| First Author | Takai M | Year | 2013 |
| Journal | Biosci Biotechnol Biochem | Volume | 77 |
| Issue | 5 | Pages | 1134-7 |
| PubMed ID | 23649248 | Mgi Jnum | J:312041 |
| Mgi Id | MGI:6782842 | Doi | 10.1271/bbb.130072 |
| Citation | Takai M, et al. (2013) Assessment of key amino-acid residues of CD36 in specific binding interaction with an oxidized low-density lipoprotein. Biosci Biotechnol Biochem 77(5):1134-7 |
| abstractText | CD36 binds oxidized low-density lipoprotein (oxLDL). A synthetic peptide comprising amino-acid residues 149-168 of mouse CD36 was recently found to bind fluorescence-labeled oxLDL particles. Based on our oxLDL-binding analysis of various synthetic CD36 peptides, we suggest that not only hydrophilic residues (e.g., Lys164 and Lys166) but also hydrophobic ones (e.g., Phe153, Leu158, and Leu161) are critical to binding. |
