methionine has been researched along with laccase in 7 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (14.29) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (42.86) | 29.6817 |
2010's | 1 (14.29) | 24.3611 |
2020's | 2 (28.57) | 2.80 |
Authors | Studies |
---|---|
Co, MS; Hodgson, KO; Solomon, EI; Spira, DJ | 1 |
Antonyuk, S; Dodd, FE; Hall, JF; Hasnain, SS; Hough, MA; Kanbi, LD | 1 |
Koul, S; Lehnig, M; Müller, GH; Völkert, M; Waldmann, H | 1 |
Ivanic, J; Jensen, JH; Li, H; Webb, SP | 1 |
Dong, Y; Fan, Y; Gao, Z; Gong, Y; Liu, X; Tian, J; Wang, H; Wu, N; Yan, Y; Yue, Q; Zhang, Z; Zhao, J | 1 |
Avelar, M; Miranda-Blancas, R; Rodriguez-Arteaga, A; Rudiño-Piñera, E; Sinicropi, A | 1 |
Xie, Y; Xu, Z; Yang, S; Yu, H; Zhou, J | 1 |
7 other study(ies) available for methionine and laccase
Article | Year |
---|---|
EXAFS investigation of the binuclear cupric site in met T2D Rhus laccase and its azide bound derivative.
Topics: Azides; Binding Sites; Chemical Phenomena; Chemistry; Copper; Hemocyanins; Laccase; Methionine; Oxidoreductases; Plants, Toxic; Spectrum Analysis; Toxicodendron; X-Rays | 1983 |
Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins.
Topics: Amino Acid Sequence; Aspartic Acid; Azurin; Binding Sites; Ceruloplasmin; Copper; Crystallography, X-Ray; Hydrogen Bonding; Laccase; Leucine; Ligands; Methionine; Models, Molecular; Molecular Sequence Data; Mutation; Nitrite Reductases; Oxidation-Reduction; Oxidoreductases; Phylogeny; Protein Folding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Serine; Thiobacillus | 2002 |
Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis.
Topics: Agaricales; Amino Acids; Catalysis; Chemistry, Organic; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Hydrolysis; Laccase; Methionine; Molecular Structure; Monophenol Monooxygenase; Oxidation-Reduction; Oxidoreductases; Oxygen; Peptides; Phenylhydrazines; Temperature | 2002 |
Determinants of the relative reduction potentials of type-1 copper sites in proteins.
Topics: Azurin; Binding Sites; Ceruloplasmin; Copper; Cysteine; Humans; Hydrogen Bonding; Laccase; Ligands; Methionine; Oxidation-Reduction; Plastocyanin; Proteins; Quantum Theory | 2004 |
Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity.
Topics: Amino Acid Sequence; Binding Sites; Copper; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Laccase; Methionine; Models, Molecular; Mutation; Oxidoreductases; Protein Conformation; Protein Structure, Tertiary; Substrate Specificity | 2018 |
The β-hairpin from the Thermus thermophilus HB27 laccase works as a pH-dependent switch to regulate laccase activity.
Topics: Amino Acid Motifs; Bacterial Proteins; Crystallography, X-Ray; Hydrazones; Hydrogen-Ion Concentration; Laccase; Methionine; Molecular Dynamics Simulation; Oxidation-Reduction; Oxidoreductases; Phylogeny; Protein Conformation; Temperature; Thermus thermophilus | 2021 |
Modulating the adsorption orientation of methionine-rich laccase by tailoring the surface chemistry of single-walled carbon nanotubes.
Topics: Adsorption; Electrodes; Laccase; Methionine; Nanotubes, Carbon | 2022 |