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adenosine monophosphate and asparagine

adenosine monophosphate has been researched along with asparagine in 14 studies

Research

Studies (14)

TimeframeStudies, this research(%)All Research%
pre-19902 (14.29)18.7374
1990's3 (21.43)18.2507
2000's8 (57.14)29.6817
2010's1 (7.14)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Makarewicz, W1
Balaji, PV; Rao, VS; Saenger, W1
Fox, SW; Weber, AL1
Boehlein, SK; Richards, NG; Schuster, SM; Walworth, ES1
Boehlein, SK; Richards, NG; Schuster, SM; Stewart, JD; Thirumoorthy, R; Walworth, ES1
Jensen, RA; Luengo, JM; Miñambres, B; Olivera, ER1
Boehlein, SK; Hiratake, J; Nakatsu, T; Richards, NG; Schuster, SM; Stewart, JD; Thirumoorthy, R1
Black, ME; Stolworthy, TS1
Colman, RF; Palenchar, JB1
Colman, RF; Segall, ML1
Iwasaki, W; Kuramitsu, S; Kuroishi, C; Sekine, S; Shirouzu, M; Yokoyama, S1
Simonson, T; Thompson, D1
Bae, E; Bingman, CA; Lee, JE; Phillips, GN; Raines, RT1
Hou, Y; Leng, W; Li, S; Liu, Y; Pi, D; Shi, H; Wang, X; Zhu, H1

Other Studies

14 other study(ies) available for adenosine monophosphate and asparagine

ArticleYear
[The purine nucleotide cycle (author's transl)].
    Postepy biochemii, 1979, Volume: 25, Issue:2

    Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphate; Adenylosuccinate Lyase; Adenylosuccinate Synthase; Amino Acids; AMP Deaminase; Animals; Asparagine; Guanosine Monophosphate; Guanosine Triphosphate; Humans; In Vitro Techniques; Inosine Monophosphate; Muscles; Purine Nucleotides; Rabbits; Rats

1979
Modes of binding of 2'-AMP to RNase T1. A computer modeling study.
    Journal of biomolecular structure & dynamics, 1992, Volume: 9, Issue:5

    Topics: Adenosine Monophosphate; Asparagine; Binding Sites; Computer Simulation; Glutathione; Guanine; Ribonuclease T1; X-Ray Diffraction

1992
Aminoacylation and acetylaminoacylation of homopolyribonucleotides.
    Biochimica et biophysica acta, 1973, Aug-24, Volume: 319, Issue:2

    Topics: Acetylation; Acylation; Adenosine Monophosphate; Amino Acyl-tRNA Synthetases; Asparagine; Binding Sites; Carbon Radioisotopes; Cytosine Nucleotides; Fluoroacetates; Genetic Code; Glycine; Hydroxylamines; Imidazoles; Kinetics; Mathematics; Models, Chemical; Phenylalanine; Poly U; Polynucleotides; Proline; Spectrophotometry, Ultraviolet; Time Factors

1973
Mutagenesis and chemical rescue indicate residues involved in beta-aspartyl-AMP formation by Escherichia coli asparagine synthetase B.
    The Journal of biological chemistry, 1997, May-09, Volume: 272, Issue:19

    Topics: Adenosine Monophosphate; Amino Acid Sequence; Arginine; Asparagine; Aspartate-Ammonia Ligase; Aspartic Acid; Escherichia coli; Glutamine; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis; Mutagenesis, Site-Directed; Sequence Alignment; Software; Structure-Activity Relationship; Threonine

1997
Kinetic mechanism of Escherichia coli asparagine synthetase B.
    Biochemistry, 1998, Sep-22, Volume: 37, Issue:38

    Topics: Adenosine Monophosphate; Asparagine; Aspartate-Ammonia Ligase; Aspartic Acid; Bacterial Proteins; Binding, Competitive; Escherichia coli; Glutamine; Isotope Labeling; Kinetics; Oxygen Isotopes; Substrate Specificity

1998
A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus.
    The Journal of biological chemistry, 2000, Dec-15, Volume: 275, Issue:50

    Topics: Adenosine Monophosphate; Allosteric Site; Amino Acid Sequence; Ammonia; Asparagine; Aspartic Acid; Base Sequence; Carbon; Catalysis; Cell Division; DNA; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Evolution, Molecular; Glutamate Dehydrogenase; Glycerol; Hydrogen-Ion Concentration; Ketoglutaric Acids; Kinetics; Molecular Sequence Data; Molecular Weight; NAD; Nitrogen; Phylogeny; Polymerase Chain Reaction; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Streptomyces; Temperature; Time Factors; Tricarboxylic Acids

2000
Characterization of inhibitors acting at the synthetase site of Escherichia coli asparagine synthetase B.
    Biochemistry, 2001, Sep-18, Volume: 40, Issue:37

    Topics: Adenosine Monophosphate; Adenosine Triphosphate; Asparagine; Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor; Cysteine; Enzyme Inhibitors; Escherichia coli; Hydrolysis; Methionine Sulfoximine; Models, Chemical; Neurotransmitter Agents; Nuclear Magnetic Resonance, Biomolecular; Phosphorus Isotopes; Spectrometry, Mass, Electrospray Ionization

2001
The mouse guanylate kinase double mutant E72Q/D103N is a functional adenylate kinase.
    Protein engineering, 2001, Volume: 14, Issue:11

    Topics: Adenosine Monophosphate; Adenylate Kinase; Animals; Asparagine; Binding Sites; DNA, Complementary; Escherichia coli; Genetic Complementation Test; Genetic Vectors; Glutamine; Guanosine Monophosphate; Guanylate Kinases; Mice; Models, Chemical; Mutagenesis; Mutation; Nucleoside-Phosphate Kinase; Spectrophotometry; Substrate Specificity; Time Factors

2001
Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural role.
    Biochemistry, 2003, Feb-25, Volume: 42, Issue:7

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Aminoimidazole Carboxamide; Arginine; Asparagine; Bacillus subtilis; Bacterial Proteins; Circular Dichroism; Enzyme Activation; Humans; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Ribonucleotides; Substrate Specificity; Threonine

2003
Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.
    Biochemistry, 2004, Jun-15, Volume: 43, Issue:23

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Animals; Arginine; Asparagine; Bacillus subtilis; Binding Sites; Catalysis; Circular Dichroism; Glutamine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Sequence Alignment; Thermodynamics

2004
Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase.
    Journal of molecular biology, 2006, Jul-07, Volume: 360, Issue:2

    Topics: Adenosine Monophosphate; Amino Acid Sequence; Aminoacylation; Asparagine; Aspartate-tRNA Ligase; Binding Sites; Crystallography, X-Ray; Escherichia coli; Models, Molecular; Molecular Sequence Data; Protein Conformation; Pyrococcus horikoshii; RNA, Transfer, Amino Acyl; RNA, Transfer, Asn; Sequence Alignment; Substrate Specificity; Thermus thermophilus; Water

2006
Molecular dynamics simulations show that bound Mg2+ contributes to amino acid and aminoacyl adenylate binding specificity in aspartyl-tRNA synthetase through long range electrostatic interactions.
    The Journal of biological chemistry, 2006, Aug-18, Volume: 281, Issue:33

    Topics: Adenosine Monophosphate; Adenosine Triphosphate; Aminoacylation; Archaeal Proteins; Asparagine; Aspartate-tRNA Ligase; Aspartic Acid; Binding Sites; Catalysis; Cations, Divalent; Computer Simulation; Crystallography, X-Ray; Enzyme Stability; Magnesium; Pyrococcus; RNA, Transfer; Static Electricity; Substrate Specificity; Thermodynamics

2006
Structural basis for catalysis by onconase.
    Journal of molecular biology, 2008, Jan-04, Volume: 375, Issue:1

    Topics: Adenosine Monophosphate; Alanine; Amino Acid Sequence; Amino Acid Substitution; Asparagine; Binding Sites; Catalysis; Crystallography, X-Ray; Disulfides; Glutamic Acid; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; K562 Cells; Kinetics; Lysine; Models, Biological; Models, Chemical; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Synthesis Inhibitors; Ribonucleases; Sequence Homology, Amino Acid; Substrate Specificity; X-Ray Diffraction

2008
Asparagine attenuates intestinal injury, improves energy status and inhibits AMP-activated protein kinase signalling pathways in weaned piglets challenged with Escherichia coli lipopolysaccharide.
    The British journal of nutrition, 2015, Aug-28, Volume: 114, Issue:4

    Topics: Adenosine Monophosphate; Adenosine Triphosphate; AMP-Activated Protein Kinases; Animals; Asparagine; Dietary Supplements; Disaccharidases; Energy Metabolism; Enterocytes; Escherichia coli; Intestinal Diseases; Intestinal Mucosa; Intestine, Small; Lipopolysaccharides; Male; Phosphorylation; Signal Transduction; Sirtuin 1; Swine; Transcription Factors; Weaning

2015
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