Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Zenglin Yuan"'
Autor:
Yinlong Yang, Yingying Yue, Nannan Song, Cuiling Li, Zenglin Yuan, Yan Wang, Yue Ma, Hui Li, Fengyu Zhang, Weiwei Wang, Haihong Jia, Peng Li, Xiaobing Li, Qi Wang, Zhe Ding, Hongjie Dong, Lichuan Gu, Bingqing Li
Publikováno v:
Cell Reports, Vol 32, Iss 12, Pp 108161- (2020)
Summary: Sensing stressful conditions and adjusting the cellular metabolism to adapt to the environment are essential activities for bacteria to survive in variable situations. Here, we describe a stress-related protein, YdiU, and characterize YdiU a
Externí odkaz:
https://doaj.org/article/8a319b3db9c04ee38abd5981f0db421e
Autor:
Jiaxu Wang, Zenglin Yuan, Yaqi Cui, Rong Xie, Guang Yang, Muzaffer A. Kassab, Mengxi Wang, Yinliang Ma, Chen Wu, Xiaochun Yu, Xiuhua Liu
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Tudor interacting repair regulator (TIRR) is a negative regulator of 53BP1 in DNA damage repair processes. Here the authors give mechanistic insights into how TIRR mediates suppression by solving the crystal structure of TIRR bound to the 53BP1 tande
Externí odkaz:
https://doaj.org/article/c49f7c9d4afb46d58974291e19e39bff
Publikováno v:
Frontiers in Microbiology, Vol 9 (2019)
NrnC from Agrobacterium tumefaciens (At_NrnC, UniProt accession number A9CG28) is a nuclease containing a single DEDDy domain. Here, we determined the structures of both the apo and metal-ion-bound forms of At_NrnC. Although the overall structure of
Externí odkaz:
https://doaj.org/article/7d4236335b09495899562af3f4130615
Autor:
Jiaxu Wang, Zenglin Yuan, Yaqi Cui, Rong Xie, Guang Yang, Muzaffer A. Kassab, Mengxi Wang, Yinliang Ma, Chen Wu, Xiaochun Yu, Xiuhua Liu
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-1 (2019)
The original version of this Article contained an error in the author affiliations. Xiaochun Yu was incorrectly associated with College of Life Sciences, Hebei University, Baoding 071000 Hebei, China.This has now been corrected in both the PDF and HT
Externí odkaz:
https://doaj.org/article/e304da6f4ddb4ec9829784224a4d7bf5
Autor:
Yijun Du, Jiaqiang Wu, Bin Wei, Jinbao Wang, Guijun Shang, Jun Li, Lichuan Gu, Bo Wu, Sujuan Xu, Feng Li, Defen Lu, Xiaoyan Cong, Zenglin Yuan, Jing Qi, Xiangju Wu, Youjia Zhang
Publikováno v:
Journal of Biological Chemistry. 294:11420-11432
The cyclic dinucleotide (CDN)-stimulator of interferon genes (STING) pathway plays an important role in the detection of viral and bacterial pathogens in animals. Previous studies have shown that the metazoan second messenger cyclic [G(2′,5′)pA(3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d79d582a5b2777ccc5fa0a4936888a21
https://doi.org/10.1074/jbc.ra119.007367
https://doi.org/10.1074/jbc.ra119.007367
Autor:
Ming Peng, Tian-Di Wei, Fang Zhao, Zenglin Yuan, Hai-Yan Cao, Wei-Ling Shi, Yu-Zhong Zhang, Xuan Shao, Jonathan D. Todd, Peng Wang, Xiu-Lan Chen, Chun-Yang Li, Xiao-Hua Zhang
Publikováno v:
Molecular Microbiology
Summary The vast majority of oceanic dimethylsulfoniopropionate (DMSP) is thought to be catabolized by bacteria via the DMSP demethylation pathway. This pathway contains four enzymes termed DmdA, DmdB, DmdC and DmdD/AcuH, which together catabolize DM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f03a8b7198f0745d8f98f44f43af98fc
https://doi.org/10.1111/mmi.14211
https://doi.org/10.1111/mmi.14211
Autor:
Xiuhua Liu, Rong Xie, Xiaochun Yu, Guang Yang, Jiaxu Wang, Yinliang Ma, Chen Wu, Mengxi Wang, Zenglin Yuan, Muzaffer Ahmad Kassab, Yaqi Cui
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
53BP1 performs essential functions in DNA double-strand break (DSB) repair and it was recently reported that Tudor interacting repair regulator (TIRR) negatively regulates 53BP1 during DSB repair. Here, we present the crystal structure of the 53BP1 t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4cbfa6bbc312650e998be60c50d5285
https://doaj.org/article/c49f7c9d4afb46d58974291e19e39bff
https://doaj.org/article/c49f7c9d4afb46d58974291e19e39bff
Publikováno v:
Biochemical and Biophysical Research Communications. 501:423-427
The pathogenic Mycobacterium tuberculosis encodes two members of the DtxR family metalloregulators, IdeR and MntR. IdeR represses gene expression in response to ferrous iron, while MntR (Rv2788) functions as a manganese-dependent transcriptional repr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e461da06ce2a19e52ae2c759090816f7
https://doi.org/10.1016/j.bbrc.2018.05.005
https://doi.org/10.1016/j.bbrc.2018.05.005
Publikováno v:
Biochemical and Biophysical Research Communications. 490:774-779
AP endonuclease recognizes and cleaves apurinic/apyrimidinic (AP) sites and plays a critical role in base excision repair. Many ExoIII and EndoIV family AP endonucleases have been characterized both biochemically and structurally in Eukaryote and Bac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6b4a006730219208a2910bc9b5b512c
https://doi.org/10.1016/j.bbrc.2017.06.116
https://doi.org/10.1016/j.bbrc.2017.06.116
Autor:
Yinlong Yang, Fengyu Zhang, B Li, Peng Li, Zhihui Li, Yingying Yue, Lichuan Gu, Zenglin Yuan, Yan Liu, Wei Lin, Nannan Song
Publikováno v:
Nucleic Acids Research
Salmonella reduces flagella biogenesis to avoid detection within host cells by a largely unknown mechanism. We identified an EAL-like protein STM1697 as required and sufficient for this process. STM1697 surges to a high level after Salmonella enters
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6a80dc8e3f4abd9154d47c39bef8b0d
https://doi.org/10.1093/nar/gkx656
https://doi.org/10.1093/nar/gkx656