methylamine has been researched along with tryptophan tryptophylquinone in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ferguson, SJ; Page, MD | 1 |
| Chen, ZW; Ferrari, D; Kuusk, V; Labesse, G; Mathews, FS; McIntire, WS; Rossi, GL | 1 |
| Davidson, VL; Jones, LH; Pearson, AR; Tang, Y; Wilmot, CM | 1 |
| Biermann, N; Cavalieri, C; Einsle, O; Ferrari, D; Merli, A; Rossi, GL; Ubbink, M; Vlasie, MD | 1 |
4 other study(ies) available for methylamine and tryptophan tryptophylquinone
| Article | Year |
|---|---|
Mutants of Methylobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesise the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophylquinone group.
Topics: Benzoquinones; Choline; Cytochrome c Group; Gram-Negative Aerobic Bacteria; Indolequinones; Methylamines; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Peptides; Quinones; Tryptophan | 1993 |
Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1.
Topics: Bacterial Proteins; Binding Sites; Cesium; Crystallography, X-Ray; Indolequinones; Methylamines; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrophotometry; Tryptophan | 1998 |
Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.
Topics: Aspartic Acid; Binding Sites; Crystallography, X-Ray; Cysteine; Disulfides; Indolequinones; Kinetics; Mass Spectrometry; Methylamines; Models, Chemical; Models, Molecular; Models, Statistical; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Protein Conformation; Tryptophan | 2005 |
Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus.
Topics: Bacterial Proteins; Binding Sites; Catalysis; Copper; Crystallization; Crystallography, X-Ray; Electron Transport; Indolequinones; Kinetics; Metalloproteins; Methylamines; Models, Molecular; Molecular Weight; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Solutions; Tryptophan | 2008 |