标题
Dual binding of 14-3-3 protein regulates Arabidopsis nitrate reductase activity
作者
关键词
Phosphorylation, Acidic motif, 14-3-3, Nitrate reductase, Regulation
出版物
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 20, Issue 2, Pages 277-286
出版商
Springer Nature
发表日期
2015-01-12
DOI
10.1007/s00775-014-1232-4
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Specificity of ε and Non-ε Isoforms of Arabidopsis 14-3-3 Proteins Towards the H+-ATPase and Other Targets
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- The role of protein disorder in the 14-3-3 interaction network
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- Plant 14-3-3 proteins catch up with their mammalian orthologs
- (2009) Claudia Oecking et al. CURRENT OPINION IN PLANT BIOLOGY
- Recognition of an intra-chain tandem 14-3-3 binding site within PKCɛ
- (2009) Brenda Kostelecky et al. EMBO REPORTS
- A novel pocket in 14-3-3ɛ is required to mediate specific complex formation with cdc25C and to inhibit cell cycle progression upon activation of checkpoint pathways
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- Ribosome and transcript copy numbers, polysome occupancy and enzyme dynamics in Arabidopsis
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