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Hans Will

Researcher at Heinrich Pette Institute

Publications -  237
Citations -  15836

Hans Will is an academic researcher from Heinrich Pette Institute. The author has contributed to research in topics: Hepatitis B virus & Virus. The author has an hindex of 67, co-authored 235 publications receiving 15405 citations. Previous affiliations of Hans Will include Heidelberg University & Leibniz Association.

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Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2

TL;DR: It is demonstrated that the human serine/threonine kinase homeodomain-interacting protein kinase-2 colocalizes and interacts with p53 and CREB-binding protein (CBP) within promyelocytic leukaemia (PML) nuclear bodies and implies that HIPK2 is a novel regulator of p53 effector functions involved in cell growth, proliferation and apoptosis.
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A novel method for efficient amplification of whole hepatitis B virus genomes permits rapid functional analysis and reveals deletion mutants in immunosuppressed patients.

TL;DR: It is suggested that HBV genomes with C gene deletions can have a selective advantage in immunosuppressed patients and the potential for the structural and functional characterization of heterogeneous populations of complete virion-encapsidated HBV DNAs is demonstrated.
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Repopulation of mouse liver with human hepatocytes and in vivo infection with hepatitis B virus

TL;DR: Partial repopulation of the liver of immunodeficient urokinase‐type plasminogen activator (uPA)/recombinant activation gene‐2 (RAG‐2) mice with normal human hepatocytes isolated from the adult liver is reported, providing proof that normalhuman hepatocytes can integrate into the mouse hepatic parenchyma, undergo multiple cell divisions, and remain permissive for a human hepatotropic virus in a xenogenic liver.
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Regulation of p53 activity in nuclear bodies by a specific PML isoform

TL;DR: The results indicate the existence of a cross‐talk between PML‐ and p53‐dependent growth suppression pathways, implying an important role for NBs and their resident proteins as modulators of p53 functions.