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231223s2009 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2009.01.005
|2 doi
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|a pubmed25n0623.xml
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|a (DE-627)NLM186750293
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|a (NLM)19250836
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Lin, Chung-Wen
|e verfasserin
|4 aut
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|a Early signalling pathways in rice roots under vanadate stress
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|c 2009
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 21.10.2009
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Vanadate is beneficial to plant growth at low concentration. However, plant exposure to high concentrations of vanadate has been shown to arrest cell growth and lead to cell death. We are interested in understanding the signalling pathways of rice roots in response to vanadate stress. In this study, we demonstrated that vanadate induced rice root cell death and suppressed root growth. In addition, we found that vanadate induced ROS accumulation, increased lipid peroxidation and elicited a remarkable increase of MAPKs and CDPKs activities in rice roots. In contrast, pre-treatment of rice roots with ROS scavenger (sodium benzoate), serine/threonine protein phosphatase inhibitor (endothall), and CDPK antagonist (W7), reduced the vanadate-induced MAPKs activation. Furthermore, the expression of a MAPK gene (OsMPK3) and four tyrosine phosphatase genes (OsDSP3, OsDSP5, OsDSP6, and OsDSP10) were regulated by vanadate in rice roots. Collectively, these results strongly suggest that ROS, protein phosphatase, and CDPK may function in the vanadate-triggered MAPK signalling pathway cause cell death and retarded growth in rice roots
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Dicarboxylic Acids
|2 NLM
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|a Enzyme Inhibitors
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Reactive Oxygen Species
|2 NLM
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|a Sulfonamides
|2 NLM
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|a endothall
|2 NLM
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|a 145-73-3
|2 NLM
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|a Vanadates
|2 NLM
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|a 3WHH0066W5
|2 NLM
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|a Malondialdehyde
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|a 4Y8F71G49Q
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|a W 7
|2 NLM
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|a 65595-90-6
|2 NLM
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|a Protein Kinases
|2 NLM
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|a EC 2.7.-
|2 NLM
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|a calcium-dependent protein kinase
|2 NLM
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|a EC 2.7.1.-
|2 NLM
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|a Mitogen-Activated Protein Kinases
|2 NLM
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|a EC 2.7.11.24
|2 NLM
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| 650 |
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|a Protein Phosphatase 1
|2 NLM
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|a EC 3.1.3.16
|2 NLM
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| 700 |
1 |
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|a Lin, Chung-Yi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chang, Ching-Chun
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lee, Ruey-Hua
|e verfasserin
|4 aut
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| 700 |
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|a Tsai, Tsung-Mu
|e verfasserin
|4 aut
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| 700 |
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|a Chen, Po-Yu
|e verfasserin
|4 aut
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| 700 |
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|a Chi, Wen-Chang
|e verfasserin
|4 aut
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| 700 |
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|a Huang, Hao-Jen
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 47(2009), 5 vom: 15. Mai, Seite 369-76
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
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|g volume:47
|g year:2009
|g number:5
|g day:15
|g month:05
|g pages:369-76
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|u http://dx.doi.org/10.1016/j.plaphy.2009.01.005
|3 Volltext
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