methionine has been researched along with iodoacetic acid in 6 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (50.00) | 18.7374 |
| 1990's | 3 (50.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cummings, JG; Lau, SM; Powell, PJ; Thorpe, C | 1 |
| Campbell, DG; Coggins, JR; Kleanthous, C | 1 |
| Coggins, JR; Kleanthous, C | 1 |
| Bazaes, S; Heinrikson, RL; Kemp, RG; Latshaw, SP; Poorman, RA; Randolph, A | 1 |
| Goverman, JM; Pierce, JG | 1 |
| Baehner, RL; Boxer, LA; Yasaka, T | 1 |
6 other study(ies) available for methionine and iodoacetic acid
| Article | Year |
|---|---|
Reductive half-reaction in medium-chain acyl-CoA dehydrogenase: modulation of internal equilibrium by carboxymethylation of a specific methionine residue.
Topics: Acyl Coenzyme A; Acyl-CoA Dehydrogenase; Acyl-CoA Dehydrogenases; Amino Acid Sequence; Animals; Binding Sites; Energy Metabolism; Iodoacetates; Iodoacetic Acid; Kidney; Macromolecular Substances; Methionine; Models, Chemical; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Sequence Homology; Structure-Activity Relationship; Swine | 1992 |
Active site labeling of the shikimate pathway enzyme, dehydroquinase. Evidence for a common substrate binding site within dehydroquinase and dehydroquinate synthase.
Topics: Affinity Labels; Amino Acid Sequence; Binding Sites; Escherichia coli; Hydro-Lyases; Iodoacetates; Iodoacetic Acid; Kinetics; Lyases; Methionine; Molecular Sequence Data; Molecular Structure; Peptide Fragments; Phosphorus-Oxygen Lyases; Shikimic Acid | 1990 |
Reversible alkylation of an active site methionine residue in dehydroquinase.
Topics: Affinity Labels; Alkylation; Binding Sites; Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Enzyme Reactivators; Escherichia coli; Guanidine; Guanidines; Hydro-Lyases; Hydrogen-Ion Concentration; Iodoacetates; Iodoacetic Acid; Kinetics; Mass Spectrometry; Mercaptoethanol; Methionine; Peptide Mapping; Protein Conformation; Protein Denaturation; Sulfides; Urea | 1990 |
Identification of highly reactive cysteinyl and methionyl residues of rabbit muscle phosphofructokinase.
Topics: Allosteric Site; Amino Acid Sequence; Animals; Binding Sites; Chemical Phenomena; Chemistry; Cyclic AMP; Cysteine; Escherichia coli; Fructosephosphates; Geobacillus stearothermophilus; Iodoacetates; Iodoacetic Acid; Methionine; Muscles; Peptide Fragments; Phosphofructokinase-1; Rabbits; Structure-Activity Relationship; Trypsin | 1987 |
Differential effects of alkylation of methionine residues on the activities of pituitary thyrotropin and lutropin.
Topics: Alkylation; Animals; Cattle; Chickens; Iodoacetates; Iodoacetic Acid; Kinetics; Luteinizing Hormone; Macromolecular Substances; Male; Methionine; Phosphates; Pituitary Gland, Anterior; Rats; Receptors, Cell Surface; Receptors, LH; Receptors, Thyrotropin; Testis; Thyroid Gland; Thyrotropin | 1981 |
Monocyte aggregation and superoxide anion release in response to formyl-methionyl-leucyl-phenylalanine (FMLP) and platelet-activating factor (PAF).
Topics: Calcium; Cell Aggregation; Cytochalasin B; Deoxyglucose; Humans; Iodoacetates; Iodoacetic Acid; Lysophosphatidylcholines; Magnesium; Methionine; Monocytes; Muramidase; N-Formylmethionine; N-Formylmethionine Leucyl-Phenylalanine; Oligopeptides; Oxygen; Platelet Activating Factor; Superoxides | 1982 |