fructose-1,6-diphosphate and asparagine

fructose-1,6-diphosphate has been researched along with asparagine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	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
Aragón, JJ; García-Salguero, L; Gómez, ME; González-Mateos, F; Sánchez, V	1
Dodds, DC; Pettigrew, DW; Smith, GB; Thomas, KP	1

Other Studies

2 other study(ies) available for fructose-1,6-diphosphate and asparagine

Article	Year
Inhibition of glycolysis by amino acids in ascites tumor cells. Specificity and mechanism. The Journal of biological chemistry, 1993, Apr-15, Volume: 268, Issue:11 Topics: Amino Acids; Aminooxyacetic Acid; Animals; Asparagine; Carcinoma, Ehrlich Tumor; Fructosediphosphates; Glucose; Glutamine; Glycolysis; Kinetics; Lactates; Male; Mice; Phosphofructokinase-1; Tumor Cells, Cultured	1993
Conserved active site aspartates and domain-domain interactions in regulatory properties of the sugar kinase superfamily. Archives of biochemistry and biophysics, 1998, Jan-15, Volume: 349, Issue:2 Topics: Allosteric Regulation; Allosteric Site; Amino Acid Sequence; Asparagine; Aspartic Acid; Binding Sites; Conserved Sequence; Escherichia coli; Escherichia coli Proteins; Fructosediphosphates; Glycerol Kinase; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Phosphoenolpyruvate Sugar Phosphotransferase System; Point Mutation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins	1998

Article

Year

Inhibition of glycolysis by amino acids in ascites tumor cells. Specificity and mechanism.

The Journal of biological chemistry, 1993, Apr-15, Volume: 268, Issue:11

Topics: Amino Acids; Aminooxyacetic Acid; Animals; Asparagine; Carcinoma, Ehrlich Tumor; Fructosediphosphates; Glucose; Glutamine; Glycolysis; Kinetics; Lactates; Male; Mice; Phosphofructokinase-1; Tumor Cells, Cultured

1993

Conserved active site aspartates and domain-domain interactions in regulatory properties of the sugar kinase superfamily.

Archives of biochemistry and biophysics, 1998, Jan-15, Volume: 349, Issue:2

Topics: Allosteric Regulation; Allosteric Site; Amino Acid Sequence; Asparagine; Aspartic Acid; Binding Sites; Conserved Sequence; Escherichia coli; Escherichia coli Proteins; Fructosediphosphates; Glycerol Kinase; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Phosphoenolpyruvate Sugar Phosphotransferase System; Point Mutation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins

1998