ReviewMethods (San Diego, Calif.)2011
Structure determination of membrane proteins in five easy pieces.
Review in Methods (San Diego, Calif.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.PloS one · 2014Article
- SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.Journal of biomolecular NMR · 2013Article
- Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013Review
- Membrane protein structure determination in membrana.Accounts of chemical research · 2013Article
- Plant High-Affinity Potassium (HKT) Transporters involved in salinity tolerance: structural insights to probe differences in ion selectivity.International journal of molecular sciences · 2013Review
- Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.Journal of biomolecular NMR · 2013Article
- Structure determination of membrane proteins by nuclear magnetic resonance spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2013Review
- Membrane protein structure determination: back to the membrane.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Improved 1H amide resonance line narrowing in oriented sample solid-state NMR of membrane proteins in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- M2 protein from influenza A: from multiple structures to biophysical and functional insights.Current opinion in virology · 2012Review
- Structure determination of a membrane protein in proteoliposomes.Journal of the American Chemical Society · 2012Article
- AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- The development of solid-state NMR of membrane proteins.Biomedical spectroscopy and imagingArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Rotational Alignment (RA) solid-state NMR provides the basis for a general method for determining the structures of membrane proteins in phospholipid bilayers under physiological conditions. Membrane proteins are high priority targets for structure determination, and are challenging for existing experimental methods. Because membrane proteins reside in liquid crystalline phospholipid bilayer membranes it is important to study them in this type of environment. The RA solid-state NMR approach we have developed can be summarized in five steps, and incorporates methods of molecular biology, biochemistry, sample preparation, the implementation of NMR experiments, and structure calculations. It relies on solid-state NMR spectroscopy to obtain high-resolution spectra and residue-specific structural restraints for membrane proteins that undergo rotational diffusion around the membrane normal, but whose mobility is otherwise restricted by interactions with the membrane phospholipids. High resolution spectra of membrane proteins alone and in complex with other proteins and ligands set the stage for structure determination and functional studies of these proteins in their native, functional 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.