scholarly journals Solution Structure Analysis of the HPV16 E6 Oncoprotein Reveals a Self-Association Mechanism Required for E6-Mediated Degradation of p53

Structure ◽  
2012 ◽  
Vol 20 (4) ◽  
pp. 604-617 ◽  
Author(s):  
Katia Zanier ◽  
Abdellahi ould M'hamed ould Sidi ◽  
Charlotte Boulade-Ladame ◽  
Vladimir Rybin ◽  
Anne Chappelle ◽  
...  
Keyword(s):  
Structure Analysis ◽  
Solution Structure ◽  
Hpv16 E6 ◽  
E6 Oncoprotein ◽  
Self Association

Defining the minimal interacting regions of the tight junction protein MAGI-1 and HPV16 E6 oncoprotein for solution structure studies

2008 ◽  
Vol 60 (1) ◽  
pp. 64-73 ◽  
Author(s):  
Sebastian Charbonnier ◽  
Gunter Stier ◽  
Georges Orfanoudakis ◽  
Bruno Kieffer ◽  
R. Andrew Atkinson ◽  
...  
Keyword(s):  
Tight Junction ◽  
Solution Structure ◽  
Tight Junction Protein ◽  
Hpv16 E6 ◽  
E6 Oncoprotein ◽  
Junction Protein

scholarly journals HPV16 E6 oncoprotein‐induced upregulation of lncRNA GABPB1‐AS1 facilitates cervical cancer progression by regulating miR‐519e‐5p/Notch2 axis

2020 ◽  
Vol 34 (10) ◽  
pp. 13211-13223
Author(s):  
Rongying Ou ◽  
Mingfen Lv ◽  
Xuan Liu ◽  
Jiangmin Lv ◽  
Jinduo Zhao ◽  
...  
Keyword(s):  
Cervical Cancer ◽  
Cancer Progression ◽  
Hpv16 E6 ◽  
E6 Oncoprotein

scholarly journals Solution structures of long-acting insulin analogues and their complexes with albumin

2019 ◽  
Vol 75 (3) ◽  
pp. 272-282 ◽  
Author(s):  
Line A. Ryberg ◽  
Pernille Sønderby ◽  
Fabian Barrientos ◽  
Jens T. Bukrinski ◽  
Günther H. J. Peters ◽  
...  
Keyword(s):  
Solution Structure ◽  
Insulin Analogues ◽  
Size Exclusion ◽  
Life Extension ◽  
Once Daily ◽  
Solution Structures ◽  
X Ray Scattering ◽  
Exclusion Chromatography ◽  
Self Association ◽  
Long Acting

The lipidation of peptide drugs is one strategy to obtain extended half-lives, enabling once-daily or even less frequent injections for patients. The half-life extension results from a combination of self-association and association with human serum albumin (albumin). The self-association and association with albumin of two insulin analogues, insulin detemir and insulin degludec, were investigated by small-angle X-ray scattering (SAXS) and dynamic light scattering (DLS) in phenolic buffers. Detemir shows concentration-dependent self-association, with an equilibrium between hexamer, dihexamer, trihexamer and larger species, while degludec appears as a dihexamer independent of concentration. The solution structure of the detemir trihexamer has a bent shape. The stoichiometry of the association with albumin was studied using DLS. For albumin–detemir the molar stoichiometry was determined to be 1:6 (albumin:detemir ratio) and for albumin–degludec it was between 1:6 and 1:12 (albumin:degludec ratio). Batch SAXS measurements of a 1:6 albumin:detemir concentration series revealed a concentration dependence of complex formation. The data allowed the modelling of a complex between albumin and a detemir hexamer and a complex consisting of two albumins binding to opposite ends of a detemir dihexamer. Measurements of size-exclusion chromatography coupled to SAXS revealed a complex between a degludec dihexamer and albumin. Based on the results, equilibria for the albumin–detemir and albumin–degludec mixtures are proposed.

Solution Structure and Self-association Properties of the p8 TFIIH Subunit Responsible for Trichothiodystrophy

2007 ◽  
Vol 368 (2) ◽  
pp. 473-480 ◽  
Author(s):  
Marc Vitorino ◽  
Frédéric Coin ◽  
Olga Zlobinskaya ◽  
R. Andrew Atkinson ◽  
Dino Moras ◽  
...  
Keyword(s):  
Solution Structure ◽  
Self Association

scholarly journals The E6 Oncoproteins of High-Risk Papillomaviruses Bind to a Novel Putative GAP Protein, E6TP1, and Target It for Degradation

1999 ◽  
Vol 19 (1) ◽  
pp. 733-744 ◽  
Author(s):  
Qingshen Gao ◽  
Seetha Srinivasan ◽  
Sarah N. Boyer ◽  
David E. Wazer ◽  
Vimla Band
Keyword(s):  
High Risk ◽  
P53 Protein ◽  
Single Gene ◽  
Human Papillomaviruses ◽  
Dominant Negative ◽  
Hpv16 E6 ◽  
Hpv E6 ◽  
E6 Oncoprotein ◽  
E6 Protein

ABSTRACT The high-risk human papillomaviruses (HPVs) are associated with carcinomas of the cervix and other genital tumors. Previous studies have identified two viral oncoproteins, E6 and E7, which are expressed in the majority of HPV-associated carcinomas. The ability of high-risk HPV E6 protein to immortalize human mammary epithelial cells (MECs) has provided a single-gene model to study the mechanisms of E6-induced oncogenic transformation. In this system, the E6 protein targets the p53 tumor suppressor protein for degradation, and mutational analyses have shown that E6-induced degradation of p53 protein is required for MEC immortalization. However, the inability of most dominant-negative p53 mutants to induce efficient immortalization of MECs suggests the existence of additional targets of the HPV E6 oncoprotein. Using the yeast two-hybrid system, we have isolated a novel E6-binding protein. This polypeptide, designated E6TP1 (E6-targeted protein 1), exhibits high homology to GTPase-activating proteins for Rap, including SPA-1, tuberin, and Rap1GAP. The mRNA for E6TP1 is widely expressed in tissues and in vitro-cultured cell lines. The gene for E6TP1 localizes to chromosome 14q23.2-14q24.3 within a locus that has been shown to undergo loss of heterozygosity in malignant meningiomas. Importantly, E6TP1 is targeted for degradation by the high-risk but not the low-risk HPV E6 proteins both in vitro and in vivo. Furthermore, the immortalization-competent but not the immortalization-incompetent HPV16 E6 mutants target the E6TP1 protein for degradation. Our results identify a novel target for the E6 oncoprotein and provide a potential link between HPV E6 oncogenesis and alteration of a small G protein signaling pathway.

HPV16 E6 oncoprotein increases cell adhesion in human keratinocytes

2008 ◽  
Vol 154 (1) ◽  
pp. 55-63 ◽  
Author(s):  
Alexander Epshtein ◽  
A. Jackman ◽  
P. Gonen ◽  
L. Sherman
Keyword(s):  
Cell Adhesion ◽  
Human Keratinocytes ◽  
Hpv16 E6 ◽  
E6 Oncoprotein

scholarly journals Inhibition of Serum- and Calcium-Induced Differentiation of Human Keratinocytes by HPV16 E6 Oncoprotein: Role of p53 Inactivation

Virology ◽  
1997 ◽  
Vol 237 (2) ◽  
pp. 296-306 ◽  
Author(s):  
Levana Sherman ◽  
Anna Jackman ◽  
Hagar Itzhaki ◽  
Melissa Conrad Stöppler ◽  
Debbie Koval ◽  
...  
Keyword(s):  
Human Keratinocytes ◽  
Induced Differentiation ◽  
Hpv16 E6 ◽  
E6 Oncoprotein ◽  
P53 Inactivation
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