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heme (24) 24
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electron spin resonance spectroscopy (20) 20
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sequence homology, amino acid (20) 20
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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2010, Volume 107, Issue 43, pp. 18517 - 18522
Microtubules (MTs) contribute to key processes during cell motility, including the regulation of focal adhesion turnover and the establishment and maintenance... 
Cell motility | Phosphorylation | Complementary DNA | Epithelial cells | Microtubules | Adenosine triphosphatases | Actins | Small interfering RNA | Cell membranes | Gene expression regulation | Memo protein | Receptor tyrosine kinase | Kinase-3 | Glycogen synthase | Adenomatous polyposis coli | PROTEIN | ACTIN | MULTIDISCIPLINARY SCIENCES | FIBROBLASTS | cell motility | GSK3-BETA PHOSPHORYLATION | glycogen synthase kinase-3 | ADENOMATOUS POLYPOSIS-COLI | EPITHELIAL-CELLS | APC | adenomatous polyposis coli | DYNAMICS | ENDS | receptor tyrosine kinase | BINDING | RNA, Small Interfering - genetics | Nonheme Iron Proteins - metabolism | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Nonheme Iron Proteins - antagonists & inhibitors | Receptor, ErbB-2 - metabolism | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Cell Movement - physiology | Breast Neoplasms - metabolism | Microtubules - metabolism | Adaptor Proteins, Signal Transducing - antagonists & inhibitors | Female | Cell Membrane - metabolism | Microfilament Proteins - metabolism | Microfilament Proteins - genetics | Adenomatous Polyposis Coli Protein - antagonists & inhibitors | Adenomatous Polyposis Coli Protein - genetics | Green Fluorescent Proteins - metabolism | Signal Transduction | Glycogen Synthase Kinase 3 - antagonists & inhibitors | Glycogen Synthase Kinase 3 - metabolism | Nonheme Iron Proteins - genetics | Breast Neoplasms - pathology | Models, Biological | Focal Adhesions - metabolism | Adaptor Proteins, Signal Transducing - genetics | Adenomatous Polyposis Coli Protein - metabolism | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Tyrosine | Synthesis | Glycogen | Genetic aspects | Research | Properties | Cell migration | Protein binding | Biological Sciences
Journal Article
Journal Article
Journal Article
Journal Article
Biochimie, ISSN 0300-9084, 12/2015, Volume 119, pp. 92 - 102
Coenzyme Q (Q) is an isoprenylated benzoquinone electron carrier required for electronic transport in the mitochondrial respiratory chain, shuttling electrons... 
Coenzyme Q | Phosphorylation | Coq7p | MULTISUBUNIT COMPLEX | NULL MUTANTS | COLI SHUTTLE VECTORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | COENZYME-Q BIOSYNTHESIS | RESTRICTION SITES | PARA-AMINOBENZOIC ACID | UBIQUINONE BIOSYNTHESIS | TRANSFER-RNA | GENETIC-EVIDENCE | Nonheme Iron Proteins - metabolism | Saccharomyces cerevisiae - genetics | Phylogeny | Protein Subunits - metabolism | Ubiquinone - biosynthesis | Saccharomyces cerevisiae - metabolism | Conserved Sequence | Mitochondrial Membranes - enzymology | Nonheme Iron Proteins - chemistry | Protein Subunits - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Biocatalysis | Mutagenesis, Site-Directed | Hot Temperature - adverse effects | Hydroxylation | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Mitochondrial Membranes - metabolism | Nonheme Iron Proteins - genetics | Sequence Alignment | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Protein Conformation | Protein Processing, Post-Translational | Protein Subunits - chemistry | Mutation | Saccharomyces cerevisiae - growth & development | Amino Acid Substitution | Saccharomyces cerevisiae Proteins - chemistry | Enzymes | Amino acids | Cytochrome b | Analysis | Quinone
Journal Article
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 04/2009, Volume 131, Issue 13, pp. 4872 - 4879
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2013, Volume 288, Issue 34, pp. 24590 - 24599
Journal Article
The FEBS Journal, ISSN 1742-464X, 07/2009, Volume 276, Issue 13, pp. 3669 - 3682
The nonheme iron oxygenase VioC from Streptomyces vinaceus catalyzes Fe(II)‐dependent and α‐ketoglutarate‐dependent Cβ‐hydroxylation of l‐arginine during the... 
viomycin | Cβ‐hydroxylation of l‐arginine | oxidoreductase | nonribosomal peptide synthesis | iron(II)/α‐ketoglutarate‐dependent oxygenase | Iron(II)/α-ketoglutarate- dependent oxygenase | Oxidoreductase | Viomycin | Cβ;-hydroxylation of l-arginine | Nonribosomal peptide synthesis | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | iron(II)/alpha-ketoglutarate-dependent oxygenase | C beta-hydroxylation of L-arginine | KETOGLUTARATE DIOXYGENASE | BETA-HYDROXYLATION | CLONING | ENZYMES | NONHEME IRON DIOXYGENASE | RESIDUE | CATALYTIC MECHANISM | Protein Structure, Tertiary | Catalytic Domain | Nonheme Iron Proteins - metabolism | Protein Structure, Secondary | Stereoisomerism | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Oxygenases - chemistry | Arginine - chemistry | Viomycin - biosynthesis | Nonheme Iron Proteins - genetics | Oxygenases - metabolism | Bacterial Proteins - metabolism | Streptomyces - enzymology | Anti-Bacterial Agents - biosynthesis | Molecular Structure | Oxygenases - genetics | Nonheme Iron Proteins - chemistry | Arginine - metabolism | Oxidases | Peptides | Hydroxylation | Diastereomers | Crystals | Physiological aspects | Asparagine | Structure | non-ribosomal peptide synthesis | Cβ-hydroxylation of L-arginine | α-ketoglutarate-dependent oxygenase | iron(II)
Journal Article
Biochemistry, ISSN 0006-2960, 12/2011, Volume 50, Issue 51, pp. 11058 - 11069
In all structurally characterized bacterial multicomponent monooxygenase (BMM) hydroxylase proteins, a series of hydrophobic cavities in the α-subunit trace a... 
METHANE MONOOXYGENASE | DIOXYGEN ACTIVATION | SYSTEM | DIIRON CENTER | TOLUENE/O-XYLENE MONOOXYGENASE | METHYLOCOCCUS-CAPSULATUS BATH | BIOCHEMISTRY & MOLECULAR BIOLOGY | STUTZERI OX1 | COMPONENT | BINDING | PROTEIN COMPLEX | Nonheme Iron Proteins - metabolism | Bacterial Proteins - chemistry | Mixed Function Oxygenases - metabolism | Multiprotein Complexes - genetics | Mixed Function Oxygenases - chemistry | Protein Subunits - metabolism | Multiprotein Complexes - metabolism | Copper - chemistry | Pseudomonas - enzymology | Oxygenases - metabolism | Copper - metabolism | Glycerol - chemistry | Binding Sites | Nonheme Iron Proteins - chemistry | Recombinant Proteins - metabolism | Catalytic Domain | Biocatalysis | Bacterial Proteins - genetics | Solubility | Models, Molecular | Recombinant Proteins - chemistry | Oxygenases - chemistry | Xenon - metabolism | Nonheme Iron Proteins - genetics | Multiprotein Complexes - chemistry | Glycerol - metabolism | Hydrophobic and Hydrophilic Interactions | Bacterial Proteins - metabolism | Ligands | Protein Conformation | Protein Subunits - chemistry | Xenon - chemistry | Mixed Function Oxygenases - genetics | Microbial enzymes | Analysis | Microbiological synthesis | Physiological aspects | Enzyme binding | Research | Chemical properties | Pseudomonas | Binding sites (Biochemistry) | X-ray crystallography | substrate transport | phenol hydroxylase | xenon | dioxygen
Journal Article