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1. Full Text Modulating Uranium binding affinity in engineered calmodulin EF-hand peptides: Effect of phosphorylation
by Pardoux, Romain and Sauge-Merle, Sandrine and Lemaire, David and Delangle, Pascale and Guilloreau, Luc and Adriano, Jean-Marc and Berthomieu, Catherine
PLoS ONE, ISSN 1932-6203, 08/2012, Volume 7, Issue 8, p. e41922
To improve our understanding of uranium toxicity, the determinants of uranyl affinity in proteins must be better characterized. In this work, we analyzed the... 
SPECTROSCOPY | AMINO-ACIDS | PROTEIN-KINASE CK2 | COMPLEXES | CALCIUM | BIOLOGY | GAS-PHASE | COORDINATION | URANYL-ION | SPECTRA | AQUEOUS-SOLUTION | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Calmodulin - genetics | Arabidopsis Proteins - genetics | Phosphorylation | Arabidopsis - chemistry | Calmodulin - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Casein Kinase II - genetics | Uranium - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Uranium - toxicity | Casein Kinase II - chemistry | Arabidopsis Proteins - chemistry | Protein Engineering | Protein Binding | Uranium - chemistry | Calmodulin - chemistry | Casein Kinase II - metabolism | Hydrogen-Ion Concentration | Arabidopsis thaliana | Tyrosine | Uranium | Analysis | Physiological aspects | Fluorescence | Protein kinases | Calmodulin | Protein binding | Protein kinase C | Peptides | Calcium | Toxicity | Physical chemistry | Amino acids | Biochemistry | Kinases | pH effects | Casein kinase II | Proteins | Spectrometry | Hydrogen ions | Calcium-binding protein | Catalysis | Uranium dioxide | Recombinant | Vibration | Threonine | Ion-exchange chromatography | EF-hand | Homogeneity | Affinity | Ligands | Binding sites | Life Sciences | Biomolecules | Environmental Engineering | Biochemistry, Molecular Biology | Environmental Sciences | pH
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2. Full Text Actin, Spectrin, and Associated Proteins Form a Periodic Cytoskeletal Structure in Axons
by Ke Xu and Guisheng Zhong and Xiaowei Zhuang
Science, ISSN 0036-8075, 1/2013, Volume 339, Issue 6118, pp. 452 - 456
Actin and spectrin play important roles in neurons, but their organization in axons and dendrites remains unclear. We used stochastic optical reconstruction... 
Axons | Sodium channels | Neurons | Microfilaments | Imaging | REPORTS | Periodicity | Actins | Cytoskeleton | Dendrites | Three dimensional imaging | VISUALIZATION | ORGANIZATION | CELLS | LOCALIZATION | MICROTUBULES | ANKYRIN(G) | MULTIDISCIPLINARY SCIENCES | INITIAL SEGMENT | DYNAMICS | ERYTHROCYTE-MEMBRANE SKELETON | OPTICAL RECONSTRUCTION MICROSCOPY | Rats, Wistar | Protein Multimerization | Actin Cytoskeleton - chemistry | Actins - ultrastructure | Dendrites - ultrastructure | Neurons - ultrastructure | Axons - ultrastructure | Actins - chemistry | Hippocampus - ultrastructure | Actin Capping Proteins - ultrastructure | Cytoskeleton - chemistry | Spectrin - chemistry | Neurons - chemistry | Actin Capping Proteins - chemistry | Calmodulin-Binding Proteins - ultrastructure | Cells, Cultured | Rats | Axons - chemistry | Calmodulin-Binding Proteins - chemistry | Cytoskeleton - ultrastructure | Dendrites - chemistry | Animals | Image Processing, Computer-Assisted | Microscopy, Fluorescence - methods | Sodium Channels - chemistry | Spectrin - ultrastructure | Actin Cytoskeleton - ultrastructure | Sodium Channels - ultrastructure | Properties | Actin | Proteins | Microscopy | Membranes | Circumferences | Erythrocytes | Dendritic structure
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3. Full Text Labeling proteins with fluorophore/thioamide Förster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligation
by Wissner, Rebecca F and Batjargal, Solongo and Fadzen, Colin M and Petersson, E. James
Journal of the American Chemical Society, ISSN 0002-7863, 05/2013, Volume 135, Issue 17, pp. 6529 - 6540
We have recently shown that p-cyanophenylalanine (Cnf) and a thioamide can be used as a minimally perturbing Forster resonant energy transfer (FRET) pair to... 
GENETIC-CODE | IN-VITRO | FLUORESCENCE | RECOGNITION | CALMODULIN | ALPHA-SYNUCLEIN | RAM TESTIS | E-OLEFIN | CHEMISTRY, MULTIDISCIPLINARY | PEPTIDE | PARKINSONS-DISEASE | Factor Xa - chemistry | Humans | Molecular Conformation | Amino Acids - chemistry | Aminopeptidases - chemistry | Escherichia coli - metabolism | Plasmids - genetics | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Calmodulin - chemistry | Amino Acyl-tRNA Synthetases - metabolism | Fluorescent Dyes - chemistry | Thioamides - chemistry | Aminopeptidases - genetics | Calmodulin - metabolism | Factor Xa - genetics | Protein Hydrolysates - chemistry | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - genetics | Models, Molecular | alpha-Synuclein - chemistry | Mutagenesis | Escherichia coli - genetics | Protein Binding | Bacterial Proteins - metabolism | Energy Transfer | Proteins - chemistry | Trypsin - chemistry | Amino Acid Substitution | Index Medicus
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4. Full Text Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis
by Dai, Yue and Haque, Mohammad Mahfuzul and Stuehr, Dennis J
Journal of Biological Chemistry, ISSN 0021-9258, 04/2017, Volume 292, Issue 16, pp. 6753 - 6764
The signaling molecule nitric oxide (NO) is synthesized in animals by structurally related NO synthases (NOSs), which contain NADPH/FAD-and FMN-binding... 
REDUCTASE DOMAIN | CYTOCHROME P450 OXIDOREDUCTASE | DIFLAVIN REDUCTASE | MECHANISM | STRUCTURAL BASIS | CALMODULIN | FMN | BIOCHEMISTRY & MOLECULAR BIOLOGY | DYNAMICS | NO SYNTHASE | MOTIONS | Flavoproteins - chemistry | Cross-Linking Reagents - chemistry | Nitric Oxide - chemistry | Oxidation-Reduction | Rats | Cysteine - chemistry | NADP - chemistry | Spectrophotometry, Ultraviolet | Cytochromes c - chemistry | Animals | Disulfides - chemistry | Nitric Oxide Synthase Type I - metabolism | Protein Domains | Flavins - chemistry | Sulfhydryl Compounds - chemistry | Catalysis | Kinetics | Mutation | Calmodulin - chemistry | Maleimides - chemistry | Electrons | Hydrogen-Ion Concentration | redox enzyme | nitric oxide | electron transfer | pre-steady-state kinetics | domain motion | kinetic model | cysteine-mediated cross-linking | Enzymology | flavin
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5. Full Text A Rapid Coarse Residue-Based Computational Method for X-Ray Solution Scattering Characterization of Protein Folds and Multiple Conformational States of Large Protein Complexes
by Yang, Sichun and Park, Sanghyun and Makowski, Lee and Roux, Benoît
Biophysical Journal, ISSN 0006-3495, 06/2009, Volume 96, Issue 11, pp. 4449 - 4463
We present a coarse residue-based computational method to rapidly compute the solution scattering profile from a protein with dynamical fluctuations. The... 
CYTOCHROME-C | LOW-RESOLUTION | BIOLOGICAL MACROMOLECULES | HYDRATION SHELL | BIOPHYSICS | SMALL-ANGLE SCATTERING | HUMAN TRANSFERRIN | CRYSTAL-STRUCTURE | NEUTRON-SCATTERING | ESCHERICHIA-COLI | STRUCTURE PREDICTION | Muramidase - chemistry | Viral Proteins - chemistry | Bacterial Proteins - chemistry | Elasticity | Models, Molecular | Protein Folding | bcl-X Protein - chemistry | Algorithms | Animals | X-Rays | Chickens | Databases, Protein | Transferrin - chemistry | Water - chemistry | Actins - chemistry | Protein Conformation | Acyltransferases - chemistry | Scattering, Radiation | Egg Proteins - chemistry | Proteins - chemistry | Calmodulin - chemistry | Escherichia coli Proteins - chemistry | Computer science | Chemical properties | Methods | Lysozyme | Biophysical Theory and Modeling
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6. Full Text An Intracellular Allosteric Modulator Binding Pocket in SK2 Ion Channels Is Shared by Multiple Chemotypes
by Cho, Lily T.-Y and Alexandrou, Aristos J and Torella, Rubben and Knafels, John and Hobbs, Jake and Taylor, Toni and Loucif, Alex and Konopacka, Agnieszka and Bell, Sigourney and Stevens, Edward B and Pandit, Jay and Horst, Reto and Withka, Jane M and Pryde, David C and Liu, Shenping and Young, Gareth T
Structure, ISSN 0969-2126, 04/2018, Volume 26, Issue 4, pp. 533 - 544.e3
Small conductance potassium (SK) ion channels define neuronal firing rates by conducting the after-hyperpolarization current. They are key targets in... 
KCa | CyPPA | SK2 | structure-based drug discovery | ion channels | riluzole | RILUZOLE | ATAXIA TYPE-2 | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CA2+-ACTIVATED K+ CHANNELS | ACTIVATED POTASSIUM CHANNELS | CELL BIOLOGY | BIOPHYSICS | SPIKE FREQUENCY ADAPTATION | CALMODULIN | NEURONS | DRUGGABILITY | SMALL-CONDUCTANCE | Calmodulin - genetics | Small-Conductance Calcium-Activated Potassium Channels - genetics | Allosteric Regulation | Humans | Crystallography, X-Ray | Pyrimidines - chemistry | Pyrimidines - metabolism | Indoles - metabolism | Pyrazoles - chemistry | Oximes - metabolism | Cloning, Molecular | Escherichia coli - metabolism | HEK293 Cells | Protein Interaction Domains and Motifs | Calmodulin - chemistry | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Calmodulin - metabolism | Genetic Vectors - chemistry | Anticonvulsants - metabolism | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Pyrazoles - metabolism | Small-Conductance Calcium-Activated Potassium Channels - chemistry | Small-Conductance Calcium-Activated Potassium Channels - metabolism | Amino Acid Motifs | Oximes - chemistry | Escherichia coli - genetics | Riluzole - chemistry | Anticonvulsants - chemistry | Protein Binding | Riluzole - metabolism | Indoles - chemistry | Neurosciences | Amines | Neurons | Epilepsy | Ion channels | Drug discovery | Calcium-binding proteins | Calmodulin
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7. Full Text Effects of Metal Ion Adduction on the Gas-Phase Conformations of Protein Ions
by Flick, Tawnya G and Merenbloom, Samuel I and Williams, Evan R
Journal of The American Society for Mass Spectrometry, ISSN 1044-0305, 11/2013, Volume 24, Issue 11, pp. 1654 - 1662
Changes in protein ion conformation as a result of nonspecific adduction of metal ions to the protein during electrospray ionization (ESI) from aqueous... 
Biotechnology | Chemistry | Analytical Chemistry | Ion mobility spectrometry | Electrospray ionization | Proteomics | Nonspecific adduction | Bioinformatics | Protein–metal interactions | Protein | Organic Chemistry | Conformation | Protein-metal interactions | CHEMISTRY, ANALYTICAL | METALLOPROTEINS | COMPLEXES | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, PHYSICAL | PEPTIDES | SPECTROSCOPY | CALMODULIN | CALCIUM-BINDING | ALPHA-LACTALBUMIN | STRUCTURAL TRANSITIONS | IONIZATION MASS-SPECTROMETRY | IRMPD SPECTROSCOPY | ELECTROSPRAY-IONIZATION | Cations, Divalent - chemistry | Cytochromes c - chemistry | Gases - chemistry | Ions - chemistry | Metals - chemistry | Solutions | Spectrometry, Mass, Electrospray Ionization - methods | Lactalbumin - chemistry | Ubiquitin - chemistry | Protein Conformation | Proteins - chemistry | Proteins | Ionization | Protein binding | Metals | Ionic mobility | Ions | Cases (containers) | Ion charge | Aqueous solutions | Cations | Cross sections | Elongation | Adducts | Metal ions
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8. Full Text Characterization of the Protein Kinase Activity of TRPM7/ChaK1, a Protein Kinase Fused to the Transient Receptor Potential Ion Channel
by Lillia V. Ryazanova and Maxim V. Dorovkov and Athar Ansari and Alexey G. Ryazanov
Journal of Biological Chemistry, ISSN 0021-9258, 01/2004, Volume 279, Issue 5, pp. 3708 - 3716
Channel-kinase TRPM7/ChaK1 is a member of a recently discovered family of protein kinases called α-kinases that display no sequence homology to conventional... 
DICTYOSTELIUM | SECONDARY HYPOCALCEMIA | MECHANISM | TYROSINE KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DIVALENT METAL CATION | CATALYTIC DOMAIN | HEAVY-CHAIN KINASE | ELONGATION FACTOR-2 KINASE | MIC CHANNELS | FAMILY | Phosphorylation | Threonine - chemistry | Histones - chemistry | Humans | Protein-Serine-Threonine Kinases | Electrophysiology | Molecular Sequence Data | Protein Kinases - chemistry | Ion Channels - physiology | Zinc - chemistry | Calcium - chemistry | Dose-Response Relationship, Drug | Phosphoamino Acids - chemistry | Time Factors | Membrane Proteins - physiology | Acetophenones - pharmacology | Escherichia coli - metabolism | TRPM Cation Channels | Benzopyrans - pharmacology | Calmodulin - chemistry | Ion Channels - chemistry | Protein Structure, Tertiary | Catalytic Domain | Electrophoresis, Polyacrylamide Gel | Enzyme Inhibitors - pharmacology | Ions | Magnesium - pharmacology | Serine - chemistry | DNA - chemistry | Magnesium - chemistry | Membrane Proteins - chemistry | Protein Kinases - physiology | Cations | HeLa Cells | Kinetics | Chromatography, Gel | Cobalt - chemistry | Staurosporine - pharmacology | Myelin Basic Protein - physiology
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9. Full Text Structure-function analysis of core STRIPAK proteins: A signaling complex implicated in Golgi polarization
by Kean, Michelle J and Ceccarelli, Derek F and Goudreault, Marilyn and Sanches, Mario and Tate, Stephen and Larsen, Brett and Gibson, Lucien C. D and Derry, W. Brent and Scott, Ian C and Pelletier, Laurence and Baillie, George S and Sicheri, Frank and Gingras, Anne-Claude
Journal of Biological Chemistry, ISSN 0021-9258, 07/2011, Volume 286, Issue 28, pp. 25065 - 25075
Cerebral cavernous malformations (CCMs) are alterations in brain capillary architecture that can result in neurological deficits, seizures, or stroke. We... 
CEREBRAL CAVERNOUS MALFORMATIONS | STRIATIN FAMILY | PHOSPHATASE 2A | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | VASCULAR INTEGRITY | KINASE | RHO GTPASES | CELL-GROWTH | SACCHAROMYCES-CEREVISIAE | GENOME-SCALE | Protein Phosphatase 2 - chemistry | Humans | Multiprotein Complexes - genetics | Proto-Oncogene Proteins - chemistry | Structure-Activity Relationship | Multiprotein Complexes - metabolism | Nerve Tissue Proteins - chemistry | HEK293 Cells | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | Golgi Apparatus - chemistry | Protein-Serine-Threonine Kinases - metabolism | Calmodulin-Binding Proteins - genetics | Proto-Oncogene Proteins - metabolism | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Protein Phosphatase 2 - genetics | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | Nerve Tissue Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Nerve Tissue Proteins - metabolism | Multiprotein Complexes - chemistry | Animals | Membrane Proteins - chemistry | Protein Phosphatase 2 - metabolism | Golgi Apparatus - metabolism | Mice | Protein-Serine-Threonine Kinases - chemistry | HeLa Cells | Golgi Apparatus - genetics | MST4 | Striatin | Signal Transduction | Mass Spectrometry (MS) | Golgi | PP2A | Serine Threonine Protein Phosphatase | Serine Threonine Protein Kinase | Cerebral Cavernous Malformations | Protein-Protein Interactions
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10. Full Text A Pyrrolysine Analogue for Protein Click Chemistry
by Fekner, Tomasz and Li, Xin and Lee, Marianne M and Chan, Michael K
Angewandte Chemie International Edition, ISSN 1433-7851, 02/2009, Volume 48, Issue 9, pp. 1633 - 1635
Ignoring the STOP sign: A pyrrolysine analogue bearing a terminal alkyne was site‐specifically incorporated into recombinant calmodulin (CaM) through a UAG... 
click chemistry | pyrrolysine | FRET | calmodulin | amino acids | Amino acids | Click chemistry | Pyrrolysine | Calmodulin | ACIDS | ESCHERICHIA-COLI | ALDEHYDES | CHEMISTRY, MULTIDISCIPLINARY | TRANSFER-RNA SYNTHETASES | CYCLOADDITION | GENETIC-CODE | RESIDUE | UAG | EFFICIENT | BACTERIAL-CELLS | Calmodulin - genetics | Lysine - analogs & derivatives | Calmodulin - biosynthesis | Codon, Terminator - genetics | Recombinant Proteins - chemistry | Alkynes - chemistry | Azides - chemistry | Copper - chemistry | Fluorescence Resonance Energy Transfer | Lysine - chemical synthesis | Catalysis | Calmodulin - chemistry | Lysine - chemistry | Azides - chemical synthesis
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11. Full Text A comprehensive search for calcium binding sites critical for TMEM16A calcium-activated chloride channel activity
by Tien, J and Peters, CJ and Wong, XM and Cheng, T and Jan, YN and Jan, LY and Yang, HH
ELIFE, ISSN 2050-084X, 06/2014, Volume 3
physiological processes such as the secretions of airway epithelia and exocrine glands, the contraction of smooth muscles, and the excitability of neurons.... 
TOPOLOGY | DOMAIN | VOLTAGE | MECHANISM | POTASSIUM CHANNELS | BK CHANNELS | CALMODULIN | CA2+/CALMODULIN | BIOLOGY | K+ CHANNEL | CATIONS | Anoctamin-1 | Solvents - chemistry | Humans | Electrophysiology | Molecular Sequence Data | Alanine - chemistry | Calcium - chemistry | HEK293 Cells | Calmodulin - chemistry | Green Fluorescent Proteins - chemistry | Binding Sites | Amino Acid Sequence | Chloride Channels - chemistry | Oxidation-Reduction | Drosophila | Xenopus laevis | Gene Expression Regulation | Ions | Neoplasm Proteins - chemistry | Cysteine - chemistry | Strontium - chemistry | Sequence Homology, Amino Acid | Animals | Mutagenesis | Mice | Mutation | Data analysis | Calcium channels | Channel gating | Glands | Excitability | Amino acids | Secretions | Muscle contraction | Contraction | Chloride channels (calcium-gated) | Calcium chloride | Exocrine glands | Respiratory tract | Proteins | Calcium-binding protein | Polarity | Physiology | Redox potential | Gating | Binding sites | Cytoplasm
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12. Full Text Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5
by Liu, Shanshan and Moulton, Kevin Ryan and Auclair, Jared Robert and Zhou, Zhaohui Sunny
Amino Acids, ISSN 0939-4451, 4/2016, Volume 48, Issue 4, pp. 1059 - 1067
Common yet often overlooked, deamidation of peptidyl asparagine (Asn or N) generates aspartic acid (Asp or D) or isoaspartic acid (isoAsp or isoD). Being a... 
Biochemistry, general | Isoaspartic acid | Isomerization | Neurobiology | Deamidation | Exenatide | Artifact | Life Sciences | Analytical Chemistry | Adrenocorticotropic hormone | Life Sciences, general | Biochemical Engineering | Proteomics | Mass spectrometry | Glu-C | Calmodulin | PROTEIN ISOASPARTATE METHYLTRANSFERASE | SAMPLE PREPARATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECOMBINANT MONOCLONAL-ANTIBODY | ELECTRON-TRANSFER DISSOCIATION | CHEMICAL PATHWAYS | TISSUE-PLASMINOGEN-ACTIVATOR | LIQUID-CHROMATOGRAPHY | PEPTIDE DEGRADATION | MASS-SPECTROMETRY ANALYSIS | ASPARAGINE RESIDUES | Amino Acid Sequence | Peptides - chemistry | Adrenocorticotropic Hormone - chemistry | Serine Endopeptidases - chemistry | Artifacts | Animals | Isoaspartic Acid - chemistry | Solutions | Cattle | Proteolysis | Amides - chemistry | Protein Processing, Post-Translational | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Aspartic Acid - chemistry | Venoms - chemistry | Buffers | Calmodulin - chemistry | Asparagine - chemistry | Hydrogen-Ion Concentration | Post-translational modification | Peptides | ACTH | Aspartate | Proteases | Analysis | Asparagine | Carbonates | Hydrogen-ion concentration | Proteins | Bicarbonates | Amino acids | Aspartic acid | Digestion | deamidation | artifact | isomerization | mass spectrometry | calmodulin | isoaspartic acid | adrenocorticotropic hormone | exenatide
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13. Full Text The Tuberous Sclerosis Protein TSC2 Is Not Required for the Regulation of the Mammalian Target of Rapamycin by Amino Acids and Certain Cellular Stresses
by Ewan M. Smith and Stephen G. Finn and Andrew R. Tee and Gareth J. Browne and Christopher G. Proud
Journal of Biological Chemistry, ISSN 0021-9258, 05/2005, Volume 280, Issue 19, pp. 18717 - 18727
Amino acids positively regulate signaling through the mammalian target of rapamycin (mTOR). Recent work demonstrated the importance of the tuberous sclerosis... 
ELONGATION-FACTOR-2 KINASE | TRANSLATION FACTORS | RHEB | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-PRODUCTS | FACTOR 4E-BINDING PROTEIN-1 | INITIATION-FACTOR 4E | ISOLATED RAT HEPATOCYTES | BINDING | PHOSPHORYLATION SITE | MTOR | Humans | Multienzyme Complexes - metabolism | Immunoblotting | Ras Homolog Enriched in Brain Protein | Elongation Factor 2 Kinase | AMP-Activated Protein Kinases | Phosphoproteins - chemistry | Time Factors | Guanosine Triphosphate - chemistry | Guanosine Diphosphate - chemistry | Protein Synthesis Inhibitors - pharmacology | Transgenes | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | Fibroblasts - metabolism | Tumor Suppressor Proteins - metabolism | Signal Transduction | Neuropeptides - metabolism | Tumor Suppressor Proteins - physiology | Adaptor Proteins, Signal Transducing | Models, Biological | Monomeric GTP-Binding Proteins - chemistry | Glucose - chemistry | Mice | TOR Serine-Threonine Kinases | Mutation | Neuropeptides - chemistry | Protein Kinases - metabolism | Monomeric GTP-Binding Proteins - physiology | Phosphorylation | Immunoprecipitation | Amino Acids - chemistry | Neuropeptides - physiology | Dose-Response Relationship, Drug | Repressor Proteins - physiology | Amino Acids - metabolism | Carrier Proteins - chemistry | Guanine - chemistry | Protein Structure, Tertiary | Cell Line | Cells, Cultured | Gene Expression Regulation | Hydrogen Peroxide - pharmacology | Cycloheximide - pharmacology | Hydrolysis | Animals | Monomeric GTP-Binding Proteins - metabolism | Ribosomal Protein S6 - metabolism | Adenosine Triphosphate - chemistry | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | Sorbitol - pharmacology
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