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Bo Lv
Researcher at Fudan University
Publications - 9
Citations - 699
Bo Lv is an academic researcher from Fudan University. The author has contributed to research in topics: Abiotic stress & Arabidopsis. The author has an hindex of 7, co-authored 8 publications receiving 515 citations.
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Journal ArticleDOI
A Rice NAC Transcription Factor Promotes Leaf Senescence via ABA Biosynthesis
Chanjuan Mao,Lu Songchong,Bo Lv,Bin Zhang,Jiabin Shen,He Jianmei,Liqiong Luo,Dandan Xi,Xu Chen,Feng Ming +9 more
TL;DR: A rice NAC transcription factor, OsNAC2, that participates in ABA-induced leaf senescence and elucidates the transcriptional network of ABA production during leaf senesence in rice is demonstrated.
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The NAC Family Transcription Factor OsNAP Confers Abiotic Stress Response Through the ABA Pathway
TL;DR: OsNAP functions as a transcriptional activator that plays a role in mediating abiotic stress responses in rice, and microarray analysis of transgenic plants overexpressing OsNAP revealed that many stress-related genes were up-regulated.
Journal ArticleDOI
The NAC-type transcription factor OsNAC2 regulates ABA-dependent genes and abiotic stress tolerance in rice.
TL;DR: The results suggest that in rice OsNAC2 regulates both abiotic stress responses and ABA-mediated responses, and acts at the junction between the ABA and abiotic Stress pathways.
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OsNAC2 encoding a NAC transcription factor that affects plant height through mediating the gibberellic acid pathway in rice
Xu Chen,Lu Songchong,Yaofeng Wang,Xuan Zhang,Bo Lv,Liqiong Luo,Dandan Xi,Jiabin Shen,Hong Ma,Feng Ming +9 more
TL;DR: It is proposed that OsNAC2 is a negative regulator of the plant height and flowering time, which acts by directly regulating key genes of the GA pathway in rice.
Journal ArticleDOI
RcLEA, a late embryogenesis abundant protein gene isolated from Rosa chinensis, confers tolerance to Escherichia coli and Arabidopsis thaliana and stabilizes enzyme activity under diverse stresses
TL;DR: In vitro analysis showed that RcLEA was able to prevent the freeze–thaw-induced inactivation or heat-induced aggregation of various substrates, such as lactate dehydrogenase and citrate synthase, and protected the proteome of E. coli from denaturation when the proteins were heat-shocked or subjected to acidic conditions.