phosphoserine and fructose-1,6-diphosphate

phosphoserine has been researched along with fructose-1,6-diphosphate in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19901 (33.33)18.7374
1990's0 (0.00)18.2507
2000's1 (33.33)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Engström, L; Forsberg, PO; Humble, E; Nettelblad, FA1
Moreno, S; Portela, P; Rossi, S1
Bustos, DM; Guerrero, SA; Iglesias, AÁ; Piattoni, CV1

Other Studies

3 other study(ies) available for phosphoserine and fructose-1,6-diphosphate

ArticleYear
Aspects on the phosphorylation of muscle phosphofructokinase by protein kinase C--inhibition by phosphofructokinase stabilisers.
    Biochemical and biophysical research communications, 1986, Apr-29, Volume: 136, Issue:2

    Topics: Adenosine Monophosphate; Animals; Fructosediphosphates; Fructosephosphates; Kinetics; Muscles; Phosphofructokinase-1; Phosphorylation; Phosphoserine; Phosphothreonine; Protein Kinase C; Rabbits; Rats

1986
Characterization of yeast pyruvate kinase 1 as a protein kinase A substrate, and specificity of the phosphorylation site sequence in the whole protein.
    The Biochemical journal, 2006, May-15, Volume: 396, Issue:1

    Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Cattle; Consensus Sequence; Cyclic AMP-Dependent Protein Kinases; Electrophoresis, Polyacrylamide Gel; Fructosediphosphates; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Phosphorylation; Phosphoserine; Protein Binding; Protein Processing, Post-Translational; Reproducibility of Results; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Substrate Specificity

2006
Nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at serine-404 by an SNF1-related protein kinase allosterically inhibited by ribose-5-phosphate.
    Plant physiology, 2011, Volume: 156, Issue:3

    Topics: Allosteric Regulation; Amino Acid Sequence; Cations, Divalent; Endosperm; Fructosediphosphates; Glyceraldehyde-3-Phosphate Dehydrogenases; Glyceric Acids; Kinetics; Models, Biological; Molecular Sequence Data; Organ Specificity; Peptides; Phosphorylation; Phosphoserine; Protein Serine-Threonine Kinases; Ribosemonophosphates; Sequence Alignment; Triticum

2011