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John J. Dumas Dept. of Chemical & Screening Sciences Wyeth (formerly Genetics Institute) 200 CambridgePark Drive Cambridge, MA 02140 |
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| [email protected] | ||||||||||||||||||||
| PUBLICATIONS | ||||||||||||||||||||
| Dumas, J.J., Kumar, R., Sullivan, F., Stahl, M.L, Somers, W.S., Mosyak, L. Crystal structure of the wild-type Von Willebrand Factor A1-Glycoprotein Ib(alpha) complex reveals conformation differences with a complex bearing Von Willebrand Disease mutations. (2004) J. Biol. Chem., 279: 23327-23334. [abstract] Dumas, J.J., Kumar, R., Seehra, J., Somers, W.S., Mosyak, L. Crystal structure of the GpIb-alpha/thrombin complex essential for platelet aggregation. (2003) Science, 301: 222-226. [abstract] Lawe, D.C., Chawla, A., Merithew, E., Dumas, J., Carrington, W., Fogarty, K., Lifshitz, L., Tuft, R., Lambright, D., and Corvera, S. Sequential roles for phosphatidylinositol-3-phosphate and Rab5 in tethering and fusion of early endosomes via their interaction with EEA1. (2002) J. Biol. Chem., 277: 8611-8617. [abstract] Dumas, J.J., Merithew, E., Sudharshan, E., Rajamani, D., Hayes, S., Lawe, D., Corvera, S., and Lambright, D.G. Multivalent endosome targeting by homodimeric EEA1. (2001) Mol. Cell, 8: 947-958. [abstract] Zhu, Z., Dumas, J.J., Lietzke, S.E., and Lambright, D.G. A helical turn motif in Mss4 is a critical determinant of Rab binding and nucleotide release. (2001) Biochemistry, 40: 3027-3036. [abstract] Merithew, E., Hatherley, S., Dumas, J.J., Lawe, D.C., Heller-Harrison, R., and Lambright, D.G. Structural plasticity of an invariant hydrophobic triad in the switch regions of Rab GTPases is a determinant of effector recognition. (2001) J. Biol. Chem., 276: 13982-13988. [abstract] Dumas, J.J., Zhu, Z., Connolly, J.L., and Lambright, D.G. Structural basis of activation and GTP hydrolysis in Rab proteins. (1999) Structure, 7: 413-423. [abstract] Dumas, J.J. and Lambright, D.G. Gs alpha meets its target - Shedding light on a key signal transduction event. (1998) Structure, 6: 407-411. [abstract] Dumas, J.J. Direct demonstration of the interaction of alpha q, alpha 11, and a novel 97 kDa protein with the substance P receptor. (1997) Doctoral dissertation. Macdonald, S.G., Dumas, J.J., and Boyd, N.D. Chemical cross-linking of the substance P (NK-1) receptor to the alpha subunits of G proteins Gq and G11. (1996) Biochemistry, 35: 2909-2916. [abstract] Boyd, N.D., Kage, R., Dumas, J.J., Krause, J.E., and Leeman, S.E. The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: Presence of a disulfide bond. (1996) Proc. Natl. Acad. Sci. U. S. A., 93: 433-437. [abstract] Boyd, N.D., Kage, R., Dumas, J.J., Silberman, S.C., Krause, J.E., and Leeman, S.E. Localization of the peptide binding domain of the NK-1 tachykinin receptor using photoreactive analogues of substance P. (1995) N. Y. Acad. Sci. Proc., 757: 405-413. |
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| RECENT PRESENTATIONS | ||||||||||||||||||||
| Dumas, J.J., Kumar, R., Sullivan, F., Stahl, M.L, Somers, W.S., Mosyak, L. Crystal structure of the wild-type Von Willebrand Factor A1-Glycoprotein Ib(alpha) complex reveals conformation differences with a complex bearing Von Willebrand Disease mutations. Wyeth Discovery Annual Meeting, May, 2004. Dumas, J.J. Structure of the GpIb(alpha)-thrombin complex essential for platelet aggregation. Invited Seminar. Advanced Light Source - LBNL, Berkeley, CA, March, 2004. Dumas, J.J. Crystal structure of the GpIb(alpha)-thrombin complex essential for platelet aggregation. Wyeth Research Postdoc Day, October, 2003. Dumas, J.J., Merithew, E., Corvera, S., Lambright, D.G. The crystal structure of an EEA1 homodimer bound to phosphatidyl inositol 3-phosphate. Woods Hole Annual Retreat, 2001. Dumas, J.J. Regulation of membrane trafficking: Insights from high resolution structures of Rab GTPases. UMMS Program in Molecular Medicine, Postdoc Data Club, December, 1999. Dumas, J.J. The structural basis of activation and GTP hydrolysis in Rab proteins. UMass Biophysics Group Seminar, January, 1999. |
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| Cell Nature Protein Data Bank PubMed Science Software |
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