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Anthony N. Brady Professor of Pathology and Cell Biology Director, Boyer Center for Molecular Medicine |
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| Marchesi lab website Phone: (203) 737-2775 / -2263 e-mail: vincent.marchesi@Yale.edu |
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Department of Pathology <Courier Address> |
We investigate the regulation of cell division. Among the questions to be answered, if we are to understand mitosis at the molecular level, are (1) what triggers the disassembly of the interphase cytoskeleton, (2) what organizes the assembly of the nascent mitotic spindle, (3) how do the mitotic spindle tubules make contact with and then help orient the paired chromatids along the metaphase plate, and (4) what triggers first the anaphase separation of the sister chromatids and then their segregation to each of the progeny. We have developed simple methods for the isolation of synchronized cultured cells that progress through one complete mitotic cycle in a 70 min. period. These cells can be studied both morphologically and biochemically, and they can be transfected with specific genes whose expression can be controlled. A long term goal of this work is to identify specific inhibitors that may be used to control neoplastic proliferation.
Cai SY, Babbitt RW, Marchesi V (1999)@A mutant deubiquitinating enzyme \(Ubp-M\) associates with mitotic chromosomes and blocks cell division. Proceedings of the National Academy of Sciences (USA). 96(6): 2828-33.
Marchesi V T. (1996) The life sciences forum--a call for contributions [editorial]. Faseb Journal. 10(10): 1111.
Baklouti F, Huang SC, Tang TK, Delaunay J, Marchesi VT, Benz EJ Jr. (1995) Asynchronous regulation of splicing events within protein 4.1 pre-mRNA during erythroid differentiation.. Blood. 87(9): 3934-41, 1 May 1996
Marchesi V T. Yale's Boyer Center for molecular medicine. Molecular Medicine. 1(5): 477-8.
Huang JP, Tang CJ, Kou GH, Marchesi VT, Benz EJ Jr, Tang TK. (1993) Genomic structure of the locus encoding protein 4.1. Structural basis for complex combinational patterns of tissue-specific alternative RNA splicing. Journal of Biological Chemistry. 268(5): 3758-66.
Marchesi VT, Ngo N. (1993) In vitro assembly of multi-protein complexes containing alpha, beta, and gamma tubulin, Hsp 70 and elongation factor 1-alpha. Proc. Natl. Acad. Sci. 90:3028-3032.
Huang JP, Tang CJ, Kou GH, Marchesi VT, Bentz Jr. EJ, Tang TK. (1993) Genomic structure of the locus encoding protein 4.1 Journal Biol. Chem. 268:3758-3766.
Winkelmann, J.C., Chang, J.G., Tse, W. T., Scarpa, A.L., Marchesi, V.T., and FOrget, B.G. (1990) Full-length sequence of the cDNA for human erythroid b specrtrin. J. Biol. Cehm ., 265:11827-11832.
Sahr, K. E., Laurila, P., Kotula, L., Scarpa, A. L., Coupal, E., Leto, T. L., Linnenbach, A. J., Winkelmann, J. C., Speicher, D. W., Marchesi, V. T., Curtis, P. J. and Forget, B. G (1990) The complete cDNA and polypeptide sequences of human erythroid a-spectrin. J. Biol. Chem., 265:4434-4443.
Tang K. Tang, Qin, Z., Leto, T.L., Marchesi, V.T., and Benz, E.J., Jr. (1990) Human erythroid and non-erythroid cells is composed of multiple isoforms with novel sizes, functions and tissue specific expression. Cell Molec. Biol. of Normal and Abnormal Erythroid Membranes, 43-59.
Tang K. Tang, Qin, Z., Leto, T.L., Marchesi, V.T., and Benz, E.J., Jr. (1990) Heterogeneity of mRNA and protein products arising from the protein 4.1 gene in erythroid and non-erythroid tissues. J.Cell Biol. 110: 617-624.
