dihydroxyacetone and flavin-adenine dinucleotide

dihydroxyacetone has been researched along with flavin-adenine dinucleotide in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Cabezas, A; Cameselle, JC; Costas, MJ; Couto, A; Pinto, RM	1
Cabezas, A; Cameselle, JC; Ribeiro, JM; Rodrigues, JR	1

Other Studies

2 other study(ies) available for dihydroxyacetone and flavin-adenine dinucleotide

Article	Year
Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases. Biochemical and biophysical research communications, 2005, Dec-30, Volume: 338, Issue:4 Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Cloning, Molecular; Dihydroxyacetone; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Humans; Liver; Molecular Sequence Data; Phosphorus-Oxygen Lyases; Phosphotransferases (Alcohol Group Acceptor); Rats; Recombinant Proteins; Sequence Alignment	2005
Closure of the Human TKFC Active Site: Comparison of the Apoenzyme and the Complexes Formed with Either Triokinase or FMN Cyclase Substrates. International journal of molecular sciences, 2019, Mar-04, Volume: 20, Issue:5 Topics: Adenosine Triphosphate; Apoenzymes; Binding Sites; Catalysis; Catalytic Domain; Dihydroxyacetone; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glyceraldehyde; Humans; Molecular Dynamics Simulation; Phosphorus-Oxygen Lyases; Phosphorylation; Phosphotransferases (Alcohol Group Acceptor); Substrate Specificity	2019

Article

Year

Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases.

Biochemical and biophysical research communications, 2005, Dec-30, Volume: 338, Issue:4

Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Cloning, Molecular; Dihydroxyacetone; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Humans; Liver; Molecular Sequence Data; Phosphorus-Oxygen Lyases; Phosphotransferases (Alcohol Group Acceptor); Rats; Recombinant Proteins; Sequence Alignment

2005

Closure of the Human TKFC Active Site: Comparison of the Apoenzyme and the Complexes Formed with Either Triokinase or FMN Cyclase Substrates.

International journal of molecular sciences, 2019, Mar-04, Volume: 20, Issue:5

Topics: Adenosine Triphosphate; Apoenzymes; Binding Sites; Catalysis; Catalytic Domain; Dihydroxyacetone; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glyceraldehyde; Humans; Molecular Dynamics Simulation; Phosphorus-Oxygen Lyases; Phosphorylation; Phosphotransferases (Alcohol Group Acceptor); Substrate Specificity

2019