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Partner 15: Mario Negri Institute for Pharmacological Research – Milano – Italy
Scientist responsible: Dr. Mario Salmona
Istituto di Ricerche Farmacologiche "Mario Negri" (Mario Negri Institute for Pharmacological Research) is a non-profit private organization for biomedical research. Legally incorporated in 1961, the Institute started research activities in Milan on February 1st, 1963. Today, it manages research centres in Bergamo, Ranica/Bergamo, and S. Maria Imbaro/Chieti.
The Institute's chief activity is to safeguard human health and life. To accomplish this mission, it conducts in-depth studies on the intimate processes of living organisms, on why diseases arise, and on the processes taking place inside the body after the administration of foreign substances. Research conducted at the Institute is devoted to this purpose, from the molecular level to humans. The findings are then exploited to suggest new drugs and to make those already existing more effective.
The main fields of interest are:
- the fight against cancer;
- nervous and mental disorders;
- cardiovascular diseases;
- kidney diseases and organ transplants;
- rare diseases;
- toxic effects of environmental pollutants;
- research on pain relief and drug addiction.
The Institute also organizes training schemes for laboratory technicians and graduate researchers. In conjunction with the Open University (Milton Keynes, UK), it grants PhDs.
Through various initiatives, the Institute also strives to foster the dissemination of scientific culture in biomedicine, both in general terms and in supporting healthcare practice in particular, in order to use drugs more rationally.
The Institute currently employs about 900 people working at the various research units. Ever since inception, it has provided training to 2,321 students, 627 "short" specializations, 913 three-year specializations, and 24 PhDs. Beneficiaries of scholarships and of specializations granted by the institute amount to 6,300, while 668 foreign researchers from 70 countries have spent periods at the Institute for educational purposes.
Scientific publications appearing in periodicals throughout the world are over 10,000.
Current group members involved in NAD:
Dr. M. Salmona
Dr. G. Forloni
Dr. M. Gobbi
Publications:
Di Fede G, Catania M, Morbin M, Rossi G, Suardi S, Mazzoleni G, Merlin M, Giovagnoli AR, Prioni S, Erbetta A, Falcone C, Gobbi M, Colombo L, Bastone A, Beeg M, Manzoni C, Francescucci B, Spagnoli A, Cantù L, Del Favero E, Levy E, Salmona M, Tagliavini F.
A recessive mutation in the APP gene with dominant-negative effect on amyloidogenesis.
Science 2009, 323: 1473-7
Repici M, Mare L, Colombo A, Ploia C, Sclip A, Bonny C, Nicod P, Salmona M, Borsello T.
c-Jun N-terminal kinase binding domain-dependent phosphorylation of mitogen-activated protein kinase kinase 4 and mitogen-activated protein kinase kinase 7 and balancing cross-talk between c-Jun N-terminal kinase and extracellular signal-regulated kinase pathways in cortical neurons.
Neuroscience 2009, 159: 94-103
Colombo A, Bastone A, Ploia C, Sclip A, Salmona M, Forloni G, Borsello T.
JNK regulates APP cleavage and degradation in a model of Alzheimer's disease.
Neurobiol Dis. 2009, 33: 518-25
Pera M, Martínez-Otero A, Colombo L, Salmona M, Ruiz-Molina D, Badia A, Clos MV.
Acetylcholinesterase as an amyloid enhancing factor in PrP82-146 aggregation
process.
Mol Cell Neurosci. 2009, 40: 217-24
Saracino GA, Villa A, Moro G, Cosentino U, Salmona M.
Spontaneous beta-helical fold in prion protein: The case of PrP(82-146).
Proteins 2008, [Epub ahead of print]
Cosentino U, Pitea D, Moro G, Saracino GA, Caria P, Varì RM, Colombo L, Forloni G, Tagliavini F, Salmona M.
The anti-fibrillogenic activity of tetracyclines on PrP 106-126: a 3D-QSAR study.
J Mol Model. 2008, 14: 987-94
Natalello A, Prokorov VV, Tagliavini F, Morbin M, Forloni G, Beeg M, Manzoni C, Colombo L, Gobbi M, Salmona M, Doglia SM.
Conformational plasticity of the Gerstmann-Sträussler-Scheinker disease peptide as indicated by its multiple aggregation pathways.
J Mol Biol. 2008, 381: 1349-61
Bate C, Tayebi M, Diomede L, Salmona M, Williams A.
Docosahexaenoic and eicosapentaenoic acids increase prion formation in neuronal cells.
BMC Biol. 2008, 6: 39
Bate C, Marshall V, Colombo L, Diomede L, Salmona M, Williams A.
Docosahexaenoic and eicosapentaenoic acids increase neuronal death in response to HuPrP82-146 and Abeta 1-42.
Neuropharmacology 2008, 54: 934-43
De Luigi A, Colombo L, Diomede L, Capobianco R, Mangieri M, Miccolo C, Limido L, Forloni G, Tagliavini F, Salmona M.
The efficacy of tetracyclines in peripheral and intracerebral prion infection.
PLoS ONE 2008, 3: e1888
Luo X, Inouye H, Gross AA, Hidalgo MM, Sharma D, Lee D, Avila RL, Salmona M, Kirschner DA.
Cytoplasmic domain of zebrafish myelin protein zero: adhesive role depends on beta-conformation.
Biophys J. 2007, 93: 3515-28
Luo X, Sharma D, Inouye H, Lee D, Avila RL, Salmona M, Kirschner DA.
Cytoplasmic Domain of Human Myelin Protein Zero Likely Folded as {beta}-Structure
in Compact Myelin.
Biophys J. 2007, 92: 1585-97
Link:
http://www.marionegri.it/mn/en/index.html?l=en
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