Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Chantal Diaz-Latoud"'
Knock down of heat shock protein 27 (HspB1) induces degradation of several putative client proteins.
Autor:
Benjamin Gibert, Bénédicte Eckel, Lydie Fasquelle, Maryline Moulin, Frantz Bouhallier, Vincent Gonin, Gregory Mellier, Stéphanie Simon, Carole Kretz-Remy, André-Patrick Arrigo, Chantal Diaz-Latoud
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29719 (2012)
Hsp27 belongs to the heat shock protein family and displays chaperone properties in stress conditions by holding unfolded polypeptides, hence avoiding their inclination to aggregate. Hsp27 is often referenced as an anti-cancer therapeutic target, but
Externí odkaz:
https://doaj.org/article/c51afa4923024b758fc69a3d4b5dfe06
Autor:
Frédéric Lemaire, Céline A Mandon, Julien Reboud, Alexandre Papine, Jesus Angulo, Hervé Pointu, Chantal Diaz-Latoud, Christian Lajaunie, François Chatelain, André-Patrick Arrigo, Béatrice Schaack
Publikováno v:
PLoS ONE, Vol 2, Iss 1, p e163 (2007)
BACKGROUND: Improved chemical hazard management such as REACH policy objective as well as drug ADMETOX prediction, while limiting the extent of animal testing, requires the development of increasingly high throughput as well as highly pertinent in vi
Externí odkaz:
https://doaj.org/article/972667f4ca95402ea57e3a917cd3dc4c
Autor:
Lise Clement-Demange, Pape Francois Le, Chantal Diaz-Latoud, Benedicte Eckel, Philippe Clézardin, Sandra Geraci
Publikováno v:
Bone Abstracts.
Targeting heat shock protein 27 (HspB1) interferes with bone metastasis and tumour formation in vivo
Autor:
Benjamin Gibert, Joanna Fombonne, Chantal Diaz-Latoud, Benedicte Eckel, Blandine Deux, David Goldschneider, Philippe Clézardin, A-P Arrigo, Patrick Mehlen, V Gonin
Publikováno v:
British Journal of Cancer
Background: The small stress heat shock protein 27 (Hsp27) has recently turned as a promising target for cancer treatment. Hsp27 upregulation is associated with tumour growth and resistance to chemo- and radio-therapeutic treatments, and several ongo
Autor:
Chantal Diaz-Latoud, Elie Hadchity, André-Patrick Arrigo, Marie-Thérèse Aloy, Benjamin Gibert, Czekalla A, Claire Rodriguez-Lafrasse, Colas P
Publikováno v:
Oncogene. 30:3672-3681
Human heat shock protein 27 (Hsp27, HspB1) is an anti-apoptotic protein characterized for its tumorigenic and metastatic properties, and now referenced as a major therapeutic target in many types of cancer. Hsp27 biochemical properties rely on a stru
Autor:
Elie Hadchity, Marie-Thérèse Aloy, André-Patrick Arrigo, Line Claude, Robert Rousson, Chantal Diaz-Latoud, Claire Rodriguez-Lafrasse, Clara Bionda
Publikováno v:
International Journal of Radiation Oncology*Biology*Physics. 70:543-553
Purpose The ability of heat shock protein 27 (Hsp27) to protect cells from stressful stimuli and its increased levels in tumors resistant to anticancer therapeutics suggest that it may represent a target for sensitization to radiotherapy. In this stu
Publikováno v:
FEBS Journal. 273:3076-3093
We recently reported that the transient expression of polyglutamine tracts of various size in exon 1 of the huntingtin polypeptide (httEx1) generated abnormally high levels of intracellular reactive oxygen species that directly contributed to cell de
Publikováno v:
Antioxidants & Redox Signaling. 7:436-445
Murine small stress protein [heat shock protein 25 (Hsp25)] expression confers thermotolerance and protection against oxidative stress. Hsp25 is an oligomeric ATP-independent phospho-chaperone that can generate a glutathione-dependent pro-reducing st
Autor:
Sophie Virot, Carole Kretz-Remy, André-Patrick Arrigo, Chantal Diaz-Latoud, Sylvain Chaufour, Wance Firdaus
Publikováno v:
Antioxidants & Redox Signaling. 7:414-422
Small stress proteins [small heat shock proteins (sHsps)] are molecular chaperones that modulate the ability of cells to respond to oxidative stress. The current knowledge concerning the protective mechanism generated by the expression of mammalian h