Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Debdyuti Mukhopadhyay"'
Autor:
Olivier Deloche, Alexandre Soulard, Claudio De Virgilio, James R. Broach, Robbie Loewith, Dorothea Anrather, Howard Riezman, Alexandre Huber, Gustav Ammerer, Michael N. Hall, Soyeon I. Lippman, Valeria Wanke, Jörg Urban, Debdyuti Mukhopadhyay
Publikováno v:
Molecular Cell, Vol. 26, No 5 (2007) pp. 663-74
The Target of Rapamycin (TOR) protein is a Ser/Thr kinase that functions in two distinct multiprotein complexes: TORC1 and TORC2. These conserved complexes regulate many different aspects of cell growth in response to intracellular and extracellular
Autor:
Fatima-Zahra Idrissi, Jens Pfannstiel, Howard Riezman, Helga Grötsch, M. Isabel Geli, Isabel Fernandez, Bianka L. Grosshans, Debdyuti Mukhopadhyay, Johannes Lechner
Publikováno v:
Journal of Biological Chemistry, Vol. 281, No 16 (2006) pp. 11104-11114
The yeast myosins I Myo3p and Myo5p have well established functions in the polarization of the actin cytoskeleton and in the endocytic uptake of the G protein-coupled receptor Ste2p. A number of results suggest that phosphorylation of the conserved T
Publikováno v:
Journal of Biological Chemistry, Vol. 283, No 29 (2008) pp. 20159-20169
Sphinganine-1-phosphate lyase (Dpl1p) is a highly conserved enzyme of sphingolipid metabolism that catalyzes the irreversible degradation of sphingoid base phosphates, which are potent signaling molecules. Sphingoid base phosphates play a vital role
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd4e6020634925e75ba4832988cae628
https://archive-ouverte.unige.ch/unige:145522
https://archive-ouverte.unige.ch/unige:145522
Autor:
Debdyuti Mukhopadhyay, Howard Riezman
Publikováno v:
Science, Vol. 315, No 5809 (2007) pp. 201-205
Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76–amino acid polypeptide, ubiquitin, is primarily attached to the ϵ-amino group of lysines in target proteins. Ubiquitination is a major player in regu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74dca4e41dafe709e842f24e59134ccc
https://archive-ouverte.unige.ch/unige:13118
https://archive-ouverte.unige.ch/unige:13118