ArticleNature communications2011
Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes.
Article in Nature communications, 2011. 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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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.
- Membrane Phase, Charge, and Curvature Regulate α-Synuclein Binding Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Candida auris vacuolar calcium pump mediates fluconazole efflux and resistance evolution.Nature microbiology · 2026Article
- Allosteric Modulation of SERCA Pumps in Health and Disease: Structural Dynamics, Posttranslational Modifications, and Therapeutic Potential.Journal of molecular biology · 2025Review
- Dephosphorylation and ion binding in prokaryotic calcium transport.Science advances · 2024Article
- Accounting for nonuniformity of bulk-solvent: A mosaic model.Protein science : a publication of the Protein Society · 2024Article
- Solid-state NMR structure determination of a membrane protein inScience advances · 2023Article
- Unsaturated fatty acids uniquely alter aggregation rate of α-synuclein and insulin and change the secondary structure and toxicity of amyloid aggregates formed in their presence.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
- Efficient structure-factor modeling for crystals with multiple components.Acta crystallographica. Section A, Foundations and advances · 2023Article
- Multiscale molecular dynamics simulations predict arachidonic acid binding sites in human ASIC1a and ASIC3 transmembrane domains.The Journal of general physiology · 2023Article
- Unsaturation in the Fatty Acids of Phospholipids Drastically Alters the Structure and Toxicity of Insulin Aggregates Grown in Their Presence.The journal of physical chemistry letters · 2022Article
- Investigating Structural Dynamics of KCNE3 in Different Membrane Environments Using Molecular Dynamics Simulations.Membranes · 2022Article
- Article
- Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state.Science advances · 2021Article
- Tracking Membrane Protein Dynamics in Real Time.The Journal of membrane biology · 2021Review
- Sequential purification and characterization of Torpedo californica nAChR-DC supplemented with CHS for high-resolution crystallization studies.Analytical biochemistry · 2020Article
- Linking Biochemical and Structural States of SERCA: Achievements, Challenges, and New Opportunities.International journal of molecular sciences · 2020Review
- Tracking CaScience advances · 2020Article
- Structural Changes of Sarco/Endoplasmic Reticulum CaBiomolecules · 2020Article
- Article
- Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2019Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surrounding bilayer. Here, with the aid of low-resolution X-ray crystallography, we present direct structural information on membrane interfaces as delineated by lipid phosphate groups surrounding the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) in its phosphorylated and dephosphorylated Ca(2+)-free forms. The protein-lipid interactions are further analysed using molecular dynamics simulations. We find that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts. These mutually adaptive interactions allow smooth transitions through large conformational changes associated with the transport cycle of SERCA, a strategy that may be of general nature for many membrane proteins.
Indexed as
Identifiers
21556058What 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.