asparagine has been researched along with guanosine monophosphate in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (12.50) | 18.7374 |
| 1990's | 4 (50.00) | 18.2507 |
| 2000's | 2 (25.00) | 29.6817 |
| 2010's | 1 (12.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Makarewicz, W | 1 |
| Balaji, PV; Rao, VS | 1 |
| Haikal, AF; Stanssens, P; Steyaert, J; Wyns, L | 1 |
| Grubmeyer, C; Xu, Y | 1 |
| Munagala, NR; Wang, CC | 1 |
| Black, ME; Stolworthy, TS | 1 |
| Azurmendi, HF; Mildvan, AS; Saraswat, V | 1 |
| Burak, MJ; Garcia-Diaz, M; Guja, KE | 1 |
8 other study(ies) available for asparagine and guanosine monophosphate
| 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 |
Computer modeling studies on the subsite interactions of ribonuclease T1.
Topics: Asparagine; Binding Sites; Computer Simulation; Dinucleoside Phosphates; Exoribonucleases; Guanosine Diphosphate; Guanosine Monophosphate; Tyrosine | 1992 |
Subsite interactions of ribonuclease T1: Asn36 and Asn98 accelerate GpN transesterification through interactions with the leaving nucleoside N.
Topics: Amino Acid Sequence; Asparagine; Base Composition; Binding Sites; Dinucleoside Phosphates; Esterification; Guanosine Monophosphate; Kinetics; Protein Conformation; Ribonuclease T1; Substrate Specificity | 1991 |
Catalysis in human hypoxanthine-guanine phosphoribosyltransferase: Asp 137 acts as a general acid/base.
Topics: Amino Acid Substitution; Asparagine; Aspartic Acid; Catalysis; Glutamine; Guanosine Monophosphate; Humans; Hydrogen-Ion Concentration; Hypoxanthine Phosphoribosyltransferase; Inosine Monophosphate; Kinetics; Ligands; Lysine; Mutagenesis, Site-Directed; Polymerase Chain Reaction | 1998 |
Altering the purine specificity of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus by structure-based point mutations in the enzyme protein.
Topics: Adenine Phosphoribosyltransferase; Amino Acid Substitution; Animals; Arginine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Enzyme Activation; Glutamic Acid; Guanine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Isoleucine; Lysine; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Purines; Ribonucleotides; Serine; Structure-Activity Relationship; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine | 1998 |
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 |
Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase.
Topics: Alanine; Arginine; Asparagine; Binding Sites; Deuterium Exchange Measurement; DNA Mutational Analysis; Escherichia coli Proteins; Guanosine Monophosphate; Hydrogen Bonding; Kinetics; Ligands; Magnesium; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Phosphoric Monoester Hydrolases; Protein Binding; Protons; Pyrophosphatases; Thermodynamics | 2004 |
Nucleotide binding interactions modulate dNTP selectivity and facilitate 8-oxo-dGTP incorporation by DNA polymerase lambda.
Topics: Alanine; Asparagine; Catalytic Domain; Deoxyguanine Nucleotides; Deoxyribonucleotides; DNA Polymerase beta; Guanosine Monophosphate; Humans; Kinetics; Protein Binding | 2015 |