Ling Cheng
South China Agricultural University
6 Papers
8 Citations
Ling Cheng is an academic researcher from South China Agricultural University. The author has contributed to research in topics: Bimolecular fluorescence complementation & Gene. The author has an hindex of 1, co-authored 6 publications.
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Papers
Characterization of the key region and putative phosphorylation sites of EcaICE1 in its molecular interaction with the EcaHOS1 protein in Eucalyptus camaldulensis.
TL;DR: This is the first report that EcaICE1 can interact with the EcaHOS1 protein in Eucalyptus, and it is identified as the key putative phosphorylation site for its interaction with the N-terminus of Ecaice1 protein.
Characterization of transcription activation domain of EcaICE1 and its interaction with EcaSIZ1 in Eucalyptus camaldulensis
TL;DR: In this paper, the subcellular localization of EcaICE1 and its interaction with EcaSIZ1 in Eucalyptus camaldulensis were reported.
Patent
Method for performing forest tree multiple-trait pyramiding breeding based on multiple-trait genomic selection
Yuanzhen Lin,Weihua Zhang,Zhang Xinfei,Ling Cheng,Zhang Xinxin,Zhou Wei +5 more
- 31 May 2017
TL;DR: In this paper, a method for performing forest tree multiple-trait pyramiding breeding based on multiple-triggered genomic selection is presented, which has the benefits that the workload of forest tree trait phenotype determination can be reduced, and no lamination by the correlation degree between traits and markers exists.
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Characterization of the Key Region and Phosphorylation Sites of EcaICE1 for its Molecular Interaction with EcaHOS1 Protein from Eucalyptus camaldulensis
TL;DR: It is reported that EcaICE1 could interact with EcaHOS1 protein in Eucalyptus, and identified Ser 158 of Ecaice1 as the key phosphorylation site for its interaction with ECAH OS1 protein.
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Characterization of transcription activation domain of EcaICE1 and its interaction with EcaSIZ1 in Eucalyptus camaldulensis
TL;DR: The results showed that EcaICE1 may have a SUMOylation pathway similar to Arabidopsis thaliana, and it was confirmed that the amino acid region from position 84 to 126 in ECAICE1 was critical for the strong transactivation activity of Eca ICE1.