FERONIA phosphorylates E3 ubiquitin ligase ATL6 to modulate the stability of 14-3-3 proteins in response to the carbon/nitrogen ratio
Copyright policy ) Qiansi Chen; Limei Song; Xu Guoyun; Guoqiang Zhao; Feng Yu; Feng Yu; Feng Yu; Hongdong Liao; Zhang Hui; Fucheng Lin; Huina Zhou; Weijun Chen;
FERONIA phosphorylates E3 ubiquitin ligase ATL6 to modulate the stability of 14-3-3 proteins in response to the carbon/nitrogen ratio
This study reveals a novel regulatory mechanism that links the versatile receptor kinase FERONIA with plant C/N responses.
- Rice University United States
- Hunan Women'S University China (People's Republic of)
- Zhejiang University China (People's Republic of)
- Zhejiang Ocean University China (People's Republic of)
- China National Hybrid Rice R&D Central Hunan Hybrid Rice Reserch Center China (People's Republic of)
Arabidopsis Proteins, Nitrogen, Peptide Hormones, Ubiquitin-Protein Ligases, Phosphotransferases, Research Papers, Models, Biological, Carbon, 14-3-3 Proteins, Amino Acid Sequence, Phosphorylation, Protein Binding
Arabidopsis Proteins, Nitrogen, Peptide Hormones, Ubiquitin-Protein Ligases, Phosphotransferases, Research Papers, Models, Biological, Carbon, 14-3-3 Proteins, Amino Acid Sequence, Phosphorylation, Protein Binding
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selected citations
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These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
Citations provided by BIP!popularityPopularity provided by BIP!
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
Popularity provided by BIP! 53
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