Proteomics & Mammalian Cell Biology Section
The Proteomics & Mammalian Cell Biology Section functions as a core facility for cancer proteomics at The Norwegian Radium Hospital. Furnished with a MALDI-TOF mass spectrometer and equipment for two-dimensional gel electrophoresis, the section explores the possibility of using large-scale proteomic analysis as a cancer diagnostic tool, and provides proteomic service (e.g., protein identification by tryptic peptide mass fingerprinting) for cancer researchers and other scientists at the University of Oslo.
In the section's own research projects, proteomics is used to study autophagic protein degradation in normal and malignant liver cells, and the role of phosphorylation-based signalling pathways (in particular the stress-activated AMPK pathway) in the regulation of autophagy, apoptosis (programmed cell death), and cytoskeletal organization.
In the section's own research projects, proteomics is used to study autophagic protein degradation in normal and malignant liver cells, and the role of phosphorylation-based signalling pathways (in particular the stress-activated AMPK pathway) in the regulation of autophagy, apoptosis (programmed cell death), and cytoskeletal organization.
Contact information:
Department of Cell Biology, Institute for Cancer Research,
The Norwegian Radium Hospital, Montebello, N-0310 Oslo, Norway
Email Per.O.Seglen@rr-reserach.no, Phone:+47 22 78 19 80, Fax: +47 22 78 19 95
Department of Cell Biology, Institute for Cancer Research,
The Norwegian Radium Hospital, Montebello, N-0310 Oslo, Norway
Email Per.O.Seglen@rr-reserach.no, Phone:+47 22 78 19 80, Fax: +47 22 78 19 95
News & events
Paper from Anne-Lise Børresen-Dale and co-workers published in "Science Translational Medicine"
Jun 30, 2010
More news
Jun 30, 2010
Latest articles
Per O. Seglen
Purification of autophagosomes from rat hepatocytes
Autophagy, 6 (4) (in press)
PubMed 20505360
Sequestration assays for mammalian autophagy
Methods Enzymol, 452, 63-83
PubMed 19200876
Phosphorylated and non-phosphorylated forms of catechol O-methyltransferase in rat liver, brain and other tissues
Biochem J, 417 (2), 535-45
PubMed 18831714





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