Compounds > fructose 2,6-diphosphate
Page last updated: 2024-08-26

fructose 2,6-diphosphate and ethylmaleimide

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

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19904 (66.67)18.7374
1990's2 (33.33)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Fromm, HJ; Liu, F1
Hubert, E; Reyes, A; Slebe, JC2
Meek, DW; Nimmo, HG1
Bravo, N; Iriarte, A; Ludwig, H; Reyes, AM; Slebe, JC1
Li, L; Ling, S; Wu, Cl; Xu, G; Yao, W1

Other Studies

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

ArticleYear
Relationship between thiol group modification and the binding site for fructose 2,6-bisphosphate on rabbit liver fructose-1,6-bisphosphatase.
    The Journal of biological chemistry, 1988, Jul-15, Volume: 263, Issue:20

    Topics: Adenosine Monophosphate; Allosteric Site; Animals; Binding Sites; Binding, Competitive; Chemical Phenomena; Chemistry; Ethylmaleimide; Fructose-Bisphosphatase; Fructosediphosphates; Hexosediphosphates; Kinetics; Liver; Rabbits; Structure-Activity Relationship; Sulfhydryl Compounds

1988
The reactive cysteine residue of pig kidney fructose 1,6-bisphosphatase is related to a fructose 2,6-bisphosphate allosteric site.
    Biochemical and biophysical research communications, 1985, Feb-28, Volume: 127, Issue:1

    Topics: Animals; Binding Sites; Cysteine; Enzyme Activation; Ethylmaleimide; Fructose-Bisphosphatase; Fructosediphosphates; Hexosediphosphates; Kidney; Potassium; Swine

1985
Activation of fructose-1,6-bisphosphatases by monovalent cations and its relationship with a fructose-2,6-bisphosphate allosteric site.
    Archivos de biologia y medicina experimentales, 1985, Volume: 18, Issue:3-4

    Topics: Animals; Binding Sites; Cyanates; Cysteine; Enzyme Activation; Ethylmaleimide; Fructose-Bisphosphatase; Fructosediphosphates; Hexosediphosphates; Kidney; Kinetics; Magnesium; Potassium; Swine

1985
The interaction of fructose 2,6-bisphosphate with an allosteric site of rat liver fructose 1,6-bisphosphatase.
    FEBS letters, 1983, Aug-22, Volume: 160, Issue:1-2

    Topics: Allosteric Regulation; Allosteric Site; Animals; Ethylmaleimide; Fructose-Bisphosphatase; Fructosediphosphates; Hexosediphosphates; Kinetics; Liver; Rats

1983
Modification of Cys-128 of pig kidney fructose 1,6-bisphosphatase with different thiol reagents: size dependent effect on the substrate and fructose-2,6-bisphosphate interaction.
    Journal of protein chemistry, 1993, Volume: 12, Issue:2

    Topics: Amino Acids; Animals; Cysteine; Ethylmaleimide; Fructose-Bisphosphatase; Fructosediphosphates; Kidney Cortex; Kinetics; Spectrophotometry, Ultraviolet; Substrate Specificity; Swine

1993
Separate bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: the role of the C-terminal tail in modulating enzyme activity.
    The Biochemical journal, 1997, Dec-15, Volume: 328 ( Pt 3)

    Topics: Animals; Binding Sites; Chickens; Circular Dichroism; Diethyl Pyrocarbonate; Enzyme Inhibitors; Escherichia coli; Ethylmaleimide; Fructosediphosphates; Glycerophosphates; Guanosine Triphosphate; Kinetics; Liver; Multienzyme Complexes; Mutagenesis, Site-Directed; Peptide Fragments; Phosphofructokinase-2; Phosphoric Monoester Hydrolases; Phosphotransferases; Protein Structure, Secondary; Rats; Recombinant Proteins; Sequence Deletion; Spectrometry, Fluorescence

1997