adenosine monophosphate and asparagine
adenosine monophosphate has been researched along with asparagine in 14 studies
Research
Studies (14)
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (14.29) | 18.7374 |
1990's | 3 (21.43) | 18.2507 |
2000's | 8 (57.14) | 29.6817 |
2010's | 1 (7.14) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors
Authors | Studies |
---|---|
Makarewicz, W | 1 |
Balaji, PV; Rao, VS; Saenger, W | 1 |
Fox, SW; Weber, AL | 1 |
Boehlein, SK; Richards, NG; Schuster, SM; Walworth, ES | 1 |
Boehlein, SK; Richards, NG; Schuster, SM; Stewart, JD; Thirumoorthy, R; Walworth, ES | 1 |
Jensen, RA; Luengo, JM; Miñambres, B; Olivera, ER | 1 |
Boehlein, SK; Hiratake, J; Nakatsu, T; Richards, NG; Schuster, SM; Stewart, JD; Thirumoorthy, R | 1 |
Black, ME; Stolworthy, TS | 1 |
Colman, RF; Palenchar, JB | 1 |
Colman, RF; Segall, ML | 1 |
Iwasaki, W; Kuramitsu, S; Kuroishi, C; Sekine, S; Shirouzu, M; Yokoyama, S | 1 |
Simonson, T; Thompson, D | 1 |
Bae, E; Bingman, CA; Lee, JE; Phillips, GN; Raines, RT | 1 |
Hou, Y; Leng, W; Li, S; Liu, Y; Pi, D; Shi, H; Wang, X; Zhu, H | 1 |
Other Studies
14 other study(ies) available for adenosine monophosphate and asparagine
Article | Year |
---|---|
[The purine nucleotide cycle (author's transl)].
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.
Topics: Adenosine Monophosphate; Asparagine; Binding Sites; Computer Simulation; Glutathione; Guanine; Ribonuclease T1; X-Ray Diffraction | 1992 |
Aminoacylation and acetylaminoacylation of homopolyribonucleotides.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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 |