Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Pierre André Briand"'
Publikováno v:
Molecular and Cellular Biology, Vol. 36 (2016) pp. 1310-1321
Hsp90 is the ATP-consuming core component of a very abundant molecular chaperone machine that handles a substantial portion of the cytosolic proteome. Rather than one machine, it is in fact an ensemble of molecular machines, since most mammalian cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::917e7d9c437c1c60ad675421a46e396d
https://archive-ouverte.unige.ch/unige:82275
https://archive-ouverte.unige.ch/unige:82275
Autor:
Didier Picard, Giovanna Fasanella, Vittoria Rago, Amalia Carpino, Marcello Maggiolini, Pierre-André Briand, Anna Grazia Recchia, Vincenzo Pezzi, Adele Vivacqua, Sebastiano Andò
Publikováno v:
Journal of Molecular Endocrinology, Vol. 32, No 3 (2004) pp. 777-91
The role of oestrogens in the development of prostate cancer is poorly understood. However, a large body of evidence has suggested that oestrogenic hormones may be involved in prostatic malignancy. The localization of oestrogen receptor beta (ERbeta)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::541c32983ac4e74dba187e3c80e87e37
https://doi.org/10.1677/jme.0.0320777
https://doi.org/10.1677/jme.0.0320777
Publikováno v:
The EMBO Journal. 15:2174-2183
The estrogen receptor (ER) can be activated as a transcription factor either by binding of cognate estrogenic ligand or, indirectly, by a variety of other extracellular signals. As a first step towards elucidating the mechanism of 'steroid-independen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2f3593b70f6e7fb5e11a3c255350a01
https://doi.org/10.1002/j.1460-2075.1996.tb00571.x
https://doi.org/10.1002/j.1460-2075.1996.tb00571.x
Publikováno v:
Genes and Development, Vol. 24, No 7 (2010) pp. 708-719
Genes & development
Genes & development
The estrogen receptor alpha (ERalpha) is activated as a transcription factor by both estrogen and a large variety of other extracellular signals. The mechanisms of this ligand-independent activation, notably by cAMP signaling, are still largely unkno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::580d29a740d2a57d801770dd464de1aa
https://pubmed.ncbi.nlm.nih.gov/20360387
https://pubmed.ncbi.nlm.nih.gov/20360387
Publikováno v:
Molecular and Biochemical Parasitology, Vol. 164, No 2 (2009) pp. 147-152
Developing novel drugs against the unicellular parasite Plasmodium is complicated by the paucity of simple screening systems. Heat-shock proteins are an essential class of proteins for the parasite's cyclical life style between different cellular mil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5ee290bbbe83e92aeda3238e7dda6f4
https://igi.indrastra.com/items/show/192992
https://igi.indrastra.com/items/show/192992
Publikováno v:
Experimental Cell Research, Vol. 312, No 19 (2006) pp. 3949-58
The abundant molecular chaperone Hsp90 functions in association with co-chaperones including p23 to promote the folding and maturation of a subset of cytosolic proteins. "Fluorescence recovery after photobleaching" (FRAP) experiments showed that the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8993f22067ec3c4e9d951b3c34d80f9a
https://archive-ouverte.unige.ch/unige:4585
https://archive-ouverte.unige.ch/unige:4585
Publikováno v:
Biological Chemistry, Vol. 383, No 9 (2002) pp. 1335-42
Cdc37 associates with the heat-shock protein 90 (Hsp90) molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. Cdc37 has been proposed to be a specificity factor for Hsp90, directing it nota
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a9654b9745cfa83e8125377df5363fc
https://pubmed.ncbi.nlm.nih.gov/12437126
https://pubmed.ncbi.nlm.nih.gov/12437126
Publikováno v:
Molecular and Cellular Biology, Vol. 21, No 22 (2001) pp. 7569-75
The highly abundant molecular chaperone Hsp90 functions with assistance from auxiliary factors, collectively referred to as Hsp90 cochaperones, and the Hsp70 system. Hsp104, a molecular chaperone required for stress tolerance and for maintenance of [
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc23ddfa309ec1dbe72fb08ebdf8ee08
https://pubmed.ncbi.nlm.nih.gov/11604493
https://pubmed.ncbi.nlm.nih.gov/11604493
Publikováno v:
Biological Chemistry. 378
We have identified and characterized a homolog of the 40 kDa cyclophilins in the budding yeast Saccharomyces cerevisiae. At the amino acid level, this novel yeast cyclophilin, termed Cyp40, is 47% identical to human cyclophilin-40. Recombinant Cyp40
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2e54574572e3f6d3c2eaf62550c20c2
https://doi.org/10.1515/bchm.1997.378.5.381
https://doi.org/10.1515/bchm.1997.378.5.381