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Journal Article
Developmental Cell, ISSN 1534-5807, 2004, Volume 7, Issue 4, pp. 559 - 569
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/1998, Volume 95, Issue 20, pp. 11673 - 11678
Heterogenous nucleation on small molecule crystals causes a monoclinic crystal form of bacteriorhodopsin (BR) in which trimers of this membrane protein pack... 
Protons | Molecules | Nucleation | Crystals | Lipids | Trimers | Dyadic relations | Monomers | Membrane proteins | P branes | CRYSTALLIZATION | CUBIC PHASES | PURPLE MEMBRANE | PROTON RELEASE | MULTIDISCIPLINARY SCIENCES | LIGHT | RESOLUTION | SURFACE | ELECTRON-DIFFRACTION | CRYSTALLOGRAPHY | INDUCED CONFORMATIONAL-CHANGES | Bacteriorhodopsin | Lipid research | Analysis | Research | Structure | Bacteria | Membranes | Biology | Physics | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2011, Volume 108, Issue 23, pp. 9361 - 9366
Lactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated... 
Membrane transport proteins | Proteins | Hydroxyls | Escherichia coli | Atoms | Biochemistry | Sugars | Binding sites | Alkylation | Crystal structure | Membrane protein crystal structure | Bioenergetics | Sugar binding | Affinity labeling | MTS reagents | affinity labeling | MECHANISM | VESICLES | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | membrane protein crystal structure | sugar binding | MODEL | ACTIVE-TRANSPORT | MEMBRANE-TRANSPORT PROTEIN | bioenergetics | SUBSTRATE-BINDING SITE | Galactose - metabolism | Mesylates - metabolism | Substrate Specificity | Cysteine - genetics | Lactose - metabolism | Biological Transport | Membrane Transport Proteins - genetics | X-Ray Diffraction | Escherichia coli - metabolism | Membrane Transport Proteins - metabolism | Cysteine - metabolism | Monosaccharide Transport Proteins - metabolism | Monosaccharide Transport Proteins - genetics | Protein Structure, Tertiary | Crystallization | Models, Molecular | Escherichia coli Proteins - metabolism | Binding Sites - genetics | Cysteine - chemistry | Mesylates - chemistry | Symporters - chemistry | Symporters - metabolism | Membrane Transport Proteins - chemistry | Galactose - chemistry | Escherichia coli - genetics | Symporters - genetics | Escherichia coli Proteins - genetics | Protein Binding | Lactose - chemistry | Protein Conformation | Monosaccharide Transport Proteins - chemistry | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Chemical bonds | Lactose | E coli | Sugar | Index Medicus | MEMBRANE PROTEINS | SACCHAROSE | ESCHERICHIA COLI | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | LACTOSE | CRYSTAL STRUCTURE | 60 APPLIED LIFE SCIENCES | DISULFIDES | INACTIVATION | AFFINITY | COORDINATES | RESIDUES | Biological Sciences
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 34, pp. 20649 - 20659
G protein-coupled receptor kinases (GRKs) regulate cell signaling by initiating the desensitization of active G protein-coupled receptors. The two most widely... 
LOCALIZATION | ACTIVATION | POTENT | RHODOPSIN KINASE | PHOSPHORYLATION | DESENSITIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SITES | IDENTIFICATION | MOLECULAR-BASIS | EXPRESSION | Cardiovascular Agents - chemical synthesis | Heart Ventricles - cytology | Pyridines - chemistry | Molecular Sequence Data | Myocardial Contraction - drug effects | Crystallography, X-Ray | Enzyme Inhibitors - chemical synthesis | Myocytes, Cardiac - enzymology | G-Protein-Coupled Receptor Kinase 5 - chemistry | Cattle | Heart Septum - cytology | Enzyme Inhibitors - chemistry | Heart Ventricles - enzymology | Drug Design | Protein Interaction Domains and Motifs | Catalytic Domain | Gene Expression | Heart Septum - chemistry | Myocytes, Cardiac - cytology | Protein Structure, Secondary | Enzyme Inhibitors - pharmacology | Pyridines - chemical synthesis | Models, Molecular | Heart Septum - drug effects | Myocytes, Cardiac - chemistry | Heart Septum - enzymology | Cardiovascular Agents - pharmacology | Heart Ventricles - chemistry | Sequence Alignment | Animals | Myocytes, Cardiac - drug effects | Hydrogen Bonding | G-Protein-Coupled Receptor Kinase 5 - isolation & purification | Hydrophobic and Hydrophilic Interactions | Mice | Pyridines - pharmacology | Kinetics | Mutation | Paroxetine - pharmacology | G-Protein-Coupled Receptor Kinase 5 - genetics | Cardiovascular Agents - chemistry | Heart Ventricles - drug effects | Paroxetine - chemistry | Index Medicus | site-directed mutagenesis | G protein-coupled receptor kinase | x-ray crystallography | rational drug design | crystallography | membrane targeting | Signal Transduction | enzyme inhibitor | plasma membrane | protein kinase
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2012, Volume 19, Issue 7, pp. 725 - 727
Journal Article
Cell, ISSN 0092-8674, 2005, Volume 121, Issue 7, pp. 1043 - 1057
The mitochondrial respiratory Complex II or succinate:ubiquinone oxidoreductase (SQR) is an integral membrane