Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Vanessa Brevet"'
Publikováno v:
Current Medicinal Chemistry
Current Medicinal Chemistry, Bentham Science Publishers, 2005, 4, pp.409-20
Current Medicinal Chemistry, Bentham Science Publishers, 2005, 4, pp.409-20
Much progress has been made in recent years in developing small molecules that target the minor groove of DNA. Striking advances have led to the design of synthetic molecules that recognize specific DNA sequences with affinities comparable to those o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f55d72706d7b0e72ed1928eca2d46d78
https://pubmed.ncbi.nlm.nih.gov/16101491
https://pubmed.ncbi.nlm.nih.gov/16101491
Autor:
Vera Schramke, Livia Civitelli, Pierluigi Donini, Fiorentina Ascenzioni, Anne-Sophie Berthiau, Vanessa Brevet, Eric Gilson, Vincent Géli
The number of telomeric DNA repeats at chromosome ends is maintained around a mean value by a dynamic balance between elongation and shortening. In particular, proteins binding along the duplex part of telomeric DNA set the number of repeats by progr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b6836fbb8841b0eaf9d1d49f1056541
https://europepmc.org/articles/PMC152899/
https://europepmc.org/articles/PMC152899/
Autor:
Sophie G. Martin, Florence Gaden, Susan M. Gasser, Vanessa Brevet, Karine Dubrana, Eric Gilson, Geneviève Fourel, Laurent Maillet
Publikováno v:
EMBO reports. 2(3)
In Saccharomyces cerevisiae, efficient silencer function requires telomere proximity, i.e. compartments of the nucleoplasm enriched in silencing factors. Accordingly, silencers located far from telomeres function inefficiently. We show here that cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0cf06b8afbf134dee64beceda64ebc2
https://pubmed.ncbi.nlm.nih.gov/11266361
https://pubmed.ncbi.nlm.nih.gov/11266361
Autor:
Yves Corda, Eric Gilson, Maria Pia Longhese, Vera Schramke, Vincent Géli, Giovanna Lucchini, Vanessa Brevet, Holger Neecke
SET domain proteins are present in chromosomal proteins involved in epigenetic control of transcription. The yeast SET domain protein Set1p regulates chromatin structure, DNA repair, and telomeric functions. We investigated the mechanism by which the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::606bf8c9a9e0f92d8c3ee8b5073c438f
http://hdl.handle.net/10281/1828
http://hdl.handle.net/10281/1828
Publikováno v:
Current Biology-CB
Current Biology-CB, Elsevier, 2000, 10, pp.487-490
Current Biology-CB, 2000, 10, pp.487-490
Current Biology-CB, Elsevier, 2000, 10, pp.487-490
Current Biology-CB, 2000, 10, pp.487-490
Telomere elongation by telomerase balances the progressive shortening of chromosome ends due to the succession of replication cycles [1,2]. Telomerase activity is regulated in vivo at its site of action by the telomere itself. In yeast and human cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3be9822c2add47b005d499df188f8c5
https://hal.archives-ouvertes.fr/hal-00023798
https://hal.archives-ouvertes.fr/hal-00023798
Autor:
Vanessa Brevet, Vera Schramke, Maria Pia Longhese, Yves Corda, Eric Gilson, Vera Paciotti, Tamara Smokvina, Vincent Géli
Publikováno v:
Nature genetics. 21(2)
The yeast protein Set1p, inactivation of which alleviates telomeric position effect (TPE), contains a conserved SET domain present in chromosomal proteins involved in epigenetic control of transcription1,2. Mec3p is required for efficient DNA–damag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f2b1212bb7f9467ff7e95b1d7331faa
https://pubmed.ncbi.nlm.nih.gov/9988261
https://pubmed.ncbi.nlm.nih.gov/9988261
Publikováno v:
Biology of the Cell. 91:556-556
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::39438a943b4c1af14747c3288cc00628
https://doi.org/10.1016/s0248-4900(99)90266-6
https://doi.org/10.1016/s0248-4900(99)90266-6