Publication Type |
Journal Article |
School or College |
College of Science |
Department |
Biology |
Creator |
Beckerle, Mary C. |
Other Author |
Ahern-Djamali, Shawn M.; Comer, Allen R.; Bachmann, Christiane; Kastenmeier, Andrew S.; Srinevas, K. Reddy; Hua, Ping; Walter, Ulrich; Hoffmann, F. Michael |
Title |
Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1) and EVH2 domains |
Date |
1998 |
Description |
Drosophila Enabled (Ena) was initially identified as a dominant genetic suppressor of mutations in the Abelson tyrosine kinase and, more recently, as a member of the Ena/human vasodilator-stimulated phosphoprotein (VASP) family of proteins. We have used genetic, biochemical, and cell biological approaches to demonstrate the functional relationship between Ena and human VASP. |
Type |
Text |
Publisher |
American Society for Cell Biology |
Volume |
9 |
First Page |
2157 |
Last Page |
2171 |
Subject |
Drosophila Ena; VASP |
Subject LCSH |
Phosphoproteins; Cell adhesion; Cytoskeletal proteins; Cytoskeleton -- Formation; Drosophila -- Genetics; Drosophila -- Development |
Dissertation Institution |
University of Utah |
Language |
eng |
Bibliographic Citation |
Ahern-Djamali, S. M., Comer, A. R., Bachmann, C., Kastenmeier, A. S., Srinevas, K. R., Hua, P., Beckerle, M. C., Walter, U., & Hoffmann, F. M. (1998). Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1) and EVH2 domains. Molecular Biology of the Cell, 9, 2157-71. |
Rights Management |
(c)American Society for Cell Biology http://www.molbiolcell.org/ |
Format Medium |
application/pdf |
Format Extent |
816,184 bytes |
Identifier |
ir-main,6513 |
ARK |
ark:/87278/s61z4p25 |
Setname |
ir_uspace |
ID |
707239 |
Reference URL |
https://collections.lib.utah.edu/ark:/87278/s61z4p25 |