Kinetics of Src Homology 3 Domain Association with the Proli…
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- DOI 10.1074/jbc.m501745200
- PMID https://pubmed.ncbi.nlm.nih.gov/15834155
- OpenAlex ID W2015353371
- Type Article
- Language EN
- Published 18 Apr 2005
- Volume 280 (24)
- Pages 23147–23156
- Source Journal of Biological Chemistry
- Publisher Elsevier BV
- FWCI 2.11
- Countries 1
- Institutions 1
- Added 24 Jun 2016
- Updated 08 Oct 2026
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Kinetics of Src Homology 3 Domain Association with the Proline-rich Domain of Dynamins
Article 2005 EN Hybrid
Dynamin function is mediated in part through association of its proline-rich domain (PRD) with the Src homology 3 (SH3) domains of several putative binding proteins. To assess the specificity and kinetics of this process, we undertook surface plasmon resonance studies of the interaction between isolated PRDs of dynamin-1 and -2 and several purified SH3 domains. Glutathione S-transferase-linked SH3…
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4 authors| # | Author | Institutions | ORCID |
|---|---|---|---|
| 1 | Elena Solomaha | University of Chicago (US) | — |
| 2 | Frances L. Szeto | University of Chicago (US) | — |
| 3 | Mohammed Yousef | University of Chicago (US) | — |
| 4 | H. Clive Palfrey Corresponding | University of Chicago (US) | — |
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