ReviewBiochemistry2008
Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.
Review in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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.
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
78 citing papers in PubMed, 120 citations in OpenAlex.
- Maturation of human cardiac organoids enables complex disease modeling and drug discovery.Nature cardiovascular research · 2025Article
- Microproteins-Discovery, structure, and function.Proteomics · 2023Review
- Structures of PKA-phospholamban complexes reveal a mechanism of familial dilated cardiomyopathy.eLife · 2022Article
- Murine neuronatin deficiency is associated with a hypervariable food intake and bimodal obesity.Scientific reports · 2021Article
- Article
- Thyroid Hormone Receptor α Mutations Cause Heart Defects in Zebrafish.Thyroid : official journal of the American Thyroid Association · 2021Article
- Established and Emerging Mechanisms in the Pathogenesis of Arrhythmogenic Cardiomyopathy: A Multifaceted Disease.International journal of molecular sciences · 2020Review
- Aberrant epigenetic silencing of neuronatin is a frequent event in human osteosarcoma.Oncotarget · 2020Article
- Effect of cadmium on essential metals and their impact on lipid metabolism in Saccharomyces cerevisiae.Cell stress & chaperones · 2020Review
- TScientific reports · 2019Article
- Nitroxyl (HNO) targets phospholamban cysteines 41 and 46 to enhance cardiac function.The Journal of general physiology · 2019Article
- General and specific interactions of the phospholipid bilayer with P-type ATPases.Biophysical reviews · 2019Review
- Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements.Journal of biomolecular NMR · 2019Article
- Coding sequences of sarcoplasmic reticulum calcium ATPase regulatory peptides and expression of calcium regulatory genes in recurrent exertional rhabdomyolysis.Journal of veterinary internal medicine · 2019Article
- Non and Epigenetic Mechanisms in Regulation of Adaptive Thermogenesis in Skeletal Muscle.Frontiers in endocrinology · 2019Article
- Effect of Phosphorylation on Interactions between Transmembrane Domains of SERCA and Phospholamban.Biophysical journal · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.Methods (San Diego, Calif.) · 2018Article
- The antiapoptotic protein HAX-1 mediates half of phospholamban's inhibitory activity on calcium cycling and contractility in the heart.The Journal of biological chemistry · 2018Article
- The Role of Sarcolipin in Muscle Non-shivering Thermogenesis.Frontiers in physiology · 2018Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Phospholamban (PLN) and sarcolipin (SLN) are two single-pass membrane proteins that regulate Ca2+-ATPase (SERCA), an ATP-driven pump that translocates calcium ions into the lumen of the sarcoplasmic reticulum, initiating muscle relaxation. Both proteins bind SERCA through intramembrane interactions, impeding calcium translocation. While phosphorylation of PLN at Ser-16 and/or Thr-17 reestablishes calcium flux, the regulatory mechanism of SLN remains elusive. SERCA has been crystallized in several different states along the enzymatic reaction coordinates, providing remarkable mechanistic information; however, the lack of high-resolution crystals in the presence of PLN and SLN limits the current understanding of the regulatory mechanism. This brief review offers a survey of our hybrid structural approach using solution and solid-state NMR methodologies to understand SERCA regulation from the point of view of PLN and SLN. These results have improved our understanding of the calcium translocation process and are the basis for designing new therapeutic approaches to ameliorate muscle malfunctions.
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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.