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* Department of Biology, Duke University, Durham, North Carolina 27708-1000
Department of Cell Biology and Anatomy, Finch University of Health Sciences, Chicago Medical School, North Chicago, Illinois 60064
Department of Genetics, University of Cambridge, Cambridge, United Kingdom CB2 3EH
1 Corresponding author: DCMB Group, Department of Biology, Rm. B330G, LSRC Bldg., Duke University, Box 91000, Research Dr., Durham, NC 27708-1000.
E-mail: dkiehart{at}duke.edu
100 and
75 amino acids that follow the first two lobes of the first and second FERM domains are highly conserved among myosin VIIs, suggesting that they compose a conserved myosin tail homology 7 (MyTH7) domain that may be an integral part of the FERM domain or may function independently of it. Together, our data suggest a key role for ck/myoVIIA in the formation of cellular projections and other actin-based functions required for viability. This article has been cited by other articles:
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A. B. Bohil, B. W. Robertson, and R. E. Cheney Myosin-X is a molecular motor that functions in filopodia formation PNAS, August 15, 2006; 103(33): 12411 - 12416. [Abstract] [Full Text] [PDF] |
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Y. Mao, C. Rauskolb, E. Cho, W.-L. Hu, H. Hayter, G. Minihan, F. N. Katz, and K. D. Irvine Dachs: an unconventional myosin that functions downstream of Fat to regulate growth, affinity and gene expression in Drosophila Development, July 1, 2006; 133(13): 2539 - 2551. [Abstract] [Full Text] [PDF] |
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Y. Yang, M. Kovacs, Q. Xu, J. B. Anderson, and J. R. Sellers Myosin VIIB from Drosophila Is a High Duty Ratio Motor J. Biol. Chem., September 16, 2005; 280(37): 32061 - 32068. [Abstract] [Full Text] [PDF] |
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