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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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== Summary == | == 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. | 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.<ref name="Lin">PMID: 22989878</ref> | ||
== Licensing == | == Licensing == | ||
{{subst:Non-commercial from license selector}} | {{subst:Non-commercial from license selector}} | ||
==References== | |||
<references /> | |||
Revision as of 08:49, 15 November 2012
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
{{subst:Non-commercial from license selector}}
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
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 18:49, 27 February 2023 |  | 640 × 434 (63 KB) | Sloan August (talk | contribs) | |
| 00:13, 3 December 2014 |  | 1,581 × 1,992 (1.24 MB) | Hui-Hsien Lin (talk | contribs) | CLOCK:BMAL1 complex binds to E-box element | |
| 09:36, 14 November 2012 |  | 508 × 672 (493 KB) | Emily Lum (talk | contribs) | 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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