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Nature, ISSN 0028-0836, 2014, Volume 510, Issue 7503, pp. 172 - 175
Previous studies have established that the folding, structure and function of membrane proteins are influenced by their lipid environments(1-7) and that lipids... 
MYCOBACTERIUM-TUBERCULOSIS | ATOM FORCE-FIELD | MOLECULAR-DYNAMICS | MULTIDISCIPLINARY SCIENCES | COMPLEXES | PURIFICATION | ION-CHANNEL | MOBILITY-MASS SPECTROMETRY | MODEL | MSCL | WATER | Apoproteins - chemistry | Cardiolipins - pharmacology | Protein Unfolding - drug effects | Protein Conformation - drug effects | Aquaporins - chemistry | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Membrane Lipids - chemistry | Cation Transport Proteins - metabolism | Protein Folding - drug effects | Mass Spectrometry | Mycobacterium tuberculosis - chemistry | Membrane Proteins - metabolism | Ion Channels - chemistry | Phosphatidylglycerols - metabolism | Apoproteins - metabolism | Ammonia - metabolism | Models, Molecular | Aquaporins - metabolism | Escherichia coli Proteins - metabolism | Cardiolipins - metabolism | Escherichia coli - chemistry | Cardiolipins - chemistry | Phosphatidylglycerols - chemistry | Ion Channels - metabolism | Membrane Proteins - chemistry | Protein Stability - drug effects | Membrane Lipids - metabolism | Phosphatidylglycerols - pharmacology | Bacterial Proteins - metabolism | Membrane Lipids - pharmacology | Lipid Bilayers - chemistry | Cation Transport Proteins - chemistry | Escherichia coli Proteins - chemistry | Biological research | Physiological aspects | Lipids | Cooperative binding (Biochemistry) | Research | Structure | Molecular biology | Membrane proteins | Biology, Experimental | Proteins | Studies | Membranes | E coli | Binding sites | Crystal structure
Journal Article
Nature, ISSN 0028-0836, 01/2017, Volume 541, Issue 7637, pp. 421 - 424
Oligomerization of membrane proteins in response to lipid binding has a critical role in many cell-signalling pathways(1) but is often difficult to define(2)... 
SEROTONIN TRANSPORTER | OPIOID RECEPTOR ACTIVATION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | COMPLEXES | STOICHIOMETRY | MECHANISMS | MACROMOLECULAR ASSEMBLIES | MOLECULAR-DYNAMICS SIMULATIONS | BINDING | MASS-SPECTROMETRY | Cardiolipins - pharmacology | Moritella - chemistry | Receptors, G-Protein-Coupled - metabolism | Bacterial Proteins - chemistry | Sodium-Hydrogen Exchangers - metabolism | Cell Membrane - chemistry | Thermodynamics | Lipids - chemistry | Lipids - pharmacology | Cell Membrane - metabolism | Membrane Proteins - metabolism | Thermus thermophilus - chemistry | Models, Molecular | Escherichia coli Proteins - metabolism | Cardiolipins - metabolism | Binding Sites - genetics | Escherichia coli - chemistry | Cardiolipins - chemistry | Molecular Dynamics Simulation | Sodium-Hydrogen Exchangers - chemistry | Membrane Proteins - chemistry | Protein Stability - drug effects | Bacterial Proteins - metabolism | Ligands | Escherichia coli Proteins - chemistry | Mass Spectrometry - methods | Protein Multimerization - drug effects | Receptors, G-Protein-Coupled - chemistry | Oligomers | Analysis | Membrane proteins | Protein binding | Proteins | Signal transduction | Membranes | Lipids | Mass spectrometry | Cells | Crystal structure | Biological Sciences | Biochemistry | Naturvetenskap | biokemi | Natural Sciences | Biologiska vetenskaper
Journal Article
BBA - Biomembranes, ISSN 0005-2736, 04/2011, Volume 1808, Issue 4, pp. 1092 - 1102
Membrane proteins function in the diverse environment of the lipid bilayer. Experimental evidence suggests that some lipid molecules bind tightly to specific... 
Lipopolysaccharide | ω-ratio | Lipid binding | Cholesterol binding motif | MAXIMUM-LIKELIHOOD | CRYSTAL-STRUCTURE | PHYLOGENETIC ANALYSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PURIFYING SELECTION | A(2A) ADENOSINE RECEPTOR | CYTOCHROME-C-OXIDASE | BIOPHYSICS | POSITIVE SELECTION | MITOCHONDRIAL ADP/ATP CARRIER | SUBSTITUTION RATES | omega-ratio | Receptors, G-Protein-Coupled - metabolism | Sodium-Potassium-Exchanging ATPase - chemistry | Amino Acids - chemistry | Lipopolysaccharides - metabolism | Membrane Lipids - chemistry | Receptors, Adrenergic, beta-2 - chemistry | Cholesterol - chemistry | Amino Acids - metabolism | Membrane Proteins - metabolism | Binding Sites | Protein Structure, Tertiary | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Escherichia coli Proteins - metabolism | Formate Dehydrogenases - metabolism | Cardiolipins - metabolism | Cholesterol - metabolism | Cardiolipins - chemistry | Receptors, Adrenergic, beta-2 - metabolism | Biological Evolution | Sodium-Potassium-Exchanging ATPase - metabolism | Formate Dehydrogenases - chemistry | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Membrane Lipids - metabolism | Protein Binding | Lipopolysaccharides - chemistry | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli Proteins - chemistry | Receptors, G-Protein-Coupled - chemistry
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2014, Volume 111, Issue 52, pp. 18607 - 18612
Journal Article
Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, 06/2017, Volume 154, pp. 186 - 194
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 32, pp. 19853 - 19862
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4295 - 4307
The Na+-coupled betaine symporter BetP senses changes in the membrane state and increasing levels of cytoplasmic K+ during hyperosmotic stress latter via its... 
GLYCINE-BETAINE | CARRIER BETP | CONFORMATIONAL-CHANGES | SPECIFICITY | PHASE-TRANSITIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | C-TERMINAL DOMAIN | K | TRANSPORTER BETP | BIOLOGICAL-MEMBRANES | CORYNEBACTERIUM-GLUTAMICUM | Potassium - metabolism | Temperature | Detergents - chemistry | Protein Multimerization | Bacterial Proteins - chemistry | Spectroscopy, Fourier Transform Infrared | Corynebacterium glutamicum | Symporters - antagonists & inhibitors | Glucosides - chemistry | Phosphatidylinositols - metabolism | Protein Interaction Domains and Motifs | Protein Stability | Peptide Fragments - genetics | Phosphatidylglycerols - metabolism | Recombinant Proteins - metabolism | Bacterial Proteins - antagonists & inhibitors | Peptide Fragments - metabolism | Phosphatidylinositols - chemistry | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Cardiolipins - metabolism | Symporters - chemistry | Cardiolipins - chemistry | Symporters - metabolism | Potassium - chemistry | Peptide Fragments - chemistry | Phosphatidylglycerols - chemistry | Symporters - genetics | Hydrophobic and Hydrophilic Interactions | Bacterial Proteins - metabolism | Protein Conformation | Enzyme Activation | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | protein structure | attenuated total reflection (ATR) FT-IR spectroscopy | BetP | osmoregulation | Molecular Biophysics | infrared spectroscopy (IR spectroscopy) | membrane lipid | lipid bilayer | phospholipid | activation | lipid-protein interaction
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