pteridines and cysteine

pteridines has been researched along with cysteine in 29 studies

Research

Studies (29)

TimeframeStudies, this research(%)All Research%
pre-19902 (6.90)18.7374
1990's3 (10.34)18.2507
2000's9 (31.03)29.6817
2010's14 (48.28)24.3611
2020's1 (3.45)2.80

Authors

AuthorsStudies
Hecker, E; Marks, F1
Johnson, JL; Rajagopalan, KV1
Boles, RG; Horwich, AL; Kratz, LE; Ment, LR; Meyn, MS; Rinaldo, P1
Ishibashi, S; Matsuishi, T; Nakashima, M; Satoi, M1
Barber, MJ; Pollock, VV1
Leimkühler, S; Rajagopalan, KV1
Han, MS; Kim, DH1
KAWAI, F; MITSUDA, H; SUZUKI, Y1
García-Serres, R; Hänzelmann, P; Hernández, HL; Huynh, BH; Johnson, MK; Mendel, RR; Menzel, C; Schindelin, H1
Al-Ahaidib, L; Al-Amoudi, M; Al-Shahwan, S; Eyaid, W; Jacob, M; Osman, ME; Rahbeeni, Z; Rashed, MS; Saadallah, AA; Salih, MA; Seidahmed, MZ1
Bittner, F; Heidenreich, T; Mendel, RR; Wollers, S1
Leimkühler, S; Matthies, A; Nimtz, M1
Horn, I; Lagziel, A; Landau, D; Levartovsky, D; Naamati, MS; Peretz, H; Shalev, H; Shani, E1
Affandi, O; Afroze, B; Chen, BC; Ngu, LH; Zabedah, MY1
Esaki, N; Kurihara, T; Leimkühler, S; Mihara, H; Urban, A; Zhang, W1
Kozmin, SG; Schaaper, RM; Wang, J1
White, RH1
Chen, YC; Eric Thomas, C; Garcia, GA1
Bittner, F; Heidenreich, T; Lehrke, M; Mendel, RR; Rump, S; Wissing, J1
Leimkühler, S; Nimtz, M; Voss, M1
Ceyhan, S; Clayton, PT; Footitt, EJ; Jakobs, C; Mills, PB; Struys, EA; Waters, PJ1
Baumann, O; Dosche, C; Hille, C; Leimkühler, S; Löhmannsröben, HG; Marelja, Z; Mullick Chowdhury, M1
Kozmin, SG; Schaaper, RM; Stepchenkova, EI1
Haumann, M; Hille, R; Leimkühler, S; Niks, D; Rajagopalan, KV; Reschke, S; Sigfridsson, KG; Wilson, H1
Black, KA; Dos Santos, PC1
Dau, H; Hartmann, T; Haumann, M; Kositzki, R; Leimkühler, S; Reschke, S; Schrapers, P; Schulzke, C1
Schwarz, G1
Brueck, W; Burfeind, P; Hakroush, S; Jakubiczka-Smorag, J; Kumar, A; Metz, I; Reiss, J; Santamaria-Araujo, JA; Schwarz, G; Smorag, L1
Deutz, NEP; Engelen, MPKJ; Indika, NR; Peiris, H; Perera, R; Wijetunge, S1

Reviews

4 review(s) available for pteridines and cysteine

ArticleYear
[Molybdenum cofactor deficiency].
    Ryoikibetsu shokogun shirizu, 1998, Issue:19 Pt 2

    Topics: Biomarkers; Coenzymes; Cysteine; Diagnosis, Differential; Female; Humans; Infant; Infant, Newborn; Male; Metal Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Sulfites; Xanthine

1998
Shared-intermediates in the biosynthesis of thio-cofactors: Mechanism and functions of cysteine desulfurases and sulfur acceptors.
    Biochimica et biophysica acta, 2015, Volume: 1853, Issue:6

    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
Molybdenum cofactor and human disease.
    Current opinion in chemical biology, 2016, Volume: 31

    Topics: Coenzymes; Cysteine; Cytosol; Disease; Humans; Metalloproteins; Mitochondria; Molybdenum Cofactors; Pteridines; Sulfites; Therapeutics

2016
Sulfur amino acid metabolism and related metabotypes of autism spectrum disorder: A review of biochemical evidence for a hypothesis.
    Biochimie, 2021, Volume: 184

    Topics: Autism Spectrum Disorder; Brain; Coenzymes; Cysteine; Humans; Metalloproteins; Molybdenum Cofactors; Oxidative Stress; Pteridines; S-Adenosylmethionine

2021

Other Studies

25 other study(ies) available for pteridines and cysteine

ArticleYear
[On the metabolism and mechanism of action of estrogens. 8. The biogenesis and metabolism of 2-hydroxyestrone in relation to the formation of protein-bound and water soluble estrone metabolites and to NADPH oxidation in rat liver microsomes].
    Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 1966, Volume: 345, Issue:1

    Topics: Aminopterin; Animals; Carbon Isotopes; Cysteine; Estrone; Female; Folic Acid; Glutathione; Humans; Kinetics; Liver; Male; Microsomes; NADP; Oxidation-Reduction; Phenylalanine; Phosphates; Protein Binding; Pteridines; Rats; Steroids

1966
An HPLC assay for detection of elevated urinary S-sulphocysteine, a metabolic marker of sulphite oxidase deficiency.
    Journal of inherited metabolic disease, 1995, Volume: 18, Issue:1

    Topics: Amino Acids; Biomarkers; Chromatography, High Pressure Liquid; Coenzymes; Cysteine; Humans; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Taurine

1995
Short-term response to dietary therapy in molybdenum cofactor deficiency.
    Annals of neurology, 1993, Volume: 34, Issue:5

    Topics: Acidosis, Lactic; Coenzymes; Cysteine; Developmental Disabilities; Female; Food, Fortified; Humans; Infant; Lactates; Metabolism, Inborn Errors; Metalloproteins; Methionine; Microcephaly; Molybdenum Cofactors; Pteridines

1993
Serine 121 is an essential amino acid for biotin sulfoxide reductase functionality.
    The Journal of biological chemistry, 2000, Nov-10, Volume: 275, Issue:45

    Topics: Alanine; Amino Acid Sequence; Amino Acids; Binding Sites; Biotin; Catalysis; Chromatography, High Pressure Liquid; Coenzymes; Conserved Sequence; Cysteine; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Factor Xa; Glutathione Transferase; Guanine Nucleotides; Iron-Sulfur Proteins; Ligands; Mass Spectrometry; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Mutagenesis, Site-Directed; NADP; Oxidative Stress; Oxidoreductases; Oxygen; Paraquat; Pteridines; Pterins; Recombinant Fusion Proteins; Rhodobacter sphaeroides; Sequence Homology, Amino Acid; Serine; Spectrometry, Fluorescence; Threonine; Time Factors

2000
A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli.
    The Journal of biological chemistry, 2001, Jun-22, Volume: 276, Issue:25

    Topics: Base Sequence; Chromatography, High Pressure Liquid; Coenzymes; Cysteine; DNA Primers; Enzyme Activation; Escherichia coli; Metalloproteins; Molybdenum Cofactors; Pteridines; Sulfurtransferases

2001
Molecular probe for selective detection of thiols in water of neutral pH.
    Bioorganic & medicinal chemistry letters, 2003, Aug-04, Volume: 13, Issue:15

    Topics: Amino Acids; Cysteine; Glutathione; Hydrogen-Ion Concentration; Indicators and Reagents; Kinetics; Organometallic Compounds; Pteridines; Solutions; Spectrometry, Fluorescence; Sulfhydryl Compounds; Water

2003
BIOGENESIS OF RIBOFLAVIN IN GREEN LEAVES. V. ABSENCE OF THE EFFECT OF CYSTEINE AND ASCORBIC ACID ON THE ENZYMATIC CONVERSION OF 6,7-DIMETHYL-8-RIBITYLLUMAZINE TO RIBOFLAVIN UNDER ANAEROBIC CONDITION.
    The Journal of vitaminology, 1963, Jun-10, Volume: 9

    Topics: Ascorbic Acid; Cysteine; Metabolism; Plant Leaves; Plants; Pteridines; Research; Riboflavin; Ribonucleosides

1963
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis.
    The Journal of biological chemistry, 2004, Aug-13, Volume: 279, Issue:33

    Topics: Amino Acid Motifs; Amino Acid Sequence; Carbon-Carbon Lyases; Catalysis; Circular Dichroism; Coenzymes; Conserved Sequence; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Humans; Iron; Iron-Sulfur Proteins; Magnetics; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Mutation; Nuclear Proteins; Oxygen; Protein Structure, Tertiary; Pteridines; Sequence Homology, Amino Acid; Serine; Spectrophotometry; Spectroscopy, Mossbauer; Spectrum Analysis, Raman; Ultraviolet Rays

2004
Determination of urinary S-sulphocysteine, xanthine and hypoxanthine by liquid chromatography-electrospray tandem mass spectrometry.
    Biomedical chromatography : BMC, 2005, Volume: 19, Issue:3

    Topics: Adult; Brain Diseases, Metabolic, Inborn; Child; Child, Preschool; Chromatography, Liquid; Coenzymes; Cysteine; Humans; Hypoxanthine; Infant; Infant, Newborn; Metalloproteins; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Spectrometry, Mass, Electrospray Ionization; Xanthine

2005
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration.
    The Journal of biological chemistry, 2005, Feb-11, Volume: 280, Issue:6

    Topics: Aldehyde Oxidase; Arabidopsis; Arabidopsis Proteins; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Cysteine; Cytosol; Fluorescent Dyes; Genetic Vectors; Iron-Sulfur Proteins; Kinetics; Lyases; Lysine; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Naphthalenesulfonates; Pichia; Plant Proteins; Protein Binding; Protein Structure, Tertiary; Pteridines; Pyridoxal Phosphate; Selenocysteine; Spectrophotometry; Substrate Specificity; Sulfides; Sulfurtransferases; Xanthine Dehydrogenase

2005
Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.
    Biochemistry, 2005, May-31, Volume: 44, Issue:21

    Topics: Amino Acid Sequence; Animals; Coenzymes; Cysteine; Disulfides; Histidine; Humans; Metalloproteins; Mice; Molecular Sequence Data; Molybdenum Cofactors; Mutagenesis, Site-Directed; Nucleotidyltransferases; Peptide Mapping; Protein Structure, Tertiary; Pteridines; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Sulfhydryl Compounds; Sulfides; Sulfurtransferases; Thiosulfate Sulfurtransferase

2005
Identification and characterization of the first mutation (Arg776Cys) in the C-terminal domain of the Human Molybdenum Cofactor Sulfurase (HMCS) associated with type II classical xanthinuria.
    Molecular genetics and metabolism, 2007, Volume: 91, Issue:1

    Topics: Aldehyde Oxidase; Allopurinol; Amino Acid Sequence; Amino Acid Substitution; Arginine; Base Sequence; Coenzymes; Cysteine; Female; Homozygote; Humans; Infant, Newborn; Male; Metalloproteins; Molybdenum Cofactors; Mutation; Pedigree; Phylogeny; Protein Structure, Tertiary; Pteridines; Sequence Alignment; Sulfurtransferases; Xanthine Dehydrogenase; Xanthines

2007
Molybdenum cofactor deficiency in a Malaysian child.
    Singapore medical journal, 2009, Volume: 50, Issue:10

    Topics: Brain Diseases; Child; Coenzymes; Cysteine; Diagnosis, Differential; Humans; Hypoxanthine; Hypoxia; Ischemia; Malaysia; Male; Metalloproteins; Molybdenum Cofactors; Pteridines; Sulfites; Uric Acid; Xanthine

2009
IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli.
    The Journal of biological chemistry, 2010, Jan-22, Volume: 285, Issue:4

    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
Role for CysJ flavin reductase in molybdenum cofactor-dependent resistance of Escherichia coli to 6-N-hydroxylaminopurine.
    Journal of bacteriology, 2010, Volume: 192, Issue:8

    Topics: Adenine; Bacterial Proteins; Coenzymes; Cysteine; Drug Resistance, Bacterial; Escherichia coli; Escherichia coli Proteins; FMN Reductase; Metalloproteins; Molybdenum Cofactors; Open Reading Frames; Operon; Pteridines

2010
The twists and turns of enzyme function.
    Journal of bacteriology, 2010, Volume: 192, Issue:8

    Topics: Adenine; Bacterial Proteins; Coenzymes; Cysteine; Drug Resistance, Bacterial; Escherichia coli; Escherichia coli Proteins; FMN Reductase; Metalloproteins; Molybdenum Cofactors; Open Reading Frames; Operon; Pteridines

2010
Differential heterocyclic substrate recognition by, and pteridine inhibition of E. coli and human tRNA-guanine transglycosylases.
    Biochemical and biophysical research communications, 2011, Jun-24, Volume: 410, Issue:1

    Topics: Biopterins; Catalytic Domain; Cysteine; Escherichia coli; Guanine; Humans; Mutation; Pentosyltransferases; Protein Conformation; Pteridines; Substrate Specificity

2011
Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis.
    The Biochemical journal, 2012, Feb-01, Volume: 441, Issue:3

    Topics: Arabidopsis; Arabidopsis Proteins; Bacterial Proteins; Catalytic Domain; Coenzymes; Cysteine; Disulfides; Humans; Metalloproteins; Models, Biological; Models, Molecular; Molybdenum Cofactors; Mutagenesis, Site-Directed; Protein Binding; Protein Interaction Domains and Motifs; Protein Interaction Maps; Pteridines; Sequence Homology; Structure-Activity Relationship; Sulfides; Sulfurtransferases

2012
Elucidation of the dual role of Mycobacterial MoeZR in molybdenum cofactor biosynthesis and cysteine biosynthesis.
    PloS one, 2011, Volume: 6, Issue:11

    Topics: Amino Acid Sequence; Bacterial Proteins; Circular Dichroism; Coenzymes; Cysteine; Escherichia coli; Genes, Bacterial; Genetic Complementation Test; Kinetics; Metalloproteins; Models, Biological; Molecular Sequence Data; Molybdenum Cofactors; Mycobacterium; Nitrate Reductase; Pteridines; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Sulfurtransferases

2011
Urinary AASA excretion is elevated in patients with molybdenum cofactor deficiency and isolated sulphite oxidase deficiency.
    Journal of inherited metabolic disease, 2012, Volume: 35, Issue:6

    Topics: 2-Aminoadipic Acid; Adolescent; Amino Acid Metabolism, Inborn Errors; Child; Coenzymes; Cysteine; Humans; Infant, Newborn; L-Aminoadipate-Semialdehyde Dehydrogenase; Lysine; Metabolic Networks and Pathways; Metal Metabolism, Inborn Errors; Metalloproteins; Models, Biological; Molybdenum Cofactors; Molybdoferredoxin; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Sulfite Oxidase; Sulfites

2012
The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.
    PloS one, 2013, Volume: 8, Issue:4

    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.
    MicrobiologyOpen, 2013, Volume: 2, Issue:5

    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
Effect of exchange of the cysteine molybdenum ligand with selenocysteine on the structure and function of the active site in human sulfite oxidase.
    Biochemistry, 2013, Nov-19, Volume: 52, Issue:46

    Topics: Catalytic Domain; Coenzymes; Cysteine; Electron Spin Resonance Spectroscopy; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Selenocysteine; X-Ray Absorption Spectroscopy

2013
Sulfido and cysteine ligation changes at the molybdenum cofactor during substrate conversion by formate dehydrogenase (FDH) from Rhodobacter capsulatus.
    Inorganic chemistry, 2015, Apr-06, Volume: 54, Issue:7

    Topics: Catalytic Domain; Coenzymes; Cysteine; Formate Dehydrogenases; Formates; Ligands; Metalloproteins; Models, Molecular; Molybdenum Cofactors; Pteridines; Rhodobacter capsulatus; Sulfides

2015
Mouse model for molybdenum cofactor deficiency type B recapitulates the phenotype observed in molybdenum cofactor deficient patients.
    Human genetics, 2016, Volume: 135, Issue:7

    Topics: Animals; Apoptosis; Carbon-Carbon Lyases; Coenzymes; Cysteine; Disease Models, Animal; Gene Expression; Humans; Hypoxanthine; Metal Metabolism, Inborn Errors; Metalloproteins; Mice; Mice, Knockout; Molybdenum Cofactors; Mutation; Nuclear Proteins; Phenotype; Pteridines; Xanthine

2016