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作 者:Jinzhao Liu Meiyao Chu Jiahui Kuang Xinran Wang Yijie Zhang Lutian Wang Yimeng Xia Yifan Sun Xinxin Liu Jing Li Jun Li Ting Zhu
机构地区:[1]College of Life Science,Liaoning Normal University,Dalian 116081,China [2]Lamprey Research Center,Liaoning Normal University,Dalian 116081,China [3]Collaborative Innovation Center of Seafood Deep Processing,Dalian Polytechnic University,Dalian 116081,China
出 处:《Acta Biochimica et Biophysica Sinica》2024年第3期490-493,共4页生物化学与生物物理学报(英文版)
基 金:This work was supported by the grants from the Liaoning Revitalization Talents Program(No.XLYC2203055 to T.Z.);the National Natural Science Foundation of China(No.31601044 to T.Z.);the Scientific Research Foundation of the Higher Education Institutions of Liaoning Province,China(Nos.LQ2020025 to T.Z.,LJ2020012 to J.L.,and LJKZ0990 to X.L.);the High Lever Talent Innovation Support Project from Dalian(No.2020RQ081 to T.Z.);the Undergraduate Innovation and Entrepreneurship Training Program Support Project(No.X202310165098 to J.L.);the PhD Startup Fund of Liaoning Normal University(No.BS2020L005 to J.L.).
摘 要:The myxovirus resistance(Mx)protein has strong GTP phosphohydrolase(GTPase)activity and is a member of the evolutionarily conserved GTPase dynamin protein family.The Mx protein sequence is divided into three parts:the amino-terminal GTPase domain,the central interactive domain(CID),and the carboxylterminal GTPase effector domain(GED)with a leucine zipper motif[1].The GTPase domain,a relatively conserved part of the Mx protein and other members of the dynamin protein family,is composed of approximately 300 amino acids.
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