pteridines has been researched along with sulfur in 48 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 5 (10.42) | 18.7374 |
| 1990's | 11 (22.92) | 18.2507 |
| 2000's | 21 (43.75) | 29.6817 |
| 2010's | 10 (20.83) | 24.3611 |
| 2020's | 1 (2.08) | 2.80 |
| Authors | Studies |
|---|---|
| Augier, V; Blasco, F; Chippaux, M; Giordano, G; Pommier, J | 1 |
| Bauder, R; Lingens, F; Tshisuaka, B | 1 |
| Johnson, JL; Rajagopalan, KV; Wuebbens, MM | 1 |
| Gheller, SF; Hedman, B; Hodgson, KO; Lough, SM; McDonald, JW; Newton, WE | 1 |
| Bublitz, C | 1 |
| Cotton, RG | 1 |
| Kaufman, J; Macon, JB; Wolfenden, R | 1 |
| Johnson, JL; Mize, C; Rajagopalan, KV | 1 |
| Hagen, WR; Hansen, TA; Hensgens, CM | 1 |
| Rajagopalan, KV; Wuebbens, MM | 1 |
| Johnson, JL; Pitterle, DM; Rajagopalan, KV | 1 |
| Blasco, F; Giordano, G; Magalon, A; Rothery, RA; Weiner, JH | 1 |
| Hasona, A; Ray, RM; Shanmugam, KT | 1 |
| Dismukes, GC; Gladyshev, VN; Khangulov, SV; Stadtman, TC | 1 |
| de Vries, S; Duine, JA; Luykx, DM | 1 |
| Klipp, W; Leimkühler, S | 1 |
| Fujiwara, T; Sakurai, T; Yoshimatsu, K | 1 |
| Amrani, L; Arcangeli, L; Finnerty, V; Glatigny, A; Primus, J; Scazzocchio, C | 1 |
| Brinkmann, H; Eilers, T; Hänsch, R; Hille, R; Koch, B; Mendel, RR; Nieder, J; Richter, T; Schwarz, G; Witt, C | 1 |
| Akisu, M; Arslanoglu, S; Ciriş, M; Coker, M; Darcan, S; Demirtaş, E; Gökşen, D; Kultursay, N; Tütüncüoglu, S; Yalaz, M | 1 |
| Ackerley, C; Becker, L; Salman, MS; Senger, C | 1 |
| Hänsch, R; Mendel, RR | 1 |
| Fluhr, R; Sagi, M; Scazzocchio, C | 1 |
| Dobbek, H; Gremer, L; Huber, R; Kiefersauer, R; Meyer, O | 1 |
| Holm, RH; Zhang, Y | 1 |
| Fischer, B; Mendel, RR; Nimtz, M; Otte, T; Santamaria-Araujo, JA; Schwarz, G; Wray, V | 1 |
| Ahlrichs, R; Coucouvanis, D; Han, J; Nava, P | 1 |
| Hecht, HJ; Kuper, J; Llamas, A; Mendel, RR; Schwarz, G | 1 |
| Enemark, JH; Joshi, HK | 1 |
| Nichols, JD; Rajagopalan, KV | 1 |
| Bray, RC; Eisenthal, R; Godber, BL; Harrison, R; Lowe, DJ; Mendel, RR; Schwarz, G | 1 |
| Bhachu, TS; Garner, CD; Hillier, IH; McNamara, JP | 1 |
| Leimkühler, S; Magalon, A; Neumann, M; Stöcklein, W; Walburger, A | 1 |
| Daniels, JN; Rajagopalan, KV; Schindelin, H; Wuebbens, MM | 1 |
| Chowdhury, MM; Hänzelmann, P; Lee, EY; Leimkühler, S; Nimtz, M; Schindelin, H; Schmitz, J | 1 |
| Leimkühler, S; Marelja, Z; Nimtz, M; Stöcklein, W | 1 |
| Dean, DR; Dos Santos, PC | 1 |
| Esaki, N; Kurihara, T; Leimkühler, S; Mihara, H; Urban, A; Zhang, W | 1 |
| Drew, SC; Friedrich, CG; Lubitz, W; Quentmeier, A; Reijerse, E; Rother, D | 1 |
| Mihara, H | 1 |
| Bühning, M; Dahl, JU; Denis, Y; Iobbi-Nivol, C; Jourlin-Castelli, C; Leichert, LI; Leimkühler, S; Méjean, V; Nimtz, M; Radon, C | 1 |
| Kana, BD; Mizrahi, V; Williams, M | 1 |
| Baumann, O; Dosche, C; Hille, C; Leimkühler, S; Löhmannsröben, HG; Marelja, Z; Mullick Chowdhury, M | 1 |
| Kozmin, SG; Schaaper, RM; Stepchenkova, EI | 1 |
| Black, KA; Dos Santos, PC | 1 |
| Magalon, A; Mendel, RR | 1 |
| Beilschmidt, L; Bühning, M; Leimkühler, S | 1 |
| Maruyama-Nakashita, A; Nakai, Y | 1 |
7 review(s) available for pteridines and sulfur
| Article | Year |
|---|---|
Molybdoenzymes and molybdenum cofactor in plants.
Topics: Abscisic Acid; Aldehyde Oxidase; Aldehyde Oxidoreductases; Arabidopsis Proteins; Coenzymes; Enzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductase; Nitrate Reductases; Oxidoreductases Acting on Sulfur Group Donors; Plants; Pteridines; Sulfur; Xanthine Dehydrogenase | 2002 |
[Discovery and molecular function analysis of sulfur- and selenium-eliminating enzymes crucial for biosynthesis of iron-sulfur clusters and selenoproteins].
Topics: Animals; Coenzymes; Cystathionine gamma-Lyase; Humans; Iron-Sulfur Proteins; Lyases; Metalloproteins; Molybdenum Cofactors; Pteridines; RNA, Transfer; Selenium; Selenoproteins; Sulfides; Sulfur | 2011 |
Molybdenum cofactor: a key component of Mycobacterium tuberculosis pathogenesis?
Topics: Biosynthetic Pathways; Carbon; Coenzymes; Enzymes; Metalloproteins; Molybdenum Cofactors; Mycobacterium tuberculosis; Nitrogen; Oxidation-Reduction; Pteridines; Sulfur; Virulence Factors | 2014 |
Shared-intermediates in the biosynthesis of thio-cofactors: Mechanism and functions of cysteine desulfurases and sulfur acceptors.
Topics: Bacterial Proteins; Biosynthetic Pathways; Carbon-Sulfur Lyases; Coenzymes; Cysteine; Iron-Sulfur Proteins; Metalloproteins; Models, Molecular; Molybdenum Cofactors; Protein Structure, Tertiary; Pteridines; Pyridoxal Phosphate; Sulfur | 2015 |
Biosynthesis and Insertion of the Molybdenum Cofactor.
Topics: Archaea; Bacteria; Biocatalysis; Coenzymes; Enzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogenase; Pteridines; Pterins; Sulfur; Tungsten | 2015 |
Shared Sulfur Mobilization Routes for tRNA Thiolation and Molybdenum Cofactor Biosynthesis in Prokaryotes and Eukaryotes.
Topics: Animals; Coenzymes; Escherichia coli; Escherichia coli Proteins; Humans; Metalloproteins; Models, Molecular; Molybdenum Cofactors; Protein Biosynthesis; Pteridines; RNA, Bacterial; RNA, Transfer; Sulfur | 2017 |
Biosynthesis of Sulfur-Containing Small Biomolecules in Plants.
Topics: Biosynthetic Pathways; Carbon-Sulfur Lyases; Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Molybdenum Cofactors; Plants; Pteridines; Sulfhydryl Compounds; Sulfur; Sulfurtransferases | 2020 |
41 other study(ies) available for pteridines and sulfur
| Article | Year |
|---|---|
Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli.
Topics: Blotting, Western; Coenzymes; Escherichia coli; Gene Expression; Iron; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Operon; Plasmids; Pteridines; Spectrometry, Fluorescence; Sulfur; Trypsin | 1992 |
Microbial metabolism of quinoline and related compounds. VII. Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme.
Topics: Coenzymes; Flavin-Adenine Dinucleotide; Flavoproteins; Iron; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Pseudomonas; Pteridines; Soil Microbiology; Spectrophotometry; Sulfur | 1990 |
The structure of a molybdopterin precursor. Characterization of a stable, oxidized derivative.
Topics: Alkaline Phosphatase; Animals; Chickens; Coenzymes; Escherichia coli; Intestines; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Mutation; Phosphorus; Pteridines; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfur | 1989 |
Elicitation of thiomolybdates from the iron-molybdenum cofactor of nitrogenase. Comparison with synthetic Fe-Mo-S complexes.
Topics: Azotobacter; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogenase; Oxidation-Reduction; Oxidoreductases; Pteridines; Spectrophotometry; Sulfur | 1986 |
A direct assay for liver phenylalanine hydroxylase.
Topics: Alcohols; Animals; Catalase; Chemical Phenomena; Chemistry; Colorimetry; Fluorometry; Hydrogen-Ion Concentration; Kinetics; Liver; Methods; Mixed Function Oxygenases; Oxygen; Partial Pressure; Phenylalanine; Pteridines; Rats; Sulfur | 1969 |
Phenylalanine hydroxylase of Macaca irus. Purification of two components of the enzyme.
Topics: Alcohols; Animals; Buffers; Calcium Phosphates; Chemical Precipitation; Chromatography, DEAE-Cellulose; Chromatography, Gel; Drug Stability; Electrophoresis; Ethanol; Hydrogen-Ion Concentration; Kinetics; Liver; Macaca; Methods; Mixed Function Oxygenases; Phenylalanine; Protamines; Pteridines; Quaternary Ammonium Compounds; Sulfates; Sulfhydryl Reagents; Sulfur; Sulfuric Acids | 1971 |
Ring-modified substrates of adenosine deaminases.
Topics: Adenine; Aminohydrolases; Animals; Aspergillus; Cattle; Chemical Phenomena; Chemistry; Duodenum; Electron Transport; Intestines; Kinetics; Nucleosides; Oxygen; Pteridines; Pyrimidines; Ribose; Sulfur; Thiazoles | 1969 |
Defective molybdopterin biosynthesis: clinical heterogeneity associated with molybdenum cofactor deficiency.
Topics: Adult; Coenzymes; Humans; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Purine-Pyrimidine Metabolism, Inborn Errors; Purines; Radiography; Spine; Sulfur | 1995 |
Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas.
Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Anaerobiosis; Benzyl Viologen; Coenzymes; Desulfovibrio; Electron Spin Resonance Spectroscopy; Electron Transport; Enzyme Inhibitors; Metalloproteins; Molecular Sequence Data; Molecular Weight; Molybdenum; Molybdenum Cofactors; Protein Conformation; Pteridines; Sequence Analysis; Spectrometry, Fluorescence; Substrate Specificity; Sulfur; Tungsten | 1995 |
Structural characterization of a molybdopterin precursor.
Topics: Borohydrides; Chromatography, High Pressure Liquid; Coenzymes; Escherichia coli; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metalloproteins; Molybdenum Cofactors; Organophosphorus Compounds; Oxidation-Reduction; Protein Conformation; Protein Precursors; Pteridines; Spectrophotometry, Ultraviolet; Sulfur | 1993 |
In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene.
Topics: Bacterial Proteins; Chromatography, High Pressure Liquid; Coenzymes; Escherichia coli; Metalloproteins; Molybdenum Cofactors; Organophosphorus Compounds; Protein Precursors; Pteridines; Sulfur; Sulfurtransferases | 1993 |
Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron transfer to nitrate and identification of a semiquinone radical intermediate.
Topics: Benzoquinones; Cell Membrane; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Hydroquinones; Hydroxyquinolines; Iron; Metalloproteins; Molybdenum Cofactors; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Nitrates; Oxidation-Reduction; Pteridines; Sulfur | 1997 |
Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli.
Topics: Bacterial Proteins; Chlorates; Cloning, Molecular; Coenzymes; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Formate Dehydrogenases; Genetic Complementation Test; Glucose; Hydrogen Sulfide; Hydrogenase; Metalloproteins; Methyltransferases; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nitrate Reductase; Nitrate Reductases; Plasmids; Pteridines; Restriction Mapping; Sequence Deletion; Sulfates; Sulfides; Sulfotransferases; Sulfur; Sulfurtransferases | 1998 |
Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer.
Topics: Binding Sites; Carbon Dioxide; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Escherichia coli; Formate Dehydrogenases; Formates; Hydrogenase; Iron; Metalloproteins; Molybdenum Cofactors; Multienzyme Complexes; Mutation; Oxidation-Reduction; Oxygen; Photochemistry; Protons; Pteridines; Selenium; Sulfur; Thermodynamics | 1998 |
Molybdopterin radical in bacterial aldehyde dehydrogenases.
Topics: Actinobacteria; Aldehyde Dehydrogenase; Bacterial Proteins; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Gram-Negative Aerobic Rods and Cocci; Iron; Metalloproteins; Molybdenum Cofactors; Oxidation-Reduction; Pteridines; Sulfur | 1998 |
Role of XDHC in Molybdenum cofactor insertion into xanthine dehydrogenase of Rhodobacter capsulatus.
Topics: Coenzymes; Enzyme Stability; Flavin-Adenine Dinucleotide; Genes, Bacterial; Iron; Metalloproteins; Models, Biological; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutagenesis, Insertional; Open Reading Frames; Pteridines; Rhodobacter capsulatus; Spectrometry, Fluorescence; Spectrophotometry; Sulfur; Transcription, Genetic; Xanthine Dehydrogenase | 1999 |
Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui.
Topics: Bacteria; Catalysis; Chlorates; Coenzymes; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Stability; Haloarcula marismortui; Iron; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Nitrates; Nitrites; Oxidation-Reduction; Protein Structure, Quaternary; Pteridines; Sodium Chloride; Sulfur; Thermodynamics | 2000 |
Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a mechanism for the insertion of the terminal sulphur atom in the molybdopterin cofactor.
Topics: Amino Acid Sequence; Animals; Aspergillus nidulans; Azotobacter vinelandii; Bacterial Proteins; Cloning, Molecular; Coenzymes; Drosophila melanogaster; Genes, Bacterial; Genes, Fungal; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Pteridines; Sequence Homology, Amino Acid; Sulfur | 2000 |
Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. A new player in plant sulfur metabolism.
Topics: Amino Acid Sequence; Animals; Arabidopsis; Blotting, Western; Chickens; Coenzymes; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Gene Library; Heme; Humans; Kinetics; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Nicotiana; Open Reading Frames; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Peroxisomes; Plasmids; Protein Structure, Tertiary; Pteridines; Recombinant Proteins; Sequence Homology, Amino Acid; Subcellular Fractions; Sulfur; Time Factors; Ultraviolet Rays | 2001 |
Molybdenum cofactor deficiency associated with Dandy-Walker complex.
Topics: Brain; Brain Diseases, Metabolic, Inborn; Coenzymes; Dandy-Walker Syndrome; Humans; Infant, Newborn; Magnetic Resonance Imaging; Male; Metalloproteins; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Sulfur Compounds; Uric Acid; Xanthine Dehydrogenase; Xanthines | 2001 |
New insights into the neuropathogenesis of molybdenum cofactor deficiency.
Topics: Autopsy; Coenzymes; Humans; Immunohistochemistry; Infant; Magnesium; Male; Metalloproteins; Molybdenum Cofactors; Neurodegenerative Diseases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Spectrometry, X-Ray Emission; Sulfur | 2002 |
The absence of molybdenum cofactor sulfuration is the primary cause of the flacca phenotype in tomato plants.
Topics: Abscisic Acid; Amino Acid Sequence; Arabidopsis Proteins; Base Sequence; Coenzymes; Genes, Plant; Genetic Complementation Test; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Mutation; Phenotype; Phylogeny; Pteridines; Sequence Alignment; Solanum lycopersicum; Sulfur; Sulfurtransferases | 2002 |
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
Topics: Aldehyde Oxidoreductases; Alphaproteobacteria; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Copper; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nitriles; Oxidation-Reduction; Potassium Cyanide; Pteridines; Selenium; Structure-Activity Relationship; Sulfur | 2002 |
Synthesis of a molecular Mo2Fe6S9 cluster with the topology of the PN cluster of nitrogenase by rearrangement of an edge-bridged Mo2Fe6S8 double cubane.
Topics: Biomimetic Materials; Coenzymes; Crystallography, X-Ray; Iron; Magnetic Resonance Spectroscopy; Metalloproteins; Models, Molecular; Molecular Structure; Molybdenum; Molybdenum Cofactors; Nitrogenase; Organometallic Compounds; Pteridines; Selenium Compounds; Sulfur | 2003 |
The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor.
Topics: Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Pteridines; Sulfur | 2004 |
An evaluation by density functional theory of M-M interactions in organometallic clusters with the [Fe(3)MoS(3)](2+) cores.
Topics: Catechols; Chlorides; Cluster Analysis; Cobalt; Crystallography, X-Ray; Electrons; Iron; Ligands; Models, Molecular; Molybdenum; Nitrogenase; Organometallic Compounds; Oxidation-Reduction; Pteridines; Pyridines; Sulfur | 2004 |
Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism.
Topics: Adenosine Monophosphate; Arabidopsis Proteins; Binding Sites; Calnexin; Coenzymes; Copper; Crystallization; Crystallography, X-Ray; Magnesium; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Plant Proteins; Plants; Protein Binding; Protein Structure, Tertiary; Pteridines; Sulfur | 2004 |
Geometrical control of the active site electronic structure of pyranopterin enzymes by metal-dithiolate folding: aldehyde oxidase.
Topics: Aldehyde Oxidase; Binding Sites; Coenzymes; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Protein Folding; Pteridines; Structure-Activity Relationship; Sulfur Compounds | 2004 |
In vitro molybdenum ligation to molybdopterin using purified components.
Topics: Adenosine Triphosphate; Biochemistry; Coenzymes; Dose-Response Relationship, Drug; Escherichia coli; Escherichia coli Proteins; Humans; Magnesium; Metalloproteins; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Oxidoreductases; Protein Binding; Protein Structure, Tertiary; Pteridines; Pterins; Sulfates; Sulfur; Sulfurtransferases; Time Factors; Tungsten | 2005 |
Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres.
Topics: Animals; Cattle; Coenzymes; Female; Humans; Iron; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Pteridines; Spectrum Analysis; Sulfur; Xanthine Dehydrogenase | 2005 |
The nature and function of the catalytic centres of the DMSO reductases.
Topics: Binding Sites; Catalysis; Catalytic Domain; Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Models, Molecular; Molecular Conformation; Molybdenum Cofactors; Oxidoreductases; Pteridines; Sulfur | 2005 |
Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase.
Topics: Bacterial Proteins; Carbon-Sulfur Lyases; Coenzymes; Genome, Bacterial; Genomics; Metalloproteins; Molybdenum Cofactors; Protein Interaction Mapping; Pteridines; Rhodobacter capsulatus; Sulfur; Surface Plasmon Resonance; Two-Hybrid System Techniques; Xanthine Dehydrogenase | 2007 |
Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency.
Topics: Apoproteins; Binding Sites; Catalysis; Cloning, Molecular; Coenzymes; Crystallography, X-Ray; Enzyme Precursors; Metalloproteins; Models, Molecular; Molybdenum Cofactors; Mutant Proteins; Protein Structure, Secondary; Pteridines; Staphylococcus aureus; Substrate Specificity; Sulfur; Sulfurtransferases | 2008 |
The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins.
Topics: Binding Sites; Carrier Proteins; Cell Line, Tumor; Coenzymes; Dimerization; Evolution, Molecular; Humans; Metalloproteins; Molybdenum Cofactors; Nucleotidyltransferases; Pteridines; Saccharomyces cerevisiae Proteins; Structural Homology, Protein; Sulfur; Sulfurtransferases; Thiosulfate Sulfurtransferase; Ubiquitin; Ubiquitins | 2008 |
A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.
Topics: Carbon-Sulfur Lyases; Catalysis; Coenzymes; Cytoplasm; Gene Expression Regulation; Humans; Kinetics; Metalloproteins; Models, Biological; Molybdenum Cofactors; Nucleotidyltransferases; Protein Binding; Protein Structure, Tertiary; Pteridines; Sulfur; Sulfurtransferases; Surface Plasmon Resonance; Thiosulfates | 2008 |
A newly discovered role for iron-sulfur clusters.
Topics: Biological Transport; Coenzymes; Electrons; Iron; Metalloproteins; Molybdenum Cofactors; Pteridines; Sulfur; Transcription Factors | 2008 |
IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli.
Topics: Carbon-Sulfur Lyases; Catalytic Domain; Coenzymes; Cysteine; Escherichia coli; Escherichia coli Proteins; Metalloproteins; Molybdenum Cofactors; Nucleotidyltransferases; Protein Binding; Pteridines; Species Specificity; Sulfur; Sulfur Compounds; Sulfurtransferases; Surface Plasmon Resonance | 2010 |
Spectroscopic characterization of the molybdenum cofactor of the sulfane dehydrogenase SoxCD from Paracoccus pantotrophus.
Topics: Catalytic Domain; Chlorides; Coenzymes; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Ligands; Metalloproteins; Molybdenum Cofactors; Paracoccus pantotrophus; Pteridines; Sulfur | 2011 |
The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis.
Topics: Carbon-Sulfur Lyases; Coenzymes; Electrophoresis, Gel, Two-Dimensional; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Iron-Sulfur Proteins; Metalloproteins; Models, Biological; Molybdenum Cofactors; Mutation; Oligonucleotide Array Sequence Analysis; Pteridines; RNA, Transfer; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfhydryl Compounds; Sulfides; Sulfur; Surface Plasmon Resonance; Transcription, Genetic | 2013 |
The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.
Topics: Carbon-Sulfur Lyases; Coenzymes; Cysteine; Cytosol; Fluorescence Resonance Energy Transfer; Green Fluorescent Proteins; HeLa Cells; Humans; Metalloproteins; Microscopy, Fluorescence; Molybdenum Cofactors; Mutant Proteins; Neurospora; Nitrate Reductase; Nucleotidyltransferases; Protein Interaction Mapping; Protein Transport; Pteridines; Recombinant Fusion Proteins; Subcellular Fractions; Sulfur; Sulfurtransferases; Surface Plasmon Resonance | 2013 |
TusA (YhhP) and IscS are required for molybdenum cofactor-dependent base-analog detoxification.
Topics: Adenine; Anaerobiosis; Carbon-Sulfur Lyases; Chlorates; Coenzymes; Cysteine; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Metalloproteins; Molybdenum Cofactors; Mutagens; Mutation; Pteridines; Signal Transduction; Sulfur | 2013 |