Mechanisms of apoptotic phosphatidylserine exposure
It has been a long-standing enigma which scramblase causes phosphati- dylserine residues to be exposed on the surface of apoptotic cells, thereby facilitating the phagocytic recogni- tion, engulfment and destruction of apoptotic corpses. In a recent paper in Science, Nagata and coworkers reveal that...
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Published in | Cell research Vol. 23; no. 11; pp. 1247 - 1248 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
01.11.2013
Nature Publishing Group |
Subjects | |
Online Access | Get full text |
ISSN | 1001-0602 1748-7838 1748-7838 |
DOI | 10.1038/cr.2013.115 |
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Summary: | It has been a long-standing enigma which scramblase causes phosphati- dylserine residues to be exposed on the surface of apoptotic cells, thereby facilitating the phagocytic recogni- tion, engulfment and destruction of apoptotic corpses. In a recent paper in Science, Nagata and coworkers reveal that the scramblases Xkr8 and its C. elegans ortholog, CED-8, are activated by caspase cleavage in apoptotic cells. |
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Bibliography: | 31-1568/Q It has been a long-standing enigma which scramblase causes phosphati- dylserine residues to be exposed on the surface of apoptotic cells, thereby facilitating the phagocytic recogni- tion, engulfment and destruction of apoptotic corpses. In a recent paper in Science, Nagata and coworkers reveal that the scramblases Xkr8 and its C. elegans ortholog, CED-8, are activated by caspase cleavage in apoptotic cells. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Commentary-3 content type line 23 |
ISSN: | 1001-0602 1748-7838 1748-7838 |
DOI: | 10.1038/cr.2013.115 |