典型文献
BAP60 plays an opposite role to the MRT-NURF complex in regulating lipid droplet size
文献摘要:
The lipid droplet(LD)is a unique cellular organelle with a phos-pholipid monolayer coated with resident proteins.LDs are impor-tant for cellular neutral lipid storage and utilization.As spherical balls,LDs accommodate a lot more neutral lipids with a small in-crease of size.Disrupted LD dynamics,which can be reflected by abnormal LD size alteration,has been linked to many important metabolic diseases,including obesity,neutral lipid storage disease(NLSD),liver diseases,neurodegenerative diseases,and others(Gong et al.,2009;Greenberg et al.,2011;Krahmer et al.,2013;Farmer et al.,2020;Teixeira et al.,2021).LD size regulators,in particular proteins localized on LDs,have been extensively studied in yeast,worm,fly and mammalian cells(Yu and Li,2017).The tran-scriptional and post-transcriptional regulation of LD size are rela-tively less explored.
文献关键词:
中图分类号:
作者姓名:
Yan Yao;Mengyao Xu;Lianyong Qiao;Hu Nie;Falong Lu;Xun Huang
作者机构:
State Key Laboratory of Molecular Developmental Biology,Institute of Genetics and Developmental Biology,Chinese Academy of Sciences,Beijing 100101,China;University of Chinese Academy of Sciences,Beijing 100049,China
文献出处:
引用格式:
[1]Yan Yao;Mengyao Xu;Lianyong Qiao;Hu Nie;Falong Lu;Xun Huang-.BAP60 plays an opposite role to the MRT-NURF complex in regulating lipid droplet size)[J].遗传学报,2022(04):377-379
A类:
BAP60,NURF,pholipid,Krahmer,Farmer,Teixeira
B类:
plays,opposite,role,MRT,complex,regulating,droplet,size,unique,cellular,organelle,phos,monolayer,coated,resident,proteins,LDs,are,neutral,storage,utilization,spherical,balls,accommodate,lot,more,lipids,small,crease,Disrupted,dynamics,which,can,reflected,by,abnormal,alteration,has,been,linked,many,important,metabolic,diseases,including,obesity,NLSD,liver,neurodegenerative,others,Gong,Greenberg,regulators,particular,localized,have,extensively,studied,yeast,worm,fly,mammalian,cells,Yu,Li,post,transcriptional,regulation,rela,tively,less,explored
AB值:
0.548117
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