ArticleBiophysical journal2004
Single-molecule dynamics of the calcium-dependent activation of plasma-membrane Ca2+-ATPase by calmodulin.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 36 citations in OpenAlex.
- A single compartment model of pacemaking in dissasociated substantia nigra neurons: stability and energy analysis.Journal of computational neuroscience · 2013Article
- Plasma membrane Ca-ATPases: Targets of oxidative stress in brain aging and neurodegeneration.World journal of biological chemistry · 2010Article
- Caloxins: a novel class of selective plasma membrane Ca2+ pump inhibitors obtained using biotechnology.Pflugers Archiv : European journal of physiology · 2008Review
- Interchange of autoinhibitory domain conformations in plasma-membrane Ca2+-ATPase-calmodulin complexes.Protein science : a publication of the Protein Society · 2008Article
- Calmodulin, conformational states, and calcium signaling. A single-molecule perspective.Biochemistry · 2006Article
- Dynamics of calcium fluxes in nonexcitable cells: mathematical modeling.The Journal of membrane biology · 2006Article
- Collaborative effect of SERCA and PMCA in cytosolic calcium homeostasis in human platelets.Journal of physiology and biochemistry · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The plasma membrane calcium-ATPase (PMCA) helps to control cytosolic calcium levels by pumping out excess Ca2+. PMCA is regulated by the Ca2+ signaling protein calmodulin (CaM), which stimulates PMCA activity by binding to an autoinhibitory domain of PMCA. We used single-molecule polarization methods to investigate the mechanism of regulation of the PMCA by CaM fluorescently labeled with tetramethylrhodamine. The orientational mobility of PMCA-CaM complexes was determined from the extent of modulation of single-molecule fluorescence upon excitation with a rotating polarization. At a high Ca2+ concentration, the distribution of modulation depths reveals that CaM bound to PMCA is orientationally mobile, as expected for a dissociated autoinhibitory domain of PMCA. In contrast, at a reduced Ca2+ concentration a population of PMCA-CaM complexes appears with significantly reduced orientational mobility. This population can be attributed to PMCA-CaM complexes in which the autoinhibitory domain is not dissociated, and thus the PMCA is inactive. The presence of these complexes demonstrates the inadequacy of a two-state model of Ca2+ pump activation and suggests a regulatory role for the low-mobility state of the complex. When ATP is present, only the high-mobility state is detected, revealing an altered interaction between the autoinhibitory and nucleotide-binding domains.
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What OpenQuestion holds
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.