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Xu Qian

Researcher at Nanjing Medical University

Publications -  58
Citations -  3707

Xu Qian is an academic researcher from Nanjing Medical University. The author has contributed to research in topics: Medicine & Phosphorylation. The author has an hindex of 30, co-authored 42 publications receiving 2623 citations. Previous affiliations of Xu Qian include University of Texas MD Anderson Cancer Center & Yahoo!.

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MiR-145 directly targets p70S6K1 in cancer cells to inhibit tumor growth and angiogenesis

TL;DR: These studies suggest that miR-145 serves as a tumor suppressor which downregulates HIF-1 and VEGF expression by targeting p70S6K1, leading to the inhibition of tumor growth and angiogenesis.
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KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase.

TL;DR: The findings reveal an important mechanism of histone modification and demonstrate that local generation of succinyl-CoA by the nuclear α-KGDH complex coupled with the succinyltransferase activity of KAT2A is instrumental in histone succinylation, tumour cell proliferation, and tumour development.
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Nucleus-Translocated ACSS2 Promotes Gene Transcription for Lysosomal Biogenesis and Autophagy

TL;DR: It is demonstrated that glucose deprivation results in AMP-activated protein kinase (AMPK)-mediated acetyl-CoA synthetase 2 (ACSS2) phosphorylation at S659, which exposed the nuclear localization signal of ACSS2 for importin α5 binding and nuclear translocation.
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Phosphoglycerate Kinase 1 Phosphorylates Beclin1 to Induce Autophagy

TL;DR: This study unearths an important mechanism underlying cellular-stress-induced autophagy initiation in which the protein kinase activity of the metabolic enzyme PGK1 plays an instrumental role and reveals the significance of the mutual regulation ofautophagy and cell metabolism in maintaining cell homeostasis.
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Stabilization of phosphofructokinase 1 platelet isoform by AKT promotes tumorigenesis

TL;DR: It is shown that PFK1 platelet isoform is upregulated in Glioblastoma and is required for tumor growth mechanistically, such upregulation is due to an increased stability induced by AKT activation via phosphorylation on residue S386.