Crystal structure and mutational analysis of thermostable direct hemolysin from Grimontia hollisae reveals new insights on membrane binding and physiological activity
| dc.citation.epage | 113 | en_US |
| dc.citation.issue | en_US | |
| dc.citation.spage | 113 | en_US |
| dc.citation.volume | 280 | en_US |
| dc.contributor.author | Wu, T. -K. | en_US |
| dc.contributor.department | 生物科技學系 | zh_TW |
| dc.contributor.department | Department of Biological Science and Technology | en_US |
| dc.date.accessioned | 2014-12-08T15:32:43Z | |
| dc.date.available | 2014-12-08T15:32:43Z | |
| dc.date.issued | 2013-07-01 | en_US |
| dc.identifier.issn | 1742-464X | en_US |
| dc.identifier.journal | FEBS JOURNAL | en_US |
| dc.identifier.uri | https://ir.lib.nycu.edu.tw/handle/11536/22850 | |
| dc.identifier.wosnumber | WOS:000325919200356 | |
| dc.language.iso | en_US | en_US |
| dc.title | Crystal structure and mutational analysis of thermostable direct hemolysin from Grimontia hollisae reveals new insights on membrane binding and physiological activity | en_US |
| dc.type | Meeting Abstract | en_US |
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