Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Christine Radanyi"'
Autor:
Christine Radanyi, Jean-Daniel Brion, Véronique Marsaud, Gaëlle Le Bras, Mouâd Alami, Jack-Michel Renoir, Jean-François Peyrat, Samir Messaoudi, Céline Bouclier
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 18:2495-2498
A new series of coumarin inhibitors of hsp90 lacking the noviose moiety as well as substituents on C-7 and C-8 positions of the aromatic ring was synthesised and their hsp90 inhibitory activity has been delineated: for example, their capacity to indu
Autor:
Véronique Marsaud, Dominique Elias, Jack-Michel Renoir, Christine Radanyi, Roman Rouzier, M. Kornprobst, David Atallah
Publikováno v:
International Journal of Hyperthermia. 20:405-419
Hyperthermia is used to treat intraperitoneal colorectal carcinomatosis. In this setting, the molecular effects of oxaliplatin and hyperthermia, in combination and alone, were deciphered in ovarian and colon cancer cells. The combined antiproliferati
Autor:
Jack-Michel Renoir, Christine Radanyi, Félix Sauvage, Mouad Alami, Stéphanie Denis, Davide Audisio, Délphine Methy-Gonnot, Jean-Daniel Brion, Juliette Vergnaud-Gauduchon, Samir Messaoudi
Publikováno v:
European journal of medicinal chemistry. 83
A series of substituted coumarins 1–10 was designed and synthesized as a novel class of 4TCNA analogues. Compound 2a showed excellent antiproliferative activity with mean GI50 values at a micromolar level in a diverse set of human cancer cells (GI5
Autor:
Béatrice Chambraud, Etienne-Emile Baulieu, Christine Radanyi, Kamran Shazand, Jacques Camonis, Krzysztof Rajkowski
Publikováno v:
Journal of Biological Chemistry. 271:32923-32929
We have identified a human gene encoding a 48-kDa protein that specifically interacts with the peptidyl prolyl isomerase FK506-binding protein 59 (FKBP59) and also with the well known FKBP12. FKBP59 and FKBP12 belong to the large family of immunophil
Autor:
Etienne-Emile Baulieu, Stéphane Le Bihan, Christine Radanyi, Alex Gold, Jack-Michel Renoir, Christine Mercier-Bodard, Merhdad Arjomandi
Publikováno v:
The Journal of Steroid Biochemistry and Molecular Biology. 48:101-110
The non-DNA binding form of the rabbit uterus cytosol progesterone receptor (PR) contains, in addition to the hormone binding unit and heat shock protein Mr 90kDa (hsp90), a H eat shock protein B inding I mmunophilin (p59/HBI) which interacts with hs
Autor:
Jean-Daniel Brion, Samir Messaoudi, Délphine Methy-Gonnot, Davide Audisio, Lukasz Cegielkowski, Jack-Michel Renoir, Christine Radanyi, Jean-François Peyrat, Mouâd Alami
Publikováno v:
ChemMedChem. 6(5)
Heat shock protein 90 (Hsp90) is a significant target in the development of rational cancer therapy, due to its role at the crossroads of multiple signaling pathways associated with cell proliferation and viability. Here, a novel series of Hsp90 inhi
Publikováno v:
The Journal of Steroid Biochemistry and Molecular Biology. 42:863-874
The M(r) 90,000 protein associated with steroid receptors in their non-transformed state has been identified as a heat shock protein (hsp90) but the relationship between hsp90 binding and receptor function is still poorly understood. In this work, we
Autor:
L.E. Faber, Marie-Claire Lebeau, Etienne-Emile Baulieu, J Herrick, Jack-Michel Renoir, Nelly Massol, Christine Radanyi
Publikováno v:
Journal of Biological Chemistry. 267:4281-4284
The primary sequence of the rabbit liver cDNA coding for protein p59 has been determined. The protein binds to the 90-kDa heat shock protein (hsp 90) and is associated with it, including when hsp 90 participates in hetero-oligomeric complexes of untr
Publikováno v:
Journal of Biological Chemistry. 265:10740-10745
Untransformed cytosol receptors for progesterone (PR), androgen (AR), estrogen (ER), and glucocorticosteroid (GR) in rabbit tissues contain a 59-kDa protein (p59) (Tai, P.K.K., Maeda, Y., Nakao, K., Wakim, N.G., Duhring, J.L., and Faber, L.E. (1986)
Autor:
Jack Michel Renoir, Patrick J. Murphy, Mingjie Zhang, Jennifier M. Harrell, Christine Radanyi, Mario D. Galigniana, Michael Chinkers, William B. Pratt
Publikováno v:
Biochemistry. 41(46)
FKBP52 is a steroid receptor-associated immunophilin that binds via a tetratricopeptide repeat (TPR) domain to hsp90. FKBP52 has also been shown to interact either directly or indirectly via its peptidylprolyl isomerase (PPIase) domain with cytoplasm