3-azido-2-methyl-5-methoxy-6-(3,7-dimethyloctyl)-1,4-benzoquinone and quinone

3-azido-2-methyl-5-methoxy-6-(3,7-dimethyloctyl)-1,4-benzoquinone has been researched along with quinone in 2 studies

Compound Research Comparison

Studies (3-azido-2-methyl-5-methoxy-6-(3,7-dimethyloctyl)-1,4-benzoquinone)	Trials (3-azido-2-methyl-5-methoxy-6-(3,7-dimethyloctyl)-1,4-benzoquinone)	Recent Studies (post-2010) (3-azido-2-methyl-5-methoxy-6-(3,7-dimethyloctyl)-1,4-benzoquinone)	Studies (quinone)	Trials (quinone)	Recent Studies (post-2010) (quinone)
10	0	0	2,150	3	809

Protein Interaction Comparison

Protein	Taxonomy	quinone (IC50)
Dihydroorotate dehydrogenase	Schistosoma mansoni	8.8
DNA dC->dU-editing enzyme APOBEC-3G isoform 1	Homo sapiens (human)	36.1
Amine oxidase [flavin-containing] A	Homo sapiens (human)	4.82
Caspase-1	Homo sapiens (human)	3

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	1 (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

Authors	Studies
Knaff, DB; Kriauciunas, A; Wynn, RM; Yu, CA; Yu, L	1
He, D; Yang, X; Yu, CA; Yu, L	1

Other Studies

2 other study(ies) available for 3-azido-2-methyl-5-methoxy-6-(3,7-dimethyloctyl)-1,4-benzoquinone and quinone

Article	Year
The Rhodospirillum rubrum cytochrome bc1 complex: peptide composition, prosthetic group content and quinone binding. Biochimica et biophysica acta, 1989, Aug-17, Volume: 976, Issue:1 Topics: Affinity Labels; Azides; Benzoquinones; Cytochrome b Group; Cytochrome c Group; Electron Transport; Electron Transport Complex III; Electrophoresis, Polyacrylamide Gel; Iron-Sulfur Proteins; Molecular Weight; Peptides; Photochemistry; Quinones; Rhodospirillum rubrum; Spectrophotometry; Ubiquinone	1989
The quinone-binding site in succinate-ubiquinone reductase from Escherichia coli. Quinone-binding domain and amino acid residues involved in quinone binding. The Journal of biological chemistry, 1998, Nov-27, Volume: 273, Issue:48 Topics: Affinity Labels; Amino Acid Sequence; Amino Acid Substitution; Azides; Base Sequence; Benzoquinones; Binding Sites; Chromosome Mapping; Chromosomes, Bacterial; Electron Transport Complex II; Escherichia coli; Kinetics; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Operon; Oxidoreductases; Peptide Fragments; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Succinate Dehydrogenase; Ubiquinone	1998

Article

Year

The Rhodospirillum rubrum cytochrome bc1 complex: peptide composition, prosthetic group content and quinone binding.

Biochimica et biophysica acta, 1989, Aug-17, Volume: 976, Issue:1

Topics: Affinity Labels; Azides; Benzoquinones; Cytochrome b Group; Cytochrome c Group; Electron Transport; Electron Transport Complex III; Electrophoresis, Polyacrylamide Gel; Iron-Sulfur Proteins; Molecular Weight; Peptides; Photochemistry; Quinones; Rhodospirillum rubrum; Spectrophotometry; Ubiquinone

1989

The quinone-binding site in succinate-ubiquinone reductase from Escherichia coli. Quinone-binding domain and amino acid residues involved in quinone binding.

The Journal of biological chemistry, 1998, Nov-27, Volume: 273, Issue:48

Topics: Affinity Labels; Amino Acid Sequence; Amino Acid Substitution; Azides; Base Sequence; Benzoquinones; Binding Sites; Chromosome Mapping; Chromosomes, Bacterial; Electron Transport Complex II; Escherichia coli; Kinetics; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Operon; Oxidoreductases; Peptide Fragments; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Succinate Dehydrogenase; Ubiquinone

1998