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uridine monophosphate and lysine

uridine monophosphate has been researched along with lysine in 9 studies

Research

Studies (9)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (44.44)18.2507
2000's3 (33.33)29.6817
2010's2 (22.22)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dorfman, RH; Grubmeyer, C; Ozturk, DH; Sacchettini, JC; Scapin, G1
Frey, PA; Swanson, BA1
Bendala, E; Britton, HG; Bueso, J; Cervera, J; Lusty, CJ; Nassif, Z; Rubio, V1
Fisher, BM; Raines, RT; Schultz, LW1
Ma, C; Wang, X; Xu, P1
Horii, T; Inoue, T; Kai, Y; Krungkrai, J; Krungkrai, SR; Kusakari, Y; Matsumura, H; Tokuoka, K1
Diederichsen, U; Heinrich, D; Rudolph, MG1
Buschmann, J; Jeske, M; Lilie, H; Moritz, B; Schierhorn, A; Wahle, E1
Bredeston, LM; Ebert, B; Favarolo, MB; Gonzalez Flecha, FL; Rautengarten, C; Toscanini, MA1

Other Studies

9 other study(ies) available for uridine monophosphate and lysine

ArticleYear
Locations and functional roles of conserved lysine residues in Salmonella typhimurium orotate phosphoribosyltransferase.
    Biochemistry, 1995, Aug-29, Volume: 34, Issue:34

    Topics: Base Sequence; Binding Sites; Computer Graphics; Diphosphates; Enzyme Inhibitors; Enzyme Stability; Kinetics; Lysine; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Orotate Phosphoribosyltransferase; Phosphoribosyl Pyrophosphate; Protein Binding; Protein Structure, Tertiary; Salmonella typhimurium; Substrate Specificity; Uridine Monophosphate

1995
Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from Escherichia coli.
    Biochemistry, 1993, Dec-07, Volume: 32, Issue:48

    Topics: Binding Sites; Escherichia coli; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; NAD; Recombinant Proteins; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; UDPglucose 4-Epimerase; Uridine Monophosphate

1993
Photoaffinity labeling with UMP of lysine 992 of carbamyl phosphate synthetase from Escherichia coli allows identification of the binding site for the pyrimidine inhibitor.
    Biochemistry, 1996, Jun-04, Volume: 35, Issue:22

    Topics: Affinity Labels; Amino Acid Sequence; Animals; Binding Sites; Carbamoyl-Phosphate Synthase (Ammonia); Cricetinae; Cyanogen Bromide; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Escherichia coli; Hydroxylamine; Hydroxylamines; Lysine; Molecular Sequence Data; Peptide Fragments; Peptide Mapping; Photochemistry; Sequence Alignment; Uridine Monophosphate

1996
Coulombic effects of remote subsites on the active site of ribonuclease A.
    Biochemistry, 1998, Dec-15, Volume: 37, Issue:50

    Topics: Alanine; Arginine; Binding Sites; Crystallography, X-Ray; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Isoelectric Point; Kinetics; Lysine; Protein Binding; Ribonuclease, Pancreatic; Static Electricity; Uridine Monophosphate

1998
Orotate phosphoribosyltransferase from Corynebacterium ammoniagenes lacking a conserved lysine.
    Journal of bacteriology, 2007, Volume: 189, Issue:24

    Topics: Bacterial Proteins; Cations, Divalent; Chromatography, Gel; Cloning, Molecular; Coenzymes; Conserved Sequence; Corynebacterium; Dimerization; Diphosphates; Enzyme Stability; Escherichia coli; Gene Expression; Hydrogen-Ion Concentration; Kinetics; Lysine; Molecular Sequence Data; Molecular Weight; Orotate Phosphoribosyltransferase; Orotic Acid; Phosphoribosyl Pyrophosphate; Recombinant Proteins; Sequence Analysis, DNA; Uridine Monophosphate

2007
Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase.
    Journal of biochemistry, 2008, Volume: 143, Issue:1

    Topics: Amino Acid Sequence; Animals; Apoenzymes; Binding Sites; Crystallography, X-Ray; Decarboxylation; Lysine; Models, Molecular; Molecular Sequence Data; Orotidine-5'-Phosphate Decarboxylase; Plasmodium falciparum; Protein Binding; Protein Structure, Tertiary; Protozoan Proteins; Sequence Homology, Amino Acid; Uridine Monophosphate

2008
Lys314 is a nucleophile in non-classical reactions of orotidine-5'-monophosphate decarboxylase.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2009, Jul-06, Volume: 15, Issue:27

    Topics: Animals; Catalysis; Humans; Hydrolysis; Lysine; Methanobacterium; Models, Molecular; Orotidine-5'-Phosphate Decarboxylase; Plasmodium falciparum; Stereoisomerism; Uridine Monophosphate

2009
Identification of Drosophila and human 7-methyl GMP-specific nucleotidases.
    The Journal of biological chemistry, 2013, Jan-25, Volume: 288, Issue:4

    Topics: Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Cyclic GMP; Drosophila melanogaster; Humans; Kinetics; Lysine; Molecular Sequence Data; Nucleotidases; Phosphorylation; RNA, Messenger; Sequence Homology, Amino Acid; Substrate Specificity; Ultraviolet Rays; Uridine Monophosphate

2013
Conserved Glu-47 and Lys-50 residues are critical for UDP-
    The Journal of biological chemistry, 2019, 06-28, Volume: 294, Issue:26

    Topics: Amino Acid Sequence; Animals; Glutamic Acid; Golgi Apparatus; Ion Transport; Lysine; Mice; Models, Molecular; Protein Conformation; Sequence Homology; Sodium-Phosphate Cotransporter Proteins, Type IIc; Uridine Diphosphate N-Acetylglucosamine; Uridine Monophosphate

2019