Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Tutik Ristriani"'
Autor:
Leiping Fu, Koenraad Van Doorslaer, Zigui Chen, Tutik Ristriani, Murielle Masson, Gilles Travé, Robert D Burk
Publikováno v:
PLoS ONE, Vol 5, Iss 9 (2010)
Human Papillomavirus (HPV) E6 induced p53 degradation is thought to be an essential activity by which high-risk human Alphapapillomaviruses (alpha-HPVs) contribute to cervical cancer development. However, most of our understanding is derived from the
Externí odkaz:
https://doaj.org/article/6d726a925a014bf398eae7043624d5d9
Autor:
Laurent Brino, Abdellahi Ould M'hamed Ould Sidi, Tutik Ristriani, Murielle Masson, Scott B. Vande Pol, Xavier Bernard, Christine Ruhlmann, Mireille Baltzinger, Patrick Schultz, Katia Zanier, Gilles Travé, Frederic Melin, Benoit Fischer, Petra Hellwig, Vladimir Rybin
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2010, 396 (1), pp.90-104. ⟨10.1016/j.jmb.2009.11.022⟩
Journal of Molecular Biology, Elsevier, 2010, 396 (1), pp.90-104. ⟨10.1016/j.jmb.2009.11.022⟩
Papillomavirus E6 oncoproteins bind and often provoke the degradation of many cellular proteins important for the control of cell proliferation and/or cell death. Structural studies on E6 proteins have long been hindered by the difficulties of obtain
Autor:
Etienne Weiss, Bruno Kieffer, Alain Van Dorsselaer, Sebastian Charbonnier, Gunter Stier, Yves Nominé, Gilles Travé, Tutik Ristriani, Nukhet Cavusoglu, Murielle Masson
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2003, 42 (17), pp.4909-4917. ⟨10.1021/bi026980c⟩
Biochemistry, American Chemical Society, 2003, 42 (17), pp.4909-4917. ⟨10.1021/bi026980c⟩
E6 is a viral oncoprotein implicated in cervical cancers, produced by high-risk human papillomaviruses (HPVs). Structural data concerning this protein are scarce due to the difficulty of producing recombinant E6. Recently, we described the expression
Autor:
Elsa Bensimon, Gilles Salles, Vincent Galy, Béatrice Horard, Frédérique Magdinier, Tutik Ristriani, Claire Falandry, Geneviève Fourel, Eric Gilson
Publikováno v:
The Journal of biological chemistry. 285(26)
Proteins bearing a SET domain have been shown to methylate lysine residues in histones and contribute to chromatin architecture. Methylation of histone H3 at lysine 9 (H3K9) has emerged as an important player in the formation of heterochromatin, chro
Autor:
Georges Orfanoudakis, Tutik Ristriani, Yves Nominé, Katia Zanier, Dominique Desplancq, Sebastian Charbonnier, Etienne Weiss, Annie-Paule Sibler, Bruno Kieffer, Gilles Travé, Robert Andrew Atkinson, Murielle Masson, François Deryckere
Publikováno v:
Molecular Cell
Molecular Cell, Elsevier, 2006, 21 (5), pp.665-78. ⟨10.1016/j.molcel.2006.01.024⟩
Molecular Cell, Elsevier, 2006, 21, pp.665-78
Molecular Cell, Elsevier, 2006, 21 (5), pp.665-678. ⟨10.1016/j.molcel.2006.01.024⟩
Molecular Cell, Elsevier, 2006, 21 (5), pp.665-78. ⟨10.1016/j.molcel.2006.01.024⟩
Molecular Cell, Elsevier, 2006, 21, pp.665-78
Molecular Cell, Elsevier, 2006, 21 (5), pp.665-678. ⟨10.1016/j.molcel.2006.01.024⟩
1097-2765 (Print) Journal Article; Oncoprotein E6 is essential for oncogenesis induced by human papillomaviruses (HPVs). The solution structure of HPV16-E6 C-terminal domain reveals a zinc binding fold. A model of full-length E6 is proposed and analy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee953b28a04d2289e847c8acdf7bccfe
https://hal.archives-ouvertes.fr/hal-00151143
https://hal.archives-ouvertes.fr/hal-00151143
Publikováno v:
Protein Expression and Purification
Protein Expression and Purification, Elsevier, 2002, 26 (3), pp.357-367. ⟨10.1016/s1046-5928(02)00570-3⟩
Protein Expression and Purification, Elsevier, 2002, 26 (3), pp.357-367. ⟨10.1016/s1046-5928(02)00570-3⟩
Interpretation of protein mutagenesis experiments requires the ability to distinguish functionally relevant mutations from mutations affecting the structure. When a protein is expressed soluble in bacteria, properly folded mutants are expected to rem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dc85d88256daf06443fe48a7db699d3
https://hal.archives-ouvertes.fr/hal-03406435
https://hal.archives-ouvertes.fr/hal-03406435
Autor:
Tutik Ristriani, Yves Nominé, Gilles Travé, Etienne Weiss, Jean-François Lefèvre, Cécile Laurent
Publikováno v:
Protein Expression and Purification
Protein Expression and Purification, Elsevier, 2001, 23 (1), pp.22-32. ⟨10.1006/prep.2001.1451⟩
Protein Expression and Purification, Elsevier, 2001, 23 (1), pp.22-32. ⟨10.1006/prep.2001.1451⟩
Many polypeptides overexpressed in bacteria are produced misfolded and accumulate as solid structures called inclusion bodies. Inclusion-body-prone proteins have often been reported to escape precipitation when fused to maltose-binding protein (MBP).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fea59fe10ff73ce2debfb04ab1a2bf8
https://hal.archives-ouvertes.fr/hal-03406438
https://hal.archives-ouvertes.fr/hal-03406438
Autor:
Etienne Weiss, Tutik Ristriani, Yves Nominé, Jean-François Lefèvre, Gilles Travé, Cécile Laurent
Publikováno v:
Protein Engineering, Design and Selection
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2001, 14 (4), pp.297-305. ⟨10.1093/protein/14.4.297⟩
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2001, 14 (4), pp.297-305. ⟨10.1093/protein/14.4.297⟩
Recombinant production of HPV oncoprotein E6 is notoriously difficult. The unfused sequence is produced in inclusion bodies. By contrast, fusions of E6 to the C-terminus of carrier proteins such as maltose-binding protein or glutathione-S-transferase
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2001, 305 (4), pp.729-739. ⟨10.1006/jmbi.2000.4330⟩
Journal of Molecular Biology, Elsevier, 2001, 305 (4), pp.729-739. ⟨10.1006/jmbi.2000.4330⟩
E6 is an oncoprotein implicated in cervical cancers produced by “ high risk “ human papillomaviruses. E6 binds specifically to several cellular proteins, including the tumour suppressor p53 and the ubiquitin ligase E6-AP. However, E6 is also a DN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d83317bed22eae2c9aaf729aca7092b
https://hal.archives-ouvertes.fr/hal-03406441
https://hal.archives-ouvertes.fr/hal-03406441
Autor:
Etienne Weiss, Tutik Ristriani, Jean-François Lefèvre, Yves Nominé, Murielle Masson, Gilles Travé, Cécile Laurent
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2000, 296 (5), pp.1189-1203. ⟨10.1006/jmbi.2000.3527⟩
Journal of Molecular Biology, Elsevier, 2000, 296 (5), pp.1189-1203. ⟨10.1006/jmbi.2000.3527⟩
E6 is an oncoprotein implicated in cervical cancers, produced by “high-risk” human papillomaviruses. E6 is thought to promote tumorigenesis by stimulating cellular degradation of the tumour suppressor p53, but it might display other activities. S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd5a89df3f59a6ca24fd4dcaf20efa73
https://hal.archives-ouvertes.fr/hal-03406442
https://hal.archives-ouvertes.fr/hal-03406442