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.