ArticleBiophysical journal2017
Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins with Non-native Affinity.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 17 citations in OpenAlex.
- A Structural Context for the Mechanisms of Uncoupling Protein 1 in Brown Fat Thermogenesis.Acta physiologica (Oxford, England) · 2026Review
- Molecular determinants of inhibition of UCP1-mediated respiratory uncoupling.Nature communications · 2023Article
- Activating ligands of Uncoupling protein 1 identified by rapid membrane protein thermostability shift analysis.Molecular metabolism · 2022Article
- Structure, substrate binding, and symmetry of the mitochondrial ADP/ATP carrier in its matrix-open state.Biophysical journal · 2021Article
- Molecular Dynamics Simulations of Mitochondrial Uncoupling Protein 2.International journal of molecular sciences · 2021Article
- The mitochondrial ADP/ATP carrier exists and functions as a monomer.Biochemical Society transactions · 2020Review
- Opportunities and Challenges of Backbone, Sidechain, and RDC Experiments to Study Membrane Protein Dynamics in a Detergent-Free Lipid Environment Using Solution State NMR.Frontiers in molecular biosciences · 2019Review
- Dynamics and interactions of AAC3 in DPC are not functionally relevant.Nature structural & molecular biology · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.The journal of physical chemistry letters · 2018Article
Corrections and comments
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Authors and funding
5 authors at 5 institutions in 3 countries.
Funding
Abstract
Biophysical investigation of membrane proteins generally requires their extraction from native sources using detergents, a step that can lead, possibly irreversibly, to protein denaturation. The propensity of dodecylphosphocholine (DPC), a detergent widely utilized in NMR studies of membrane proteins, to distort their structure has been the subject of much controversy. It has been recently proposed that the binding specificity of the yeast mitochondrial ADP/ATP carrier (yAAC3) toward cardiolipins is preserved in DPC, thereby suggesting that DPC is a suitable environment in which to study membrane proteins. In this communication, we used all-atom molecular dynamics simulations to investigate the specific binding of cardiolipins to yAAC3. Our data demonstrate that the interaction interface observed in a native-like environment differs markedly from that inferred from an NMR investigation in DPC, implying that in this detergent, the protein structure is distorted. We further investigated yAAC3 solubilized in DPC and in the milder dodecylmaltoside with thermal-shift assays. The loss of thermal transition observed in DPC confirms that the protein is no longer properly folded in this environment.
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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.