2003
DOI: 10.1016/s0885-5765(03)00062-6
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MALDI-Qq-TOF-MS and transient gene expression analysis indicated co-enhancement of β-1,3-glucanase and endochitinase by tMEK2 and the involvement of divergent pathways

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Cited by 16 publications
(8 citation statements)
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“…Overexpression of tMEK2 MUT in tomato enhanced resistance to the bacterial pathogen Pseudomonas syringae pv. tomato and activated different pathways in biotic stress responses (Xing et al 2001(Xing et al , 2003. Transgenic wheat overexpressing tomato tMEK2 MUT also exhibited enhanced resistance to leaf rust (Puccinia triticina) Fan et al 2009).…”
Section: Introductionmentioning
confidence: 99%
“…Overexpression of tMEK2 MUT in tomato enhanced resistance to the bacterial pathogen Pseudomonas syringae pv. tomato and activated different pathways in biotic stress responses (Xing et al 2001(Xing et al , 2003. Transgenic wheat overexpressing tomato tMEK2 MUT also exhibited enhanced resistance to leaf rust (Puccinia triticina) Fan et al 2009).…”
Section: Introductionmentioning
confidence: 99%
“…tMEK2 (also named LeMKK2) is a known MAPK kinase in tomato and was previously shown to regulate the expression of antifungal factors including β-1,3-glucanase and endochitinase in response to pathogen attacks. 24 2DE was used to compare wild type tomatoes and transgenic tomato carrying tMEK2 MUT , in which the tMEK2 was constitutively actived by replacing amino acid Ser-221 and Thr-226 between sub-domains VII and VIII with glutamic acid. 24 LC-MS/MS analysis revealed a group of phosphoproteins in tMEK2…”
Section: Nucleoside Diphosphate Protein Kinasementioning
confidence: 99%
“…24 2DE was used to compare wild type tomatoes and transgenic tomato carrying tMEK2 MUT , in which the tMEK2 was constitutively actived by replacing amino acid Ser-221 and Thr-226 between sub-domains VII and VIII with glutamic acid. 24 LC-MS/MS analysis revealed a group of phosphoproteins in tMEK2…”
Section: Nucleoside Diphosphate Protein Kinasementioning
confidence: 99%
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“…Proteomics has thus far mostly been used to seek out under-and over-expression of proteins separated by twodimensional electrophoresis, in experiments that are comparable to nucleic acid microarray experiments in genomics (e.g., Xing et al 2003). The two-dimensional gel is in fact a protein array with molecular weight and isoelectric point dimensions, and proteins from it can usually be identified successfully by peptide mass fingerprinting or de novo sequencing (Standing 2003), in either case using a matrixassisted laser desorption ionization time-of-flight mass spectrometer.…”
Section: Proteomicsmentioning
confidence: 99%