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Pier Paolo Scaglioni

Researcher at University of Texas Southwestern Medical Center

Publications -  70
Citations -  5255

Pier Paolo Scaglioni is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Hepatitis B virus & KRAS. The author has an hindex of 32, co-authored 68 publications receiving 4762 citations. Previous affiliations of Pier Paolo Scaglioni include Harvard University & University of Cincinnati Academic Health Center.

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The Mechanisms of PML-Nuclear Body Formation

TL;DR: It is demonstrated that PML contains a SUMO binding motif that is independent of its SUMOylation sites and is surprisingly necessary for PML-NB formation, and it is proposed that the PML RING domain is critical forPML SUMoylation and PML -NB formation.
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Identification of a tumour suppressor network opposing nuclear Akt function

TL;DR: It is demonstrated that Pml orchestrates a nuclear tumour suppressor network for inactivation of nuclear pAkt, and thus highlights the importance of AKT compartmentalization in human cancer pathogenesis and treatment.
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Aldehyde dehydrogenase activity selects for lung adenocarcinoma stem cells dependent on Notch signaling

TL;DR: Findings indicate that ALDH selects for a subpopulation of self-renewing NSCLC stem-like cells with increased tumorigenic potential, that NSCLCs harboring tumor cells with ALDH1A1 expression have inferior prognosis, and that AL DH 1A1 and CD133 identify different tumor subpopulations.
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Hepatitis B virus mutants associated with 3TC and famciclovir administration are replication defective

TL;DR: Findings show that 3TC and Famciclovir selected mutations alter the properties of the HBV reverse transcriptase, resulting in impaired viral replication within the cell.
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PML regulates p53 stability by sequestering Mdm2 to the nucleolus.

TL;DR: PML enhances p53 stability by sequestering Mdm2 to the nucleolus and physically associates with the nucleolar protein L11, and that L11 knockdown impairs the ability of PML to localize to nucleoli after DNA damage, demonstrating an unexpected role ofPML in theucleolar network for tumour suppression.