ReviewMolecules (Basel, Switzerland)2020
Protein Adsorption on Solid Supported Membranes: Monitoring the Transport Activity of P-Type ATPases.
Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Sarcolipin is a Conformation-Dependent Regulator of the Sarcoplasmic Reticulum Calcium Pump SERCA.The Journal of membrane biology · 2026Article
- On the mechanism of K+ transport through the inter-subunit tunnel of KdpFABC.The Journal of general physiology · 2026Article
- Multiscale computational genomics in Wilson disease: from atomic dynamics to clinical prediction.Frontiers in genetics · 2026Review
- The SURFEBiophysical reviews · 2025Review
- Identification and expression analysis of P-type ATPase IIIA subfamily in Puccinia Striiformis f. sp. tritici.BMC genomics · 2025Article
- Isolation of the Sarcoplasmic Reticulum CaMethods and protocols · 2023Article
- Protein Adsorption and Conformational Changes.Molecules (Basel, Switzerland) · 2021Article
- Stimulation of CaChemMedChem · 2021Article
- The CopA2-Type PFrontiers in microbiology · 2021Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
P-type ATPases are a large family of membrane transporters that are found in all forms of life. These enzymes couple ATP hydrolysis to the transport of various ions or phospholipids across cellular membranes, thereby generating and maintaining crucial electrochemical potential gradients. P-type ATPases have been studied by a variety of methods that have provided a wealth of information about the structure, function, and regulation of this class of enzymes. Among the many techniques used to investigate P-type ATPases, the electrical method based on solid supported membranes (SSM) was employed to investigate the transport mechanism of various ion pumps. In particular, the SSM method allows the direct measurement of charge movements generated by the ATPase following adsorption of the membrane-bound enzyme on the SSM surface and chemical activation by a substrate concentration jump. This kind of measurement was useful to identify electrogenic partial reactions and localize ion translocation in the reaction cycle of the membrane transporter. In the present review, we discuss how the SSM method has contributed to investigate some key features of the transport mechanism of P-type ATPases, with a special focus on sarcoplasmic reticulum Ca
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