Xiaoming Yang
Sichuan University
9 Papers
75 Citations
Xiaoming Yang is an academic researcher from Sichuan University. The author has contributed to research in topics: PLK1 & Phosphorylation. The author has an hindex of 8, co-authored 9 publications. Previous affiliations of Xiaoming Yang include Purdue University & Southwest University.
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Papers
Label-free fluorimetric detection of CEA using carbon dots derived from tomato juice.
TL;DR: A label-free sensitive assay for detecting carcinoembryonic antigen (CEA) in a continuous and recyclable way has been proposed on the basis of adsorption and desorption of aptamers by the surface of CDs through a competitive mechanism.
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Plk1-mediated Phosphorylation of Topors Regulates p53 Stability
Xiaoming Yang,Hongchang Li,Zinan Zhou,Wen-Horng Wang,Anping Deng,Ourania M. Andrisani,Xiaoqi Liu +6 more
TL;DR: It is demonstrated that Plk1 modulates Topors activity in suppressing p53 function and a likely mechanism for the tumorigenic potential of Plk 1 is identified.
94
Phosphorylation of CLIP-170 by Plk1 and CK2 promotes timely formation of kinetochore-microtubule attachments.
TL;DR: Polo‐like kinase 1 (Plk1) and casein kinase 2 (CK2) are identified as two kinases of CLIP‐170 and S195 and S1318 are mapped as their respective phosphorylation sites, confirming that Plk1‐ and CK2‐associated phosphorylations of CLip‐170 are involved in the timely formation of kinetochore–microtubule attachments in mitosis.
Plk1 phosphorylation of TRF1 is essential for its binding to telomeres.
TL;DR: It is suggested that Plk1-mediated phosphorylation is involved in both TRF1 overexpression-induced apoptosis and its telomeric DNA binding ability.
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Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear envelope breakdown during prophase
TL;DR: It is shown that in mammalian cells both Plk1 and p150Glued regulate NEBD and that PlK1 interacts with and phosphoryates p 150Glued during NEBD at prophase, and that plk1 phosphorylates p150 Glued at Ser-179 and that the pS179 epitope is generated at the nuclear envelope of prophase cells.
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