Compounds > threonine

threonine and fusicoccin

threonine has been researched along with fusicoccin in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (40.00)29.6817
2010's3 (60.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Batoko, H; Boutry, M; Gevaert, K; Maudoux, O; Morsomme, P; Oecking, C; Vandekerckhove, J1
Kinoshita, T; Shimazaki, K1
Bobik, K; Boutry, M; Duby, G; Kanczewska, J; Nizet, Y; Stiernet, P; Vandermeeren, C1
Inoue, S; Ishizaki, K; Kinoshita, T; Kohchi, T; Okumura, M; Takahashi, K1
Inoue, S; Kinoshita, T; Okumura, M; Takahashi, K1

Other Studies

5 other study(ies) available for threonine and fusicoccin

ArticleYear
A plant plasma membrane H+-ATPase expressed in yeast is activated by phosphorylation at its penultimate residue and binding of 14-3-3 regulatory proteins in the absence of fusicoccin.
    The Journal of biological chemistry, 2000, Jun-09, Volume: 275, Issue:23

    Topics: 14-3-3 Proteins; Amino Acid Sequence; Cell Membrane; Cloning, Molecular; Enzyme Inhibitors; Fungal Proteins; Glycosides; Isoenzymes; Kinetics; Molecular Sequence Data; Nicotiana; Peptide Fragments; Phosphorylation; Plants, Toxic; Proteins; Proton-Translocating ATPases; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Threonine; Tyrosine 3-Monooxygenase

2000
Biochemical evidence for the requirement of 14-3-3 protein binding in activation of the guard-cell plasma membrane H+-ATPase by blue light.
    Plant & cell physiology, 2002, Volume: 43, Issue:11

    Topics: 14-3-3 Proteins; Amino Acid Sequence; Cell Membrane; Glycosides; Light; Molecular Sequence Data; Phosphorylation; Pigments, Biological; Plant Epidermis; Protein Binding; Proton-Translocating ATPases; Sequence Homology, Amino Acid; Threonine; Tyrosine 3-Monooxygenase; Vicia

2002
Two widely expressed plasma membrane H(+)-ATPase isoforms of Nicotiana tabacum are differentially regulated by phosphorylation of their penultimate threonine.
    The Plant journal : for cell and molecular biology, 2010, Volume: 62, Issue:2

    Topics: Cell Membrane; Cells, Cultured; Cold Temperature; Gene Expression Regulation, Plant; Glycosides; Isoenzymes; Nicotiana; Phosphorylation; Plant Proteins; Plants, Genetically Modified; Proton-Translocating ATPases; Threonine

2010
Characterization of the plasma membrane H+-ATPase in the liverwort Marchantia polymorpha.
    Plant physiology, 2012, Volume: 159, Issue:2

    Topics: 14-3-3 Proteins; Amino Acid Sequence; Arabidopsis; Cell Membrane; Expressed Sequence Tags; Genes, Plant; Glycosides; Isoenzymes; Light; Mannose; Marchantia; Marine Toxins; Molecular Sequence Data; Osmotic Pressure; Oxazoles; Phosphorylation; Photosynthesis; Phylogeny; Plant Proteins; Protein Binding; Proton-Translocating ATPases; Sucrose; Threonine

2012
Evolutionary appearance of the plasma membrane H (+) -ATPase containing a penultimate threonine in the bryophyte.
    Plant signaling & behavior, 2012, Volume: 7, Issue:8

    Topics: Amino Acid Sequence; Arabidopsis; Bryopsida; Cell Membrane; Chara; Evolution, Molecular; Glycosides; Molecular Sequence Data; Phosphorylation; Phylogeny; Proton-Translocating ATPases; Threonine

2012