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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
Journal Article
Science, ISSN 0036-8075, 1/2013, Volume 339, Issue 6118, pp. 452 - 456
Journal Article
Journal Article
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
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2004, Volume 279, Issue 5, pp. 3708 - 3716
Journal Article
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
Journal Article
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
Journal Article
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
Journal Article