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1995, 1, ISBN 9780849345319, 282
This book presents a comprehensive and coherent picture of how molecules diffuse across a liquid that is, on average, only two molecules thick. It begins by... 
Bilayer lipid membranes | Molecular Biology
Book
Journal Article
eLife, ISSN 2050-084X, 2018, Volume 7, p. e37262
One challenge in cell biology is to decipher the biophysical mechanisms governing protein enrichment on curved membranes and the resulting membrane... 
ezrin-membrane interaction | membrane curvature | C. elegans | ezrin | I-BAR domain proteins | phosphorylation | physics of living systems | cellular protrusions | DOMAIN | ERM PROTEINS | F-ACTIN BINDING | GIANT UNILAMELLAR VESICLES | NATIVE MEMBRANES | PHOSPHORYLATION | LIPID MIXTURES | BIOLOGY | DYNAMICS | QUANTITATIVE-ANALYSIS | APICAL MEMBRANE | Phosphorylation | Protein Binding - genetics | Cytoskeletal Proteins - genetics | Mutant Proteins - genetics | Mutant Proteins - metabolism | Cell Membrane - genetics | Cytoskeletal Proteins - chemistry | Protein Domains - genetics | Actins - genetics | Cell Membrane - chemistry | Mutant Proteins - chemistry | Actins - chemistry | Cytoskeletal Proteins - metabolism | Protein Conformation | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Plasma | Membranes | Ezrin | Cell membranes | Cell adhesion & migration | Membrane proteins | Proteins | Microscopy | Filaments | Actin | Cytoskeleton | ERM protein | Binding sites | Protein Binding/genetics | Actins/geneticss | Lipid Bilayers/metabolisms | Protein Domains/genetics | Cytoskeletal Proteins/chemistry | Biochemistry, Molecular Biology | Biophysics | Actins/chemistrys | Cell Membrane/genetics | Cellular Biology | Cytoskeletal Proteins/metabolism | Life Sciences | Lipid Bilayers/chemistry | Mutant Proteins/genetics | Cell Membrane/chemistry | Mutant Proteins/metabolism | Mutant Proteins/chemistry | Cell Behavior
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2018, Volume 362, Issue 6416, pp. 829 - 834
Membrane proteins reside in lipid bilayers and are typically extracted from this environment for study, which often compromises their integrity. In this work,... 
adenine nucleotide translocase | protein interaction | bacterial outer membrane | porin | proton transporting adenosine triphosphate synthase | Escherichia coli | porosity | mitochondrial membrane | fatty acid | lipid | beta sheet | protein assembly | article | taurine cattle | protein localization | chaperone | membrane protein | lipid bilayer | mass spectrometry | nonhuman | priority journal | membrane binding | OUTER-MEMBRANE | NMR | OXIDASE | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | LIPIDS | SUBUNIT | Molecular Chaperones - metabolism | Bacterial Proteins - chemistry | Porins - metabolism | Molecular Chaperones - chemistry | Proteome - chemistry | Adenine Nucleotide Translocator 1 - chemistry | Cattle | Mass Spectrometry | Mitochondrial Membranes - chemistry | Porins - chemistry | Membrane Proteins - metabolism | SEC Translocation Channels - chemistry | SEC Translocation Channels - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Adenine Nucleotide Translocator 1 - metabolism | Mitochondrial Proton-Translocating ATPases - chemistry | Mitochondrial Proton-Translocating ATPases - metabolism | Mitochondrial Membranes - metabolism | Animals | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Protein Conformation, beta-Strand | Bacterial Proteins - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli Proteins - chemistry | Proteome - metabolism | Physiological aspects | Mass spectrometry | Methods | Membrane proteins | Stoichiometry | Membranes | Outer membranes | Lipids | Translocase | Chaperones | Lipid bilayers | Proteins | Mitochondria | E coli | Bacteria | Assemblies | Adenosine triphosphate | Efflux | Inner membranes | Adenosine | Adenosine diphosphate | Membrane vesicles | Mass spectroscopy | Electron microscopy | Fatty acids | Organic chemistry | Scientific imaging | Dimers | Disruption | Proteomes | ATP | Ejection
Journal Article
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 43, pp. 17338 - 17343
The membrane protein complex between the sarcoplasmic reticulum Ca 2+ -ATPase (SERCA) and phospholamban (PLN) controls Ca 2+ transport in cardiomyocytes,... 
Chemical equilibrium | Spectroscopy | Phosphorylation | Calcium | Sarcoplasmic reticulum | Pumps | Adenosine triphosphatases | Lipids | Lipid bilayers | Spin labels | paramagnetic relaxation enhancement | HYBRID SOLUTION | MULTIDISCIPLINARY SCIENCES | MONOMERIC PHOSPHOLAMBAN | MEMBRANE-PROTEIN | protein-protein interactions | solid-state NMR | LIPID-BILAYERS | ELECTRON-PARAMAGNETIC-RESONANCE | SARCOPLASMIC-RETICULUM CA2+-ATPASE | STATE NMR-SPECTROSCOPY | CA-ATPASE | DYNAMICS | magic angle spinning | CALCIUM-PUMP | Calcium - metabolism | Allosteric Regulation | Molecular Sequence Data | Sarcoplasmic Reticulum Calcium-Transporting ATPases - chemistry | Calcium - chemistry | Membrane Lipids - chemistry | Molecular Structure | Calcium-Binding Proteins - chemistry | Calcium-Binding Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Rabbits | Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism | Magnetic Resonance Spectroscopy | Protein Structure, Secondary | Models, Molecular | Protein Interaction Mapping - methods | Animals | Membrane Lipids - metabolism | Protein Binding | Protein Conformation | Kinetics | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Mutation | Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics | Calcium-Binding Proteins - genetics | Physiological aspects | Nuclear magnetic resonance spectroscopy | Research | Endoplasmic reticulum | Methods | Membrane proteins | Biological Sciences
Journal Article
Journal Article