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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2002, Volume 99, Issue 5, pp. 2690 - 2695
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2018, Volume 8, Issue 1, pp. 3304 - 12
The molybdenum cofactor (Moco) is a molybdenum-conjugated prosthetic group that is ubiquitously found in plants, animals, and bacteria. Moco is required for... 
MARC | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | INVOLVEMENT | NITRATE REDUCTASE | HYDROXYLATED BASE ANALOGS | Prodrugs | Oligomerization | Houses | Adenine | Molybdenum | Proteins | Conserved sequence | Next-generation sequencing | Mutagens | Hydroxylaminopurine | Bacteria | Catalysis | Crystal structure
Journal Article
Inorganic Chemistry, ISSN 0020-1669, 09/2014, Volume 53, Issue 18, pp. 9460 - 9462
Journal Article
Journal Article
Ultrasonics - Sonochemistry, ISSN 1350-4177, 01/2018, Volume 40, Issue Pt A, pp. 644 - 650
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2018, Volume 115, Issue 47, pp. 11958 - 11963
Journal Article
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 03/2017, Volume 18, Issue 3, pp. 670 - 670
The mARC (mitochondrial Amidoxime Reducing Component) proteins are recently discovered molybdenum (Mo) Cofactor containing enzymes. They are involved in the... 
Oligomers | Partners | Amidoxime | HAP | Interaction | mARC | Molybdenum | Chlamydomonas | MOLYBDENUM COFACTOR | amidoxime | COFACTOR-DEPENDENT RESISTANCE | oligomers | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CARRIER PROTEIN | CHEMISTRY, MULTIDISCIPLINARY | SULFITE OXIDASE | partners | CHLAMYDOMONAS-REINHARDTII | interaction | NITRATE REDUCTASE | HYDROXYLATED BASE ANALOGS | CYTOCHROME B | molybdenum | REDUCING COMPONENT MARC | Coenzymes - genetics | Pteridines - chemistry | Protein Multimerization | Cytochromes b5 - chemistry | Cytochromes b5 - metabolism | Pteridines - metabolism | Cytochromes b5 - genetics | Coenzymes - metabolism | Metalloproteins - metabolism | Metalloproteins - chemistry | Chlamydomonas reinhardtii - enzymology | Metalloproteins - genetics | Protein Binding | Chlamydomonas reinhardtii - metabolism | Coenzymes - chemistry | Binding Sites | Amino Acid Substitution | Cytochrome | Drugs | Reductases | Size exclusion chromatography | Cytochrome b5 | Amino acids | Biosynthesis | Proteins | Electron transport chain | Reduction | Mitochondria | NADH | Chlamydomonas reinhardtii | Hydroxylaminopurine | Chelation | Bacteria | Physiology | Enzymes | Alanine | Oligomerization | Prodrugs | RNA polymerase | Metabolism | Chemical compounds | Substrates | Mutagenesis | Mutagens | Nicotinamide adenine dinucleotide | Cytochromes | Ligands | Protein interaction | Electron transport | Reductase | Index Medicus
Journal Article
Journal Article
Journal Article
Food and Bioprocess Technology, ISSN 1935-5130, 12/2016, Volume 9, Issue 12, pp. 2046 - 2058
Journal Article