Kafatos:Povelones, Michael: Difference between revisions
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* [[ | * [[pmid:11257614|Sung YJ, Povelones M, and Ambron RT. RISK-1: a novel MAPK homologue in axoplasm that is activated and retrogradely transported after nerve injury. J Neurobiol 2001 Apr; 47(1) 67-79.]] | ||
* [[ | * [[pmid:11153011|Farr M, Zhu DF, Povelones M, Valcich D, and Ambron RT. Direct interactions between immunocytes and neurons after axotomy in Aplysia. J Neurobiol 2001 Feb 5; 46(2) 89-96.]] | ||
* [[ | * [[pmid:9185529|Povelones M, Tran K, Thanos D, and Ambron RT. An NF-kappaB-like transcription factor in axoplasm is rapidly inactivated after nerve injury in Aplysia. J Neurosci 1997 Jul 1; 17(13) 4915-20.]] | ||
* [[pmid:8922402|Ambron RT, Zhang XP, Gunstream JD, Povelones M, and Walters ET. Intrinsic injury signals enhance growth, survival, and excitability of Aplysia neurons. J Neurosci 1996 Dec 1; 16(23) 7469-77.]] | |||
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Revision as of 05:04, 20 August 2006
Michael Povelones Division of Cell & Molecular Biology |
Education
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Current Research InterestsI am a postdoctoral fellow in the Kafatos/Christophides Lab at Imperial College, London. Science is cool. |
Previous ResearchI received my doctoral degree at Stanford University in the laboratory of Roel Nusse. The focus of my research was understanding how the frizzled (fz) receptor in Drosophila functions in planar cell polarization (PCP) and Wnt-mediated cell fate specification. fz controls two different signal transduction pathways for each of these distinct developmental outcomes. How does a single receptor function in two signaling pathways? This work revealed that even though cell fate signaling requires a Wnt ligand, fz is not activated by any of the 7 Drosophila Wnt genes for its PCP function. Instead, fz has an intrinsic ability to control components of the PCP pathway and that it associates with pathway specific Wnt co-receptor for cell fate signaling. In addition, a structure-function analysis of fz suggested that, in addition to the Wnt binding site located in the extracellular cysteine-rich domain, there is a second Wnt-binding site within the transmembrane portion of the receptor.
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