Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Jean-Louis Borgna"'
Publikováno v:
The Journal of Steroid Biochemistry and Molecular Biology. 98:236-247
A purified preparation of human estrogen receptor alpha (hERalpha) ligand-binding domain (LBD) involving mainly the Ser(309)Ala(569) (approximately 30%) and Ser(309)Ala(571) (approximately 63%) ER portions was used to identify the covalent attachment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07c839f9f52984d95dcaf326d791f390
https://doi.org/10.1016/j.jsbmb.2005.10.006
https://doi.org/10.1016/j.jsbmb.2005.10.006
Publikováno v:
The Journal of Steroid Biochemistry and Molecular Biology. 98:111-121
Affinity labeling of human estrogen receptor alpha (ERalpha) by high affinity and antiestrogenic estradiol (E(2)) 11 beta-derivatives, 11 beta-bromoacetamidoethoxyphenylE(2) (11BAEOPE(2)) and 11 beta-bromoacetamidopentoxyphenylE(2) (11BAPOPE(2)) was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f6d8cea81e883f8614fb9d5c4d6f50a
https://doi.org/10.1016/j.jsbmb.2005.09.006
https://doi.org/10.1016/j.jsbmb.2005.09.006
Publikováno v:
Biochemistry. 41:7979-7988
We investigated the role of H524 of the human estrogen receptor alpha (ERalpha) for the binding of various estrogens [estradiol (E(2)), 3-deoxyestradiol (3-dE(2)), and 17beta-deoxyestradiol (17beta-dE(2))] and antiestrogens [4-hydroxytamoxifen (OHT),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eca39a4b1e5172ad1b947c3538d798ce
https://doi.org/10.1021/bi0121914
https://doi.org/10.1021/bi0121914
Autor:
Jean-Louis Borgna, Teutsch G, G. Delettre, Nique F, Hélène Mattras, el Garrouj D, Sigrid Aliau
Publikováno v:
Journal of Medicinal Chemistry. 43:613-628
Ten electrophilic estradiol 11beta-aryl derivatives were synthesized, with three different types of 11beta-substituent: (i) pOO(CH(2))(2)X (compounds: 6, X = OSO(2)CH(3); 7, X = I; 13, X = NHCOCH(2)Cl; 15, X = N(CH(3))COCH(2)Br; and 16, X = N(CH(3))C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d24d98d8657fb80e9215c6c3182e268
https://doi.org/10.1021/jm990179s
https://doi.org/10.1021/jm990179s
Publikováno v:
Biochemistry. 38:14752-14762
The efficiency of 11beta-[p(aziridinylethoxy)phenyl]estradiol 1 and 11beta-[p(aziridinylpentoxy)phenyl]estradiol 2 affinity labeling of the estrogen receptor alpha (ERalpha) was evaluated on the basis of their capacity to inhibit [(3)H]estradiol bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1b6ec24c8d55e54d6a92f83e9a529a9
https://doi.org/10.1021/bi991176k
https://doi.org/10.1021/bi991176k
Publikováno v:
European Journal of Biochemistry. 231:204-213
Interactions between the lamb uterine estrogen receptor occupied by estradiol, 4-hydroxytamoxifen (a non-steroidal partial estrogen antagonist) or ICI 164,384 (a steroidal pure estrogen antagonist), and the vitellogenin A2 estrogen-response element (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::021b395be61b0e9a4c24697edad835fc
https://doi.org/10.1111/j.1432-1033.1995.0204f.x
https://doi.org/10.1111/j.1432-1033.1995.0204f.x
Autor:
Jean-Louis Borgna, Jacqueline Scali
Publikováno v:
European Journal of Biochemistry. 199:575-585
The action of diethylpyrocarbonate on lamb uterine estrogen receptor produced an homogeneous population of the receptor (∼ 55%) which still bound triarylethylene antiestrogens such as 4-hydroxytamoxifen with a high affinity but bound classical pote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c99cf08e1b6bfee6f97f17e06c42da3
https://doi.org/10.1111/j.1432-1033.1991.tb16157.x
https://doi.org/10.1111/j.1432-1033.1991.tb16157.x
Autor:
Jean-Louis Borgna
Publikováno v:
The Journal of steroid biochemistry and molecular biology. 96(2)
The nonspecific binding (equilibrium coefficient kn) of ligand (L) and/or the incomplete recovery (alpha1) of the receptor-ligand (RL) complex in binding measurements, could hamper accurate determination of the association and dissociation rate const
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bd9beaea867cec7d2eb55560195a715
https://pubmed.ncbi.nlm.nih.gov/15925507
https://pubmed.ncbi.nlm.nih.gov/15925507
Autor:
Jean-Louis Borgna
Publikováno v:
The Journal of steroid biochemistry and molecular biology. 92(5)
Accurate calculation of the equilibrium association constant (K) and binding site concentration (N) related to a receptor (R)/ligand (L) interaction, via R saturation analysis, requires exact determination of the specifically bound L concentration (B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b5795f8a5ba67d398c519eb1082400b
https://pubmed.ncbi.nlm.nih.gov/15698547
https://pubmed.ncbi.nlm.nih.gov/15698547
Autor:
Jean-Louis Borgna, Jean-Claude Bonnafous, Patrick Jouin, Eric Richard, Hélène Mattras, Sigrid Aliau
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2002, 41 (52), pp.15713-27
Biochemistry, 2002, 41 (52), pp.15713-27
Biochemistry, American Chemical Society, 2002, 41 (52), pp.15713-27
Biochemistry, 2002, 41 (52), pp.15713-27
International audience; Mass spectrometry was used to identify the sites of covalent attachment of [(14)C]-17alpha-bromoacetamidopropylestradiol ([(14)C]17BAPE(2), an estradiol agonist) to the ligand-binding domain (LBD) of mouse estrogen receptor al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9f70e28c598fdcab9a80d21f954f64c
https://www.hal.inserm.fr/inserm-00192906
https://www.hal.inserm.fr/inserm-00192906
