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dc.contributor.authorZhang, Duanwu
dc.contributor.authorLin, Juan
dc.contributor.authorHan, Jiahuai
dc.contributor.author韩家淮
dc.date.accessioned2011-07-13T02:47:54Z
dc.date.available2011-07-13T02:47:54Z
dc.date.issued2010-04
dc.identifier.citationCellular & Molecular Immunology (2010) 7, 243–249zh_CN
dc.identifier.issn1672-7681
dc.identifier.urihttp://dx.doi.org/doi:10.1038/cmi.2010.10
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10129
dc.description.abstractReceptor-interacting protein (RIP) kinases are a group of threonine/serine protein kinases with a relatively conserved kinase domain but distinct non-kinase regions. A number of different domain structures, such as death and caspase activation and recruitment domain (CARD) domains, were found in different RIP family members, and these domains should be keys in determining the specific function of each RIP kinase. It is known that RIP kinases participate in different biological processes, including those in innate immunity, but their downstream substrates are largely unknown. This review will give an overview of the structures and functions of RIP family members, and an update of recent progress in RIP kinase research. Cellular & Molecular Immunology (2010) 7, 243-249; doi:10.1038/cmi.2010.10; published online 12 April 2010zh_CN
dc.language.isoenzh_CN
dc.publisherNATURE PUBLISHING GROUPzh_CN
dc.subjectapoptosiszh_CN
dc.subjectkinasezh_CN
dc.subjectnecrosiszh_CN
dc.subjectRIPzh_CN
dc.subjectTNFzh_CN
dc.titleReceptor-interacting protein (RIP) kinase familyzh_CN
dc.typeArticlezh_CN


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