ReviewThe Biochemical journal2001
Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum.
Review in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 187 citations in OpenAlex.
- Dominant rhabdomyolysis linked to a recurrent ATP2A2 variant reducing SERCA2 function in muscle.Brain : a journal of neurology · 2025Article
- Anti-Virulence Properties of Curcumin/CuO-NPs and Their Role in Accelerating Wound Healing In Vivo.Medicina (Kaunas, Lithuania) · 2025Article
- Research progress on endoplasmic reticulum homeostasis in acute kidney injury.Frontiers in pharmacology · 2025Review
- Factors that influence the Na/K-ATPase signaling and function.Frontiers in pharmacology · 2025Review
- Organelle abnormalities in Alzheimer's disease.Organelle (Tucson, Ariz.) · 2025Article
- Rescuing SERCA2 pump deficiency: A novel approach to improve bone mechano-responsiveness in type 2 diabetes.Mechanobiology in medicine · 2024Article
- ERMA (TMEM94) is a P-type ATPase transporter for MgMolecular cell · 2024Article
- Calcium regulation by SERC-A before and during Alzheimer diseaseBiomedica : revista del Instituto Nacional de Salud · 2023Article
- The SarcoEndoplasmic Reticulum Calcium ATPase (SERCA) pump: a potential target for intervention in aging and skeletal muscle pathologies.Skeletal muscle · 2021Review
- Highly exposed segment of the Spf1p P5A-ATPase near transmembrane M5 detected by limited proteolysis.PloS one · 2021Article
- The Physiology of the Gastric Parietal Cell.Physiological reviews · 2020Review
- Omeprazole Treatment Enhances Nitrogen Use Efficiency Through Increased Nitrogen Uptake and Assimilation in Corn.Frontiers in plant science · 2019Article
- Targeting Na/K-ATPase Signaling: A New Approach to Control Oxidative Stress.Current pharmaceutical design · 2018Review
- Proton Pump Inhibitors and Dementia: Physiopathological Mechanisms and Clinical Consequences.Neural plasticity · 2018Review
- IPCellular and molecular life sciences : CMLS · 2017Review
- Sodium potassium adenosine triphosphatase (Na/K-ATPase) as a therapeutic target for uremic cardiomyopathy.Expert opinion on therapeutic targets · 2017Review
- Reducing Cardiac Fibrosis: Na/K-ATPase Signaling Complex as a Novel Target.Cardiovascular pharmacology: open access · 2017Article
- A Benzimidazole Proton Pump Inhibitor Increases Growth and Tolerance to Salt Stress in Tomato.Frontiers in plant science · 2017Article
- P2C-Type ATPases and Their Regulation.Molecular neurobiology · 2016Review
- Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crystal structure of SERCA1a (skeletal-muscle sarcoplasmic-reticulum/endoplasmic-reticulum Ca(2+)-ATPase) has recently been determined at 2.6 A (note 1 A = 0.1 nm) resolution [Toyoshima, Nakasako, Nomura and Ogawa (2000) Nature (London) 405, 647-655]. Other P-type ATPases are thought to share key features of the ATP hydrolysis site and a central core of transmembrane helices. Outside of these most-conserved segments, structural similarities are less certain, and predicted transmembrane topology differs between subclasses. In the present review the homologous regions of several representative P-type ATPases are aligned with the SERCA sequence and mapped on to the SERCA structure for comparison. Homology between SERCA and the Na,K-ATPase is more extensive than with any other ATPase, even PMCA, the Ca(2+)-ATPase of plasma membrane. Structural features of the Na,K-ATPase are projected on to the Ca(2+)-ATPase crystal structure to assess the likelihood that they share the same fold. Homology extends through all ten transmembrane spans, and most insertions and deletions are predicted to be at the surface. The locations of specific residues are examined, such as proteolytic cleavage sites, intramolecular cross-linking sites, and the binding sites of certain other proteins. On the whole, the similarity supports a shared fold, with some particular exceptions.
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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.