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fructose-6-phosphate and adenylyl imidodiphosphate

fructose-6-phosphate has been researched along with adenylyl imidodiphosphate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19901 (25.00)18.7374
1990's2 (50.00)18.2507
2000's0 (0.00)29.6817
2010's1 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Gilbert, HF; Lee, JC; Luther, MA1
Auzat, I; Garel, JR; Gawlita, E1
Byrnes, WM; Chang, SH; Hu, W; Younathan, ES1
Crochet, RB; Kim, JD; Kim, SG; Lee, H; Lee, YH; Neau, D; Yim, YS1

Other Studies

4 other study(ies) available for fructose-6-phosphate and adenylyl imidodiphosphate

ArticleYear
Self-association of rabbit muscle phosphofructokinase: role of subunit interaction in regulation of enzymatic activity.
    Biochemistry, 1983, Nov-22, Volume: 22, Issue:24

    Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Fructosephosphates; Glutathione; Glutathione Disulfide; Kinetics; Macromolecular Substances; Molecular Weight; Muscles; Phosphofructokinase-1; Rabbits

1983
Slow ligand-induced transitions in the allosteric phosphofructokinase from Escherichia coli.
    Journal of molecular biology, 1995, Jun-02, Volume: 249, Issue:2

    Topics: Adenosine Diphosphate; Adenylyl Imidodiphosphate; Allosteric Regulation; Allosteric Site; Crystallography, X-Ray; Escherichia coli; Fructosephosphates; Kinetics; Ligands; Phosphoenolpyruvate; Phosphofructokinase-1; Protein Conformation; Spectrometry, Fluorescence; Time Factors; Tryptophan

1995
A chimeric bacterial phosphofructokinase exhibits cooperativity in the absence of heterotropic regulation.
    The Journal of biological chemistry, 1995, Feb-24, Volume: 270, Issue:8

    Topics: Adenylyl Imidodiphosphate; Base Sequence; Crystallography, X-Ray; DNA Primers; Enzyme Stability; Escherichia coli; Fluorescence Polarization; Fructosephosphates; Geobacillus stearothermophilus; Kinetics; Molecular Sequence Data; Phosphofructokinase-1; Protein Binding; Protein Conformation; Recombinant Fusion Proteins; Temperature

1995
Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding.
    Proteins, 2017, Volume: 85, Issue:1

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Binding Sites; Cattle; Citric Acid; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Fructosephosphates; Gene Expression; Humans; Isoenzymes; Kinetics; Models, Molecular; Myocardium; Phosphofructokinase-2; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Recombinant Proteins; Species Specificity; Substrate Specificity

2017