P
Pierre Chambon
Researcher at French Institute of Health and Medical Research
Publications - 893
Citations - 166555
Pierre Chambon is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Retinoic acid & Retinoic acid receptor. The author has an hindex of 211, co-authored 884 publications receiving 161565 citations. Previous affiliations of Pierre Chambon include United States University & Collège de France.
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Journal ArticleDOI
The nuclear receptor superfamily: the second decade.
David J. Mangelsdorf,Carl S. Thummel,Miguel Beato,Peter Herrlich,Günther Schütz,Kazuhiko Umesono,Bruce Blumberg,Philippe Kastner,Manuel Mark,Pierre Chambon,Ronald M. Evans +10 more
TL;DR: This research presents a new probabilistic procedure called ‘spot-spot analysis’ to characterize the response of the immune system to the presence of E.coli.
Journal ArticleDOI
A decade of molecular biology of retinoic acid receptors.
TL;DR: A review of recent developments in structure‐ function relationships of retinoic acid receptors focuses on recent developments, particularly in the area of structure‐function relationships.
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Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A
Stephen Green,P Walter,Vijay Kumar,Andrée Krust,Jean-Marc Bornert,Patrick Argos,Pierre Chambon +6 more
TL;DR: Cloned and sequenced the complete complementary DNA of the oestrogen receptor (ER) present in the breast cancer cell line MCF-7 and found extensive homology between the ER and the erb-A protein of the oncogenic avian erythroblastosis virus.
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A human retinoic acid receptor which belongs to the family of nuclear receptors
TL;DR: The protein is homologous to the receptors for steroid hormones, thyroid hormones and vitamin D3, and appears to be a retinoic acid-inducible {Tans-acting enhancer factor, suggesting that the molecular mechanisms of the effect of vitamin A (vitamin A) on embryonic development, differentiation and tumour cell growth are similar to those described for other members of this nuclear receptor family.
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Activation of the Estrogen Receptor Through Phosphorylation by Mitogen-Activated Protein Kinase
Shigeaki Kato,Hideki Endoh,Yoshikazu Masuhiro,Takuya Kitamoto,Shimami Uchiyama,Haruna Sasaki,Shoichi Masushige,Yukiko Gotoh,Eisuke Nishida,Hiroyuki Kawashima,Daniel Metzger,Pierre Chambon +11 more
TL;DR: The phosphorylation of the human estrogen receptor (ER) serine residue at position 118 is required for full activity of the ER activation function 1 (AF-1), which is modulated by the phosphorylated Ser118 through the Ras-MAPK cascade of the growth factor signaling pathways.