2014
DOI: 10.4161/15592316.2014.972845
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Protein phosphorylation in stomatal movement

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Cited by 63 publications
(47 citation statements)
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“…The ability to measure a variety of PTMs is a unique aspect of advanced proteomics technologies. Currently, more than 200 biological relevant PTMs have been reported [47] and several types of them, such as phosphorylation, acetylation, glycosylation, and thiol-based redox modifications, have been studied extensively [24,32,4850]. …”
Section: Ms-based Ptm Profilingmentioning
confidence: 99%
“…The ability to measure a variety of PTMs is a unique aspect of advanced proteomics technologies. Currently, more than 200 biological relevant PTMs have been reported [47] and several types of them, such as phosphorylation, acetylation, glycosylation, and thiol-based redox modifications, have been studied extensively [24,32,4850]. …”
Section: Ms-based Ptm Profilingmentioning
confidence: 99%
“…MPK4 is activated by upstream kinases in response to developmental cues, pathogen invasion or other environmental changes, and then interacts with and phosphorylates downstream substrates. 32 AtMKK2 and AtMEK1 (AtMKK1) are two MAP kinase kinases (MAPKKs), which share 65% sequence identity. 33 In a yeast two-hybrid (Y2H) assay, AtMEK1 and AtMKK2 specifically interacted with AtMPK4.…”
Section: Mpk4 Signaling Cascadementioning
confidence: 99%
“…Protein phosphorylation is the most studied PTMS and its elucidation is a central goal of functional proteomics research in plant biology. Many studies have been reported about their role in abiotic‐stress, energy metabolism, hormone regulation, etc. However, the analysis of phosphoproteins on a proteome‐wide scale has been less well studied in relation to anther development (Table ).…”
Section: Phosphoproteomic Studies On Anther and Pollen Developmentmentioning
confidence: 99%