Image:Binding.png
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Summary
Full length RII of PfEBA-140 binds extensively to erythrocytes (top image), while individual DBL domains show little binding. This indicates that both domains are necessary for erythrocyte binding.[1]
Licensing
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This research was originally published in The Journal of Biological Chemistry. Daniel H. Lin, Brian M. Malpede, Joseph D. Batchelor and Niraj H. Tolia. Crystal and Solution Structures of Plasmodium falciparum Erythrocyte-binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte Invasion. J Biol Chem. 2012; Vol:287. 36830-36836. © the American Society for Biochemistry and Molecular Biology."
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References
- ↑ Lin DH, Malpede BM, Batchelor JD, Tolia NH. Crystal and Solution Structures of Plasmodium falciparum Erythrocyte-binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte Invasion. J Biol Chem. 2012 Oct 26;287(44):36830-6. doi: 10.1074/jbc.M112.409276. Epub 2012, Sep 18. PMID:22989878 doi:10.1074/jbc.M112.409276
File history
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| Date/Time | User | Dimensions | File size | Comment | |
|---|---|---|---|---|---|
| (current) | 18:49, 27 February 2023 | Sloan August (Talk | contribs) | 640×434 | 63 KB | |
| 00:13, 3 December 2014 | Hui-Hsien Lin (Talk | contribs) | 1581×1992 | 1.24 MB | CLOCK:BMAL1 complex binds to E-box element | |
| 09:36, 14 November 2012 | Emily Lum (Talk | contribs) | 508×672 | 493 KB | Full length RII of PfEBA-140 binds extensively to erythrocytes (top image), while individual DBL domains show little binding. This indicates that both domains are necessary for erythrocyte binding. |
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