asparagine and 6-hydroxydopa quinone

asparagine has been researched along with 6-hydroxydopa quinone in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Green, EL; Klinman, JP; Sanders-Loehr, J; Schwartz, B	1
Dove, JE; Klinman, JP; Schwartz, B; Williams, NK	1

Other Studies

2 other study(ies) available for asparagine and 6-hydroxydopa quinone

Article	Year
Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast. Biochemistry, 1998, Nov-24, Volume: 37, Issue:47 Topics: Alanine; Amine Oxidase (Copper-Containing); Amino Acid Sequence; Asparagine; Catalysis; Coenzymes; Conserved Sequence; Dihydroxyphenylalanine; Enzyme Activation; Kinetics; Methylamines; Mutagenesis, Site-Directed; Pichia; Protein Conformation; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet; Temperature	1998
Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast. Biochemistry, 2000, Apr-04, Volume: 39, Issue:13 Topics: Amine Oxidase (Copper-Containing); Asparagine; Aspartic Acid; Binding Sites; Coenzymes; Copper; Cysteine; Dihydroxyphenylalanine; Glutamic Acid; Glutamine; Histidine; Mutagenesis, Site-Directed; Oxygen Consumption; Pichia; Recombinant Proteins; Spectrophotometry, Atomic; Spectrophotometry, Ultraviolet	2000

Article

Year

Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast.

Biochemistry, 1998, Nov-24, Volume: 37, Issue:47

Topics: Alanine; Amine Oxidase (Copper-Containing); Amino Acid Sequence; Asparagine; Catalysis; Coenzymes; Conserved Sequence; Dihydroxyphenylalanine; Enzyme Activation; Kinetics; Methylamines; Mutagenesis, Site-Directed; Pichia; Protein Conformation; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet; Temperature

1998

Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast.

Biochemistry, 2000, Apr-04, Volume: 39, Issue:13

Topics: Amine Oxidase (Copper-Containing); Asparagine; Aspartic Acid; Binding Sites; Coenzymes; Copper; Cysteine; Dihydroxyphenylalanine; Glutamic Acid; Glutamine; Histidine; Mutagenesis, Site-Directed; Oxygen Consumption; Pichia; Recombinant Proteins; Spectrophotometry, Atomic; Spectrophotometry, Ultraviolet

2000