| Publication Type |
Journal Article |
| School or College |
College of Science |
| Department |
Biology |
| Creator |
Beckerle, Mary C. |
| Other Author |
Schmeichel, Karen L. |
| Title |
Molecular dissection of a LIM domain |
| Date |
1997 |
| Description |
LIM domains are novel sequence elements that are found in more than 60 gene products, many of which function as key regulators of developmental pathways. The LIM domain, characterized by the cysteine-rich consensus CX2CX16_23HX2CX2CX2CX16_21CX2-3(C/H/ D), is a specific metal-binding structure that consists of two distinct zinc-binding subdomains. |
| Type |
Text |
| Publisher |
American Society for Cell Biology |
| Volume |
8 |
| Issue |
2 |
| First Page |
219 |
| Last Page |
230 |
| Subject |
LIM domains; Metal-binding; Zyxin; Cysteine-rich proteins |
| Subject LCSH |
Protein-protein interactions; Zinc proteins; Protein binding; Cytoskeletal proteins |
| Language |
eng |
| Bibliographic Citation |
Schmeichel, K. L., & Beckerle, M. C. (1997). Molecular dissection of a LIM domain. Molecular Biology of the Cell, 8(2), 219-30. |
| Rights Management |
(c)American Society for Cell Biology http://www.molbiolcell.org/ |
| Format Medium |
application/pdf |
| Format Extent |
2,900,660 bytes |
| Identifier |
ir-main,6502 |
| ARK |
ark:/87278/s6xp7pd3 |
| Setname |
ir_uspace |
| ID |
705967 |
| Reference URL |
https://collections.lib.utah.edu/ark:/87278/s6xp7pd3 |
