| Publication Type |
Journal Article |
| School or College |
College of Science |
| Department |
Biology |
| Creator |
Beckerle, Mary C. |
| Other Author |
Drees, Beth; Friederich, Evelyne; Fradelizi, Julie; Louvard, Daniel; Golsteyn, Roy M. |
| Title |
Characterization of the interaction between zyxin and members of the Ena/Vasodilator-stimulated Phosphoprotein family of proteins |
| Date |
2000 |
| Description |
Zyxin contains a proline-rich N-terminal domain that is similar to the C-terminal domain in the ActA protein of the bacteria, Listeria monocytogenes. We screened the entire amino acid sequence of human zyxin for Menainteracting peptides and found that, as with ActA, proline-rich sequences were the sole zyxin sequences capable of binding to Ena/vasodilator-stimulated phosphoprotein (VASP) family members in vitro. |
| Type |
Text |
| Publisher |
American Society for Biochemistry and Molecular Biology (ASBMB) |
| Volume |
275 |
| Issue |
29 |
| First Page |
22503 |
| Last Page |
22511 |
| Subject |
Zyxin; Actin; Listeria monocytogenes; Proline-rich repeats; Cell spreading |
| Subject LCSH |
Phosphoproteins; Cytoskeletal proteins; Cell adhesion |
| Language |
eng |
| Bibliographic Citation |
Drees, B., Friederich, E., Fradelizi, J., Louvard, D., Beckerle, M. C., & Golsteyn, R. M. (2000). Characterization of the interaction between zyxin and members of the Ena/Vasodiloator-stimulated Phosphoprotein family of proteins. Journal of Biological Chemistry, 275(29), 22503-11. |
| Rights Management |
(c)American Society for Biochemistry and Molecular Biology (ASBMB) http://www.asbmb.org/ |
| Format Medium |
application/pdf |
| Format Extent |
418,753 bytes |
| Identifier |
ir-main,6526 |
| ARK |
ark:/87278/s6rb7nt2 |
| Setname |
ir_uspace |
| ID |
703606 |
| Reference URL |
https://collections.lib.utah.edu/ark:/87278/s6rb7nt2 |
