The large and small isoforms of human papillomavirus type 16 E6 bind to and differentially affect procaspase 8 stability and activity - Wikidata - wikimedia - TriplyDB

The large and small isoforms of human papillomavirus type 16 E6 bind to and differentially affect procaspase 8 stability and activity

The large and small isoforms of human papillomavirus type 16 E6 bind to and differentially affect procaspase 8 stability and activity

http://www.wikidata.org/entity/Q35785399

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Recent Progress in Therapeutic Treatments and Screening Strategies for the Prevention and Treatment of HPV-Associated Head and Neck Cancer Functional Roles of E6 and E7 Oncoproteins in HPV-Induced Malignancies at Diverse Anatomical Sites A Small Molecule Inhibitor Selectively Induces Apoptosis in Cells Transformed by High Risk Human Papilloma Viruses Flavonol and imidazole derivatives block HPV16 E6 activities and reactivate apoptotic pathways in HPV⁺ cells Papillomavirus E6 oncoproteins.The full-length isoform of human papillomavirus 16 E6 and its splice variant E6* bind to different sites on the procaspase 8 death effector domain.Comparative analysis of HPV16 gene expression profiles in cervical and in oropharyngeal squamous cell carcinoma.Alternative splicing of human papillomavirus type-16 E6/E6* early mRNA is coupled to EGF signaling via Erk1/2 activation.Biological Features of Human Papillomavirus-related Head and Neck Cancers Contributing to Improved Response.Regulation of HPV16 E6 and MCL1 by SF3B1 inhibitor in head and neck cancer cells.Small molecule inhibitors of the HPV16-E6 interaction with caspase 8 Human papillomavirus 16 E6 variants differ in their dysregulation of human keratinocyte differentiation and apoptosis.HPV E6 proteins target Ubc9, the SUMO conjugating enzyme.p53 degradation activity, expression, and subcellular localization of E6 proteins from 29 human papillomavirus genotypes.Two less common human microRNAs miR-875 and miR-3144 target a conserved site of E6 oncogene in most high-risk human papillomavirus subtypes The influenza A virus spliced messenger RNA M mRNA3 is not required for viral replication in tissue culture Cellular binding partners of the human papillomavirus E6 protein.Human papillomavirus: gene expression, regulation and prospects for novel diagnostic methods and antiviral therapies Modulation of apoptotic pathways by human papillomaviruses (HPV): mechanisms and implications for therapy.Cleavage of the Junin virus nucleoprotein serves a decoy function to inhibit the induction of apoptosis during infection.Viral subversion of apoptotic enzymes: escape from death row.Cellular transformation by human papillomaviruses: lessons learned by comparing high- and low-risk viruses Complexes of human papillomavirus type 16 E6 proteins form pseudo-death-inducing signaling complex structures during tumor necrosis factor-mediated apoptosis.Human papillomaviruses, cervical cancer and cell polarity.Papillomavirus E6 proteins.The small splice variant of HPV16 E6, E6, reduces tumor formation in cervical carcinoma xenografts The critical protein interactions and structures that elicit growth deregulation in cancer and viral replication.Human papillomavirus early proteins and apoptosis.Manipulation of cellular DNA damage repair machinery facilitates propagation of human papillomaviruses.Functional effects of sequence variations in the E6 and E2 genes of human papillomavirus 16 European and Asian variants.The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8.The human papillomavirus (HPV) E6* proteins from high-risk, mucosal HPVs can direct degradation of cellular proteins in the absence of full-length E6 protein.Human papillomavirus type 16 E6 and E7 oncoproteins act synergistically to cause head and neck cancer in mice.The Role of E6 Spliced Isoforms (E6*) in Human Papillomavirus-Induced Carcinogenesis.A quantitative LumiFluo assay to test inhibitory compounds blocking p53 degradation induced by human papillomavirus oncoprotein E6 in living cells.

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P2860

The large and small isoforms of human papillomavirus type 16 E6 bind to and differentially affect procaspase 8 stability and activity

http://www.wikidata.org/entity/Q35785399

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2007 nî lūn-bûn

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The large and small isoforms o ...... spase 8 stability and activity

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The large and small isoforms o ...... spase 8 stability and activity

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The large and small isoforms o ...... spase 8 stability and activity

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P1433

Journal of Virology

P1476

The large and small isoforms o ...... spase 8 stability and activity

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P2093

Kadia Williams

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Maria Filippova

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Marnelli Bautista

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Melyssa M Johnson

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Nadja Fodor

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Sandy S Tungteakkhun

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Valery Filippov

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P2860

Interaction of oncogenic papillomavirus E6 proteins with fibulin-1

Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein

Interaction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducers

Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein

Human papillomavirus oncoprotein E6 binds to the C-terminal region of human minichromosome maintenance 7 protein

Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins

Interaction of zyxin, a focal adhesion protein, with the e6 protein from human papillomavirus type 6 results in its nuclear translocation

Human papillomavirus oncoprotein E6 inactivates the transcriptional coactivator human ADA3

Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase

The E6 oncoproteins of high-risk papillomaviruses bind to a novel putative GAP protein, E6TP1, and target it for degradation

P304

4116-4129

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scholarly article

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10.1128/JVI.01924-06

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P433

8

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81

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Penelope Duerksen-Hughes

P577

2007-01-31T00:00:00Z

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P5875

6537999

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17267478

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P932

1866154

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