ArticleThe Journal of biological chemistry2013
Novel details of calsequestrin gel conformation in situ.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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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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.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- An International Multicenter Evaluation of Inheritance Patterns, Arrhythmic Risks, and Underlying Mechanisms ofCirculation · 2020Trial
- ERG1A KScientific reports · 2025Article
- Architecture and molecular machinery of skeletal myofibers: a systematic review of the structure-function relationships.Frontiers in cell and developmental biology · 2025Review
- Article
- The Structural-Functional Crosstalk of the Calsequestrin System: Insights and Pathological Implications.Biomolecules · 2023Review
- Physiology of intracellular calcium buffering.Physiological reviews · 2023Review
- Sarcoplasmic Reticulum CaCells · 2023Review
- Excitation-contraction coupling in mammalian skeletal muscle: Blending old and last-decade research.Frontiers in physiology · 2022Review
- Structure-function relationships and modifications of cardiac sarcoplasmic reticulum Ca2+-transport.Physiological research · 2021Review
- 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
- The structure of a calsequestrin filament reveals mechanisms of familial arrhythmia.Nature structural & molecular biology · 2020Article
- The relationship between form and function throughout the history of excitation-contraction coupling.The Journal of general physiology · 2018Review
- Calsequestrin depolymerizes when calcium is depleted in the sarcoplasmic reticulum of working muscle.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Characterization of Post-Translational Modifications to Calsequestrins of Cardiac and Skeletal Muscle.International journal of molecular sciences · 2016Article
- Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Journal of muscle research and cell motility · 2015Review
- Characterization of Two Human Skeletal Calsequestrin Mutants Implicated in Malignant Hyperthermia and Vacuolar Aggregate Myopathy.The Journal of biological chemistry · 2015Article
- The couplonopathies: A comparative approach to a class of diseases of skeletal and cardiac muscle.The Journal of general physiology · 2015Review
- Activation and propagation of Ca2+ release from inside the sarcoplasmic reticulum network of mammalian skeletal muscle.The Journal of physiology · 2014Article
- CIR-Myo News: Proceedings of the 2014 Spring Padua Muscle Days: Terme Euganee and Padova (Italy), April 3-5, 2014.European journal of translational myology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Calsequestrin (CASQ) is the major component of the sarcoplasmic reticulum (SR) lumen in skeletal and cardiac muscles. This calcium-binding protein localizes to the junctional SR (jSR) cisternae, where it is responsible for the storage of large amounts of Ca(2+), whereas it is usually absent, at least in its polymerized form, in the free SR. The retention of CASQ inside the jSR is due partly to its association with other jSR proteins, such as junctin and triadin, and partly to its ability to polymerize, in a high Ca(2+) environment, into an intricate gel that holds the protein in place. In this work, we shed some light on the still poorly described in situ structure of polymerized CASQ using detailed EM images from thin sections, with and without tilting, and from deep-etched rotary-shadowed replicas. The latter directly illustrate the fundamental network nature of polymerized CASQ, revealing repeated nodal points connecting short segments of the linear polymer.
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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.