Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Hui-Yan Lei"'
Publikováno v:
The Journal of Biological Chemistry
Background: The human multiple aminoacyl-tRNA synthetase complex (MSC) has an elongated and multiarmed structure, which might be sensitive to proteases such as calpain in vivo. Results: Partial calpain hydrolysis of MSC components generated specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c688ea52be1ec6dfa35b3d65cc43a3b5
https://doi.org/10.1074/jbc.m115.681999
https://doi.org/10.1074/jbc.m115.681999
Autor:
Zhi-Rong Ruan, Xiao-Long Zhou, Gilbert Eriani, Qing Ye, En-Duo Wang, Zhi-Peng Fang, Hui-Yan Lei
Publikováno v:
Journal of Biological Chemistry. 290:1664-1678
Aminoacyl-tRNA synthetases (aaRSs) are a group of ancient enzymes catalyzing aminoacylation and editing reactions for protein biosynthesis. Increasing evidence suggests that these critical enzymes are often associated with mammalian disorders. Theref
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61904bc7680d00e1928b1e02296d7295
https://doi.org/10.1074/jbc.m114.599886
https://doi.org/10.1074/jbc.m114.599886
Autor:
Yan-Fei Wen, Ru Ding, Hui-Yan Lei, Zhihua Gong, Xiao-Long Gu, Ding-Cheng Xiang, Jian Qiu, Zheng-Hua Dong, Lan Ma, Na Ma, Jun Huang
Publikováno v:
Biochemical and Biophysical Research Communications. 443:932-937
Stromal cell-derived factor-1 (SDF-1) plays critical roles in vascular development and hematopoiesis. Here, we investigated the function of SDF-1 rs1801157G/A polymorphism in various immune cells and examined its association with susceptibility to co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24e4aef4a58ec16552f96cb00920c530
https://doi.org/10.1016/j.bbrc.2013.12.065
https://doi.org/10.1016/j.bbrc.2013.12.065
Autor:
Liang-Liang Ruan, Dao-Hai Du, Gilbert Eriani, Hui-Yan Lei, En-Duo Wang, Xiao-Long Zhou, Min Tan
Publikováno v:
Nucleic Acids Research
Aminoacyl-tRNA synthetases (aaRSs) are remarkable enzymes that are in charge of the accurate recognition and ligation of amino acids and tRNA molecules. The greatest difficulty in accurate aminoacylation appears to be in discriminating between highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a56548a52e552de5a9033e240fab70df
https://doi.org/10.1093/nar/gkr595
https://doi.org/10.1093/nar/gkr595
Publikováno v:
Journal of Biological Chemistry. 285:39437-39446
The free form of human cytoplasmic arginyl-tRNA synthetase (hcArgRS) is hypothesized to participate in ubiquitin-dependent protein degradation by offering arginyl-tRNA(Arg) to arginyl-tRNA transferase (ATE1). We investigated the effect of hemin on hc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52666ed07bc8bb5cf8fe27a9167bd028
https://doi.org/10.1074/jbc.m110.159913
https://doi.org/10.1074/jbc.m110.159913
Publikováno v:
RNA (New York, N.Y.). 20(9)
Leucyl-tRNA synthetases (LeuRSs) catalyze the linkage of leucine with tRNALeu. LeuRS contains a catalysis domain (aminoacylation) and a CP1 domain (editing). CP1 is inserted 35 Å from the aminoacylation domain. Aminoacylation and editing require CP1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecba58a9d63747d59e0199c4c6bdbc17
https://pubmed.ncbi.nlm.nih.gov/25051973
https://pubmed.ncbi.nlm.nih.gov/25051973
Publikováno v:
China Journal of Chinese Materia Medica; 8/1/2024, Vol. 49 Issue 15, p4044-4053, 10p
Autor:
Lin, Yan1,2 (AUTHOR), Yan, Hui1,2 (AUTHOR), Cao, Lei1,2 (AUTHOR), Mou, Daolin1,2 (AUTHOR), Ding, Dajiang1,2 (AUTHOR), Qin, Binting1,2 (AUTHOR), Che, Lianqiang1,2 (AUTHOR), Fang, Zhengfeng1,2 (AUTHOR), Xu, Shengyu1,2 (AUTHOR), Zhuo, Yong1,2 (AUTHOR), Li, Jian1,2 (AUTHOR), Wang, Jianping1,2 (AUTHOR), Huang, Chao3 (AUTHOR), Zou, Yuanfeng3 (AUTHOR), Li, Lixia3 (AUTHOR), Wu, De1,2 (AUTHOR) wude@sicau.edu.cn, Feng, Bin1,2 (AUTHOR) fengbin@sicau.edu.cn
Publikováno v:
Journal of Animal Science & Biotechnology. 11/4/2022, Vol. 13 Issue 1, p1-12. 12p.
Publikováno v:
Journal of Central South University; Feb2023, Vol. 30 Issue 2, p613-624, 12p
Publikováno v:
Journal of Biological Chemistry. 12/10/2010, Vol. 285 Issue 50, p39437-39446. 10p.