User:C Strambio-De-Castillia
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Contact Info
- C Strambio-De-Castillia
- University of Massachusetts Medical Scool
- Program In Molecular Medicine
- University of Massachusetts Medical School
- 373 Plantation Street, Biotech II, Suite 114
- Worcester, MA, 01605
- Email me through OpenWetWare
Education
- 1998, PhD, The Rockefeller University
- 1988, Universita' degli Studi di Pavia, Pavia, Italy
Research interests
- HIV-1 viral entry in human target cells
- HIV-1 interactions with dendritic cells and antiviral response
- Nuclear envelope structure
- Viral particle tracking
- Bioimage informatics
Publications
- Pertel T, Hausmann S, Morger D, Züger S, Guerra J, Lascano J, Reinhard C, Santoni FA, Uchil PD, Chatel L, Bisiaux A, Albert ML, Strambio-De-Castillia C, Mothes W, Pizzato M, Grütter MG, and Luban J. TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature. 2011 Apr 21;472(7343):361-5. DOI:10.1038/nature09976 |
- Strambio-De-Castillia C, Niepel M, and Rout MP. The nuclear pore complex: bridging nuclear transport and gene regulation. Nat Rev Mol Cell Biol. 2010 Jul;11(7):490-501. DOI:10.1038/nrm2928 |
- Sokolskaja E, Olivari S, Zufferey M, Strambio-De-Castillia C, Pizzato M, and Luban J. Cyclosporine blocks incorporation of HIV-1 envelope glycoprotein into virions. J Virol. 2010 May;84(9):4851-5. DOI:10.1128/JVI.01699-09 |
- Neagu MR, Ziegler P, Pertel T, Strambio-De-Castillia C, Grütter C, Martinetti G, Mazzucchelli L, Grütter M, Manz MG, and Luban J. Potent inhibition of HIV-1 by TRIM5-cyclophilin fusion proteins engineered from human components. J Clin Invest. 2009 Oct;119(10):3035-47. DOI:10.1172/JCI39354 |
- Sebastian S, Grütter C, Strambio de Castillia C, Pertel T, Olivari S, Grütter MG, and Luban J. An invariant surface patch on the TRIM5alpha PRYSPRY domain is required for retroviral restriction but dispensable for capsid binding. J Virol. 2009 Apr;83(7):3365-73. DOI:10.1128/JVI.00432-08 |
- Niepel M, Strambio-de-Castillia C, Fasolo J, Chait BT, and Rout MP. The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly. J Cell Biol. 2005 Jul 18;170(2):225-35. DOI:10.1083/jcb.200504140 |
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- ISBN:0879697164