about
The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damageEndothelial activation by angiotensin II through NFkappaB and p38 pathways: Involvement of NFkappaB-inducible kinase (NIK), free oxygen radicals, and selective inhibition by aspirinDifferential roles of p300 and PCAF acetyltransferases in muscle differentiationBinding of CDK9 to TRAF2Genome-wide identification of direct HBx genomic targetsTP63 and TP73 in cancer, an unresolved "family" puzzle of complexity, redundancy and hierarchy.Structure, function and regulation of p63 and p73.Metformin-induced ablation of microRNA 21-5p releases Sestrin-1 and CAB39L antitumoral activities.p300 is required for MyoD-dependent cell cycle arrest and muscle-specific gene transcriptionThe p53/p63/p73 family of transcription factors: overlapping and distinct functions.Occult hepatitis B virus infection.Treatment with arsenic trioxide (ATO) and MEK1 inhibitor activates the p73-p53AIP1 apoptotic pathway in leukemia cells.The transcriptional coactivator Yes-associated protein drives p73 gene-target specificity in response to DNA Damage.Replicative and transcriptional activities of hepatitis B virus in patients coinfected with hepatitis B and hepatitis delta viruses.Viral hepatitis and liver cancer: the case of hepatitis C.Viral determinants and host immune responses in the pathogenesis of HBV infection.p53-paralog DNp73 oncogene is repressed by IFNα/STAT2 through the recruitment of the Ezh2 polycomb group transcriptional repressor.Chromatin dynamics of gene activation and repression in response to interferon alpha (IFN(alpha)) reveal new roles for phosphorylated and unphosphorylated forms of the transcription factor STAT2IL6 Inhibits HBV Transcription by Targeting the Epigenetic Control of the Nuclear cccDNA Minichromosome.In vivo activity of the hepatitis B virus core promoter: tissue specificity and temporal regulation.Cytotoxic T lymphocyte response to a wild type hepatitis B virus epitope in patients chronically infected by variant viruses carrying substitutions within the epitope.The histone deacetylase inhibiting drug Entinostat induces lipid accumulation in differentiated HepaRG cells.The sodium/iodide symporter NIS is a transcriptional target of the p53-family members in liver cancer cells.Long-lasting memory T cell responses following self-limited acute hepatitis BNuclear HBx binds the HBV minichromosome and modifies the epigenetic regulation of cccDNA function.Control of cccDNA function in hepatitis B virus infection.The p53 family protein p73 provides new insights into cancer chemosensitivity and targeting.Treatment of chronic hepatitis B: update of the recommendations from the 2007 Italian Workshop.Molecular mechanisms of HBV-associated hepatocarcinogenesis.Physical interaction with human tumor-derived p53 mutants inhibits p63 activities.Reactive oxygen intermediates (ROIs) are involved in the intracellular transduction of angiotensin II signal in C2C12 cells.The hepatitis B virus (HBV) pX transactivates the c-fos promoter through multiple cis-acting elements.Two new p73 splice variants, gamma and delta, with different transcriptional activity.ChIP-on-chip analysis of in vivo mutant p53 binding to selected gene promoters.Towards an HBV cure: state-of-the-art and unresolved questions--report of the ANRS workshop on HBV cure.Reciprocal antagonism between the netrin-1 receptor uncoordinated-phenotype-5A (UNC5A) and the hepatitis C virus.Mechanisms of HBV-induced hepatocellular carcinoma.Direct-acting antiviral therapy decreases hepatocellular carcinoma recurrence rate in cirrhotic patients with chronic hepatitis C.Current treatments for chronic hepatitis B virus infections.Aiming for cure in HBV and HDV infection.
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Q22010200-E7FDF5A3-344E-4A83-AE6E-F78F1C426B4EQ28195708-5A1A0D2B-6EB6-4E58-8E7C-9AF5A706945BQ28276083-6E6DDCE7-E043-4E2E-9FAD-6E1978DCF7BEQ28289684-C0540648-A35E-481E-96AB-C5D5452BD9ACQ29048191-E3CFDCC8-4FEE-4003-9DD1-D8026DE0FE1EQ33358710-F8F4D89F-D5AA-4DC8-B8F2-31040794CEF8Q33818611-A5CA8CBC-A78B-4939-87F2-2F74658D9BB1Q33885363-4C7EA691-8E8E-41D4-8CE9-38B61D5384EAQ33886012-8D662632-D5A8-4BDE-8012-3CD1DA04311FQ33893917-70695676-46DC-462E-AD5F-91D022C812A2Q34160162-3E1F2FAE-D21C-4956-A34C-335869C9A4CEQ34306995-2C3133D0-8E3F-4C57-8086-7A09AD5CA4C7Q34418866-DD4BC8CD-5429-4DA0-95B3-54EF211916F4Q34457758-3FE618E2-2D63-4BC7-9427-89D76EE5967FQ34568619-D3F81147-EB28-401B-95DE-7DED255E407BQ34737124-E8A38F24-5D32-4867-9F73-9BF2CB34AB00Q35042810-AA00ADCD-B389-4661-99DA-79753DEE00A3Q35063436-62E1E150-44AA-4932-A92D-1F664D9B7F7CQ35845361-7264B4B1-BD9A-45AA-993D-808F64676B36Q35846709-193DC975-D6FA-42A5-A976-1490A63F03AAQ36363678-792596D0-5AEE-4D35-ACD5-39AD71DEB184Q37019277-9D239FF8-A7E6-41A9-BE56-3888B287C986Q37211959-6B7913F9-D907-448A-ADF8-D961D3927776Q37359318-27D2A25E-604E-449A-AE38-5FBCEF1F6219Q37418293-DEE2A10A-B1F7-4B8B-8D4D-30E6928E4178Q37555389-DAAFCFC5-BBD8-4BD1-B480-D8B9629769BCQ37622615-CA0629C0-FA93-459E-8873-20B9AD01799EQ37833228-C97C314F-9CE6-4EE3-83E7-492E51DC20EBQ38113182-1DC003B6-0333-4866-828C-CFE0DCA91CF9Q38291171-76BB3E67-3D0E-45D8-BA4E-B2D4270665ADQ38297415-7EE2898D-BFB3-4712-90B8-EE33CCD23B8FQ38318640-B8D235BB-342E-4023-B089-B2B12B39ACB1Q38331619-0390ADFC-156F-46F9-9AE0-45F4C76EAA1DQ38337212-0C129822-085B-4C18-B88D-2021FA872800Q38351585-9A62F43D-2CAA-4D99-9986-8135DB36B5E4Q38637134-2A566ACF-19CC-469A-8CB0-9C9519D74134Q38809557-90893EFA-B797-4A04-8160-77B65A9FE24AQ38830251-87039E89-6CEB-41E6-A654-AF18127DC608Q38851374-79DD7CCA-78CC-422B-9341-543F440674F1Q38857429-74C7C29A-09E1-4517-BAFE-1D637BCB5176
P50
description
Forscher
@de
chercheur
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investigador
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researcher
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ricercatore
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wetenschapper
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研究者
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name
Levrero M
@ast
Levrero M
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Levrero M
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Massimo Levrero
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Levrero M
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Levrero M
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Levrero M
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Massimo Levrero
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altLabel
Levrero M
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Levrero M
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Levrero M
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Levrero M
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Massimo Levrero
@en
P31
P496
0000-0002-4978-0875