ArticleJournal of muscle research and cell motility1990
Coexpression of two isoforms of calsequestrin in rabbit slow-twitch muscle.
Article in Journal of muscle research and cell motility, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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Who cites it
30 citing papers in PubMed, 58 citations in OpenAlex.
- Vacuolar myopathy caused by CASQ1 p.Asp244His: pathogenic evidence from two unrelated Chinese families.Journal of human genetics · 2026Article
- Deep-time gene expression shift reveals an ancient change in avian muscle phenotypes.PLoS genetics · 2025Article
- TAM-associated CASQ1 mutants diminish intracellular CaJournal of muscle research and cell motility · 2024Article
- Article
- Single-cell RNAseq provides insight into altered immune cell populations in human fracture nonunions.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2023Article
- Constitutive assembly of Ca2+ entry units in soleus muscle from calsequestrin knockout mice.The Journal of general physiology · 2022Article
- Ablation of Calsequestrin-1, CaFrontiers in physiology · 2022Review
- Calsequestrin, a key protein in striated muscle health and disease.Journal of muscle research and cell motility · 2021Review
- Calsequestrin: a well-known but curious protein in skeletal muscle.Experimental & molecular medicine · 2020Review
- Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders.Scientific reports · 2020Article
- Calsequestrin Deletion Facilitates Hippocampal Synaptic Plasticity and Spatial Learning in Post-Natal Development.International journal of molecular sciences · 2020Article
- Characterization of fast-twitch and slow-twitch skeletal muscles of calsequestrin 2 (CASQ2)-knock out mice: unexpected adaptive changes of fast-twitch muscles only.Journal of muscle research and cell motility · 2016Article
- Identification of ferredoxin II as a major calcium binding protein in the nitrogen-fixing symbiotic bacterium Mesorhizobium loti.BMC microbiology · 2015Article
- The C-terminal calcium-sensitive disordered motifs regulate isoform-specific polymerization characteristics of calsequestrin.Biopolymers · 2015Article
- Oxidative stress, mitochondrial damage, and cores in muscle from calsequestrin-1 knockout mice.Skeletal muscle · 2015Article
- A mutation in the CASQ1 gene causes a vacuolar myopathy with accumulation of sarcoplasmic reticulum protein aggregates.Human mutation · 2014Article
- Endogenous and maximal sarcoplasmic reticulum calcium content and calsequestrin expression in type I and type II human skeletal muscle fibres.The Journal of physiology · 2013Article
- Identification of calcium binding sites on calsequestrin 1 and their implications for polymerization.Molecular bioSystems · 2013Article
- Specific effects of endurance and sprint training on protein expression of calsequestrin and SERCA in mouse skeletal muscle.Journal of muscle research and cell motility · 2012Article
- Lessons from calsequestrin-1 ablation in vivo: much more than a Ca(2+) buffer after all.Journal of muscle research and cell motility · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cardiac and fast-twitch skeletal muscle forms of the Ca2(+)-binding protein calsequestrin (CS) are the products of two different genes, both of which are transcribed in slow-twitch skeletal muscle, though at much different rates (Scott et al., 1988., Fliegel et al., 1989). We have investigated this problem more closely at the protein level, on isolated terminal cisternae (TC) of the sarcoplasmic reticulum (SR) of rabbit slow-twitch muscle, and following purification of two distinct forms of CS from whole tissue by DEAE-Cellulose chromatography and CA2(+)-dependent elution from phenyl-Sepharose. Two electrophoretically (apparent molecular mass of 64 kDa and 54 kDa, respectively), and antigenically distinct forms of CS, here shown to be related to the fast-twitch skeletal muscle and to cardiac-type isoform of CS, respectively, colocalize to junctional TC of slow-twitch muscle. The cardiac-type isoform that is expressed in slow-twitch muscle accounts for about 25% of total CS present in isolated TC, it binds Ca2+ as effectively as the major CS form, using a 45Ca-overlay technique, and it shares extensive similarities with dog cardiac CS, not only in size and antigenically, but also in pl, as well as in the DEAE-elution characteristics. No difference in behaviour with phenyl-Sepharose resin were observed between the two CS isoforms from slow-twitch muscle.(ABSTRACT TRUNCATED AT 250 WORDS)
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