ArticleBiochimica et biophysica acta2012
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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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Who cites it
34 citing papers in PubMed, 52 citations in OpenAlex.
- Pathological mutations in the phospholamban cytoplasmic region affect its topology and dynamics modulating the extent of SERCA inhibition.Biochimica et biophysica acta. Biomembranes · 2024Article
- Structural basis for allosteric control of the SERCA-Phospholamban membrane complex by CaeLife · 2021Article
- Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?Accounts of chemical research · 2021Review
- The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes.Nucleic acids research · 2021Article
- Intrinsically disordered HAX-1 regulates CaBiochimica et biophysica acta. Biomembranes · 2020Article
- TScientific reports · 2019Article
- Probing membrane protein ground and conformationally excited states using dipolar- and J-coupling mediated MAS solid state NMR experiments.Methods (San Diego, Calif.) · 2018Review
- Effect of Phosphorylation on Interactions between Transmembrane Domains of SERCA and Phospholamban.Biophysical journal · 2018Article
- Effects of the Arg9Cys and Arg25Cys mutations on phospholamban's conformational equilibrium in membrane bilayers.Biochimica et biophysica acta. Biomembranes · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Article
- Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.Biochimica et biophysica acta · 2015Article
- Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions.Biochimica et biophysica acta · 2015Article
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- EmrE dimerization depends on membrane environment.Biochimica et biophysica acta · 2014Article
- Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Biophysical journal · 2014Article
- Secondary structure, backbone dynamics, and structural topology of phospholamban and its phosphorylated and Arg9Cys-mutated forms in phospholipid bilayers utilizing 13C and 15N solid-state NMR spectroscopy.The journal of physical chemistry. B · 2014Article
- Solid state NMR: The essential technology for helical membrane protein structural characterization.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport.Structure (London, England : 1993) · 2013Article
- Solid state NMR and protein-protein interactions in membranes.Current opinion in structural biology · 2013Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments. Previously, we proposed that the conformational equilibria of PLN are central to SERCA regulation. Here, we show that these equilibria detected in micelles and bicelles are also present in native sarcoplasmic reticulum lipid membranes as probed by MAS solid-state NMR. Importantly, we found that the kinetics of conformational exchange and the extent of ground and excited states in detergent micelles and lipid bilayers are different, revealing a possible role of the membrane composition on the allosteric regulation of SERCA. Since the extent of excited states is directly correlated to SERCA inhibition, these findings open up the exciting possibility that calcium transport in the heart can be controlled by the lipid bilayer composition. This article is part of a Special Issue entitled: Membrane protein structure and function.
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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.