adenosine monophosphate has been researched along with methioninyl adenylate in 17 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (17.65) | 18.7374 |
| 1990's | 6 (35.29) | 18.2507 |
| 2000's | 5 (29.41) | 29.6817 |
| 2010's | 2 (11.76) | 24.3611 |
| 2020's | 1 (5.88) | 2.80 |
| Authors | Studies |
|---|---|
| Lawrence, F; Robert-Gero, M; Vigier, P | 1 |
| Blanchard, P; Enouf, J; Farrugia, G; Laurence, F; Robert-Gero, M | 1 |
| Brunie, S; Ghosh, G; Pelka, H; Schulman, LH | 1 |
| Blanquet, S; Fourmy, D; Mechulam, Y | 1 |
| Blanquet, S; Mechulam, Y; Meinnel, T; Schmitt, E | 1 |
| Blanquet, S; Mechulam, Y; Panvert, M; Schmitt, E | 1 |
| Blanquet, S; Gillet, S; Hountondji, C; Schmitter, JM | 1 |
| Chun, MW; Jo, YJ; Kang, MK; Kang, SU; Kim, S; Kwak, JH; Lee, J | 1 |
| Cassio, D; Mathien, Y | 1 |
| Beauvallet, C; Blanquet, S; Hountondji, C; Pernollet, JC | 1 |
| Jo, YJ; Kang, MK; Kang, SU; Kim, S; Kim, SE; Kim, SY; Lee, J | 1 |
| Beauvallet, C; Blanquet, S; Dessen, P; Hountondji, C; Lazennec, C; Pernollet, JC; Plateau, P | 1 |
| Blanquet, S; Crepin, T; Honek, JF; Mechulam, Y; Sampson, PB; Schmitt, E; Vaughan, MD | 1 |
| Daub, E; Honek, JF; Sampson, PB; Vaughan, MD | 1 |
| Buckner, FS; Fan, E; Hol, WG; Kelley, A; Kim, JE; Larson, ET; Merritt, EA; Mueller, N; Napuli, AJ; Van Voorhis, WC; Verlinde, CL; Zucker, FH | 1 |
| Buckner, FS; Fan, E; Gillespie, JR; Hol, WG; Kim, JE; Koh, CY; Liu, J; Ranade, RM; Shibata, S; Verlinde, CL; Yu, M | 1 |
| Gaillard, T; Mechulam, Y; Nigro, G; Opuu, V; Schmitt, E; Simonson, T | 1 |
17 other study(ies) available for adenosine monophosphate and methioninyl adenylate
| Article | Year |
|---|---|
Inhibition by methioninyl adenylate of focus formation by Rous sarcoma virus.
Topics: Adenosine Monophosphate; Amino Acyl-tRNA Synthetases; Avian Sarcoma Viruses; Cell Division; Cell Transformation, Neoplastic; Cells, Cultured; Contact Inhibition; Dose-Response Relationship, Drug; Methionine; Methionine-tRNA Ligase; Neoplasm Proteins; Virus Replication | 1975 |
Comparative effect of methioninyl adenylate on the growth of Salmonella typhimurium and Pseudomonas aeruginosa.
Topics: Adenosine Monophosphate; Methionine; Methionine-tRNA Ligase; Phosphoric Diester Hydrolases; Pseudomonas; Pseudomonas aeruginosa; Salmonella typhimurium | 1976 |
Activation of methionine by Escherichia coli methionyl-tRNA synthetase.
Topics: Adenosine Monophosphate; Alanine; Amino Acid Sequence; Arginine; Aspartic Acid; Bacterial Proteins; Base Sequence; Catalysis; Enzyme Activation; Escherichia coli; Glutamine; Methionine; Methionine-tRNA Ligase; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Substrate Specificity; Transfer RNA Aminoacylation; Tryptophan | 1991 |
Crucial role of an idiosyncratic insertion in the Rossman fold of class 1 aminoacyl-tRNA synthetases: the case of methionyl-tRNA synthetase.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Amino Acyl-tRNA Synthetases; Escherichia coli; Methionine; Methionine-tRNA Ligase; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Folding; Substrate Specificity; Zinc | 1995 |
Methionyl-tRNA synthetase needs an intact and mobile 332KMSKS336 motif in catalysis of methionyl adenylate formation.
Topics: Adenosine; Adenosine Monophosphate; Adenosine Triphosphate; Amino Acid Sequence; Animals; Catalysis; Conserved Sequence; Diphosphates; Humans; Hydrolysis; Kinetics; Magnesium; Methionine; Methionine-tRNA Ligase; Molecular Sequence Data; Mutation; Sequence Alignment | 1994 |
Transition state stabilization by the 'high' motif of class I aminoacyl-tRNA synthetases: the case of Escherichia coli methionyl-tRNA synthetase.
Topics: Adenosine Monophosphate; Adenosine Triphosphate; Escherichia coli; Methionine; Methionine-tRNA Ligase; Mutagenesis, Site-Directed; Peptide Fragments; Structure-Activity Relationship | 1995 |
Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Escherichia coli; Lysine; Methionine; Methionine-tRNA Ligase; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 1997 |
Methionyl adenylate analogues as inhibitors of methionyl-tRNA synthetase.
Topics: Adenosine Monophosphate; Anti-Bacterial Agents; Anti-Infective Agents; Drug Design; Enzyme Inhibitors; Escherichia coli; Humans; Methionine; Methionine-tRNA Ligase; Microbial Sensitivity Tests; Mycobacterium tuberculosis; Saccharomyces cerevisiae | 1999 |
Effect of L-methioninyl adenylate on the level of aminoacylation in vivo of tRNA(Met) from Escherichia coli K12.
Topics: Adenosine Monophosphate; Escherichia coli; Methionine; RNA, Bacterial; RNA, Transfer, Amino Acyl; RNA, Transfer, Ile; RNA, Transfer, Leu; RNA, Transfer, Met | 1974 |
Enzyme-induced covalent modification of methionyl-tRNA synthetase from Bacillus stearothermophilus by methionyl-adenylate: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Bacterial Proteins; Carbon Radioisotopes; Catalysis; Catalytic Domain; Dimerization; Escherichia coli; Geobacillus stearothermophilus; Kinetics; Lysine; Methionine; Methionine-tRNA Ligase; Molecular Sequence Data; Sequence Alignment; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2000 |
Ester and hydroxamate analogues of methionyl and isoleucyl adenylates as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetases.
Topics: Adenosine; Adenosine Monophosphate; Binding Sites; Escherichia coli; Esters; Hydroxamic Acids; Isoleucine; Isoleucine-tRNA Ligase; Methionine; Methionine-tRNA Ligase; Models, Molecular; Structure-Activity Relationship | 2001 |
Crucial role of conserved lysine 277 in the fidelity of tRNA aminoacylation by Escherichia coli valyl-tRNA synthetase.
Topics: Acylation; Adenosine Monophosphate; Alanine; Amino Acid Sequence; Binding Sites; Catalytic Domain; Conserved Sequence; Escherichia coli Proteins; Lysine; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; RNA Editing; RNA, Transfer, Thr; RNA, Transfer, Val; Sequence Alignment; Sequence Homology, Amino Acid; Threonine; Valine-tRNA Ligase | 2002 |
Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Catalysis; Crystallography, X-Ray; Escherichia coli; Methionine; Methionine-tRNA Ligase; Molecular Sequence Data; Molecular Structure; Protein Binding; Protein Conformation; Sequence Alignment | 2003 |
Investigation of bioisosteric effects on the interaction of substrates/ inhibitors with the methionyl-tRNA synthetase from Escherichia coli.
Topics: Adenosine; Adenosine Monophosphate; Anti-Bacterial Agents; Enzyme Inhibitors; Escherichia coli; Homocysteine; Methionine; Methionine-tRNA Ligase; Organophosphonates; Phosphinic Acids; Protein Conformation; Stereoisomerism; Substrate Specificity | 2005 |
Structure of Leishmania major methionyl-tRNA synthetase in complex with intermediate products methionyladenylate and pyrophosphate.
Topics: Adenine Nucleotides; Adenosine Monophosphate; Amino Acid Motifs; Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Diphosphates; Escherichia coli; Gram-Negative Bacteria; Humans; Leishmania major; Magnesium; Methionine; Methionine-tRNA Ligase; Models, Molecular; Molecular Sequence Data; Protein Binding; Sequence Homology, Amino Acid; Tryptophan-tRNA Ligase | 2011 |
Distinct states of methionyl-tRNA synthetase indicate inhibitor binding by conformational selection.
Topics: Adenosine Monophosphate; Aminoquinolines; Antimalarials; Benzimidazoles; Catalytic Domain; Crystallography, X-Ray; Hydrogen Bonding; Methionine; Methionine-tRNA Ligase; Models, Molecular; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Subunits; Surface Properties; Trypanosoma brucei brucei | 2012 |
Adaptive landscape flattening allows the design of both enzyme: Substrate binding and catalytic power.
Topics: Adenosine Monophosphate; Azides; Binding Sites; Catalysis; Enzymes; Methionine; Methionine-tRNA Ligase; Monte Carlo Method; Mutation; Norleucine; Protein Binding; Protein Engineering; Substrate Specificity | 2020 |