Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Molecular Chaperones/chemistry/genetics/metabolism"'
Publikováno v:
Genetics, Vol. 181, No 2 (2009) pp. 447-60
In this work we addressed the role of ubiquitination in the function of the nascent polypeptide-associated complex (NAC), named EGD in the yeast Saccharomyces cerevisiae. To this end, we first identified the lysines residues required for ubiquitinati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18320773795217e0c0d706cd6ca0d3ab
https://archive-ouverte.unige.ch/unige:5319
https://archive-ouverte.unige.ch/unige:5319
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
The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
Publikováno v:
FEBS Letters, Vol. 467, No 1 (2000) pp. 111-6
The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast. A cdc37 mutant strain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4410d8a9bf00987eba7d2bdd25d6af15
https://archive-ouverte.unige.ch/unige:4652
https://archive-ouverte.unige.ch/unige:4652