ReviewProgress in nuclear magnetic resonance spectroscopy2018
Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics.
Review in Progress in nuclear magnetic resonance spectroscopy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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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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
16 citing papers in PubMed.
- The effects of biological crowders on fibrillization, structure, diffusion, and conformational dynamics of α-synuclein.Protein science : a publication of the Protein Society · 2024Article
- Neurodegeneration, Mitochondria, and Antibiotics.Metabolites · 2023Review
- Room for Two: The Synaptophysin/Synaptobrevin Complex.Frontiers in synaptic neuroscience · 2021Article
- The Influence of the Mixed DPC:SDS Micelle on the Structure and Oligomerization Process of the Human Cystatin C.Membranes · 2020Article
- Dynamic behaviors of α-synuclein and tau in the cellular context: New mechanistic insights and therapeutic opportunities in neurodegeneration.Neurobiology of disease · 2019Review
- Diverse Role of SNARE Protein Sec22 in Vesicle Trafficking, Membrane Fusion, and Autophagy.Cells · 2019Review
- Isotopic Labeling of Eukaryotic Membrane Proteins for NMR Studies of Interactions and Dynamics.Methods in enzymology · 2019Article
- Memprot: a program to model the detergent corona around a membrane protein based on SEC-SAXS data.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013Review
- Detergent-mediated protein aggregation.Chemistry and physics of lipids · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
- Role of detergents in conformational exchange of a G protein-coupled receptor.The Journal of biological chemistry · 2012Article
- An amphipathic alpha-helix controls multiple roles of brome mosaic virus protein 1a in RNA replication complex assembly and function.PLoS pathogens · 2009Article
- Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins.Journal of the American Chemical Society · 2008Article
- Visiting order on membrane proteins by using nanotechnology.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Solution NMR of large molecules and assemblies.Biochemistry · 2007Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
SNARE-mediated membrane fusion is a ubiquitous process responsible for intracellular vesicle trafficking, including membrane fusion in exocytosis that leads to hormone and neurotransmitter release. The proteins that facilitate this process are highly dynamic and adopt multiple conformations when they interact with other proteins and lipids as they form highly regulated molecular machines that operate on membranes. Solution NMR is an ideal method to capture high-resolution glimpses of the molecular transformations that take place when these proteins come together and work on membranes. Since solution NMR has limitations on the size of proteins and complexes that can be studied, lipid bilayer model membranes cannot be used in these approaches, so the relevant interactions are typically studied in various types of membrane-mimetics that are tractable by solution NMR methods. In this review we therefore first summarize different membrane-mimetic systems that are commonly used or that show promise for solution NMR studies of membrane-interacting proteins. We then summarize recent NMR studies on two SNARE proteins, syntaxin and synaptobrevin, and two related regulatory proteins, complexin and α-synuclein, and their interactions with membrane lipids. These studies provide a structural and dynamical framework for how these proteins might carry out their functions in the vicinity of lipid membranes. The common theme throughout these studies is that membrane interactions have major influences on the structural dynamics of these proteins that cannot be ignored when attempting to explain their functions in contemporary models of SNARE-mediated membrane fusion.
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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.