Výsledky vyhledávání - "FU Ming-lian"

Structural characterization of the redefined DNA-binding domain of human XPA

Autor: Chengmin Qian, Wancai Yang, Yong-Liang Jiang, Xiangwei Yang, Fu-Ming Lian

Publikováno v: Biochemical and Biophysical Research Communications. 514:985-990

XPA (xeroderma pigmentosum complementation group A), a key scaffold protein in nucleotide excision repair (NER) pathway, is important in DNA damage verification and repair proteins recruitment. Earlier studies had mapped the minimal DNA-binding domai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2938a6daadc05e5a86a044daa395f565
https://doi.org/10.1016/j.bbrc.2019.05.050

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Akademický článek

The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions.

Autor: Yinnan Mu, Fu-Ming Lian, Yan-Bin Teng, Jingqun Ao, Yong-Liang Jiang, Yong-Xing He, Yuxing Chen, Cong-Zhao Zhou, Xinhua Chen

Publikováno v: PLoS ONE, Vol 8, Iss 2, p e57061 (2013)

Peroxiredoxins (Prxs) are thiol-specific antioxidant proteins that exhibit peroxidase and peroxynitrite reductase activities involved in the reduction of reactive oxygen species. The peroxiredoxin Prx4 from the large yellow croaker Pseudosciaena croc

Externí odkaz: https://doaj.org/article/d01f9dc3ed3b4945819c7ee2ef950ca1

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The redefined DNA-binding domain of human xeroderma pigmentosum complementation group A: production, crystallization and structure solution

Autor: Yong-Liang Jiang, Xiangwei Yang, Chengmin Qian, Fu-Ming Lian, Wancai Yang

Publikováno v: Acta Crystallogr F Struct Biol Commun

Human xeroderma pigmentosum complementation group A (XPA) is a scaffold protein that plays significant roles in DNA-damage verification and in recruiting downstream endonucleases to facilitate the repair of DNA lesions in nucleotide-excision repair.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a83ba4b06768cdb1e96e3966f1224d4a
https://doi.org/10.1107/s2053230x18016990

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Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with thioredoxin Trx2 mimics a conformational intermediate during the catalytic cycle

Autor: Xiangwei Yang, Yong-Liang Jiang, Wancai Yang, Fu-Ming Lian

Publikováno v: International journal of biological macromolecules. 161

Peroxiredoxin (Prx) is a thiol-based peroxidase that eliminates reactive oxygen species to avoid oxidative damage. Alkyl hydroperoxide reductase Ahp1 is a novel and specific typical 2-cysteine Prx. Here, we present the crystal structure of sulfonic A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71aceb45be0621f74f851f09729ffe13
https://pubmed.ncbi.nlm.nih.gov/32531362

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Akademický článek

Quality characteristics and drought tolerance evaluation of Brassica juncea in Yunnan Province. (English)

Autor: YUAN Xiao-yan, FU Ming-lian, ZHANG Yun-yun, LI Gen-ze, WANG Jing-qiao, ZU Feng, LUO Yanqing, ZHAO Kai-qin, HE Xiao-ying

Publikováno v: Chinese Journal of Oil Crop Sciences; 2020, Vol. 42 Issue 4, p573-584, 12p

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Structural Snapshots of Yeast Alkyl Hydroperoxide Reductase Ahp1 Peroxiredoxin Reveal a Novel Two-cysteine Mechanism of Electron Transfer to Eliminate Reactive Oxygen Species

Autor: Xiao-Xiao Ma, Xiao-Jie Yu, Jiang Yu, Fu-Ming Lian, Yuxing Chen, Cong-Zhao Zhou

Publikováno v: Journal of Biological Chemistry. 287:17077-17087

Peroxiredoxins (Prxs) are thiol-specific antioxidant proteins that protect cells against reactive oxygen species and are involved in cellular signaling pathways. Alkyl hydroperoxide reductase Ahp1 belongs to the Prx5 subfamily and is a two-cysteine (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86a2d1cd28bd9f8e618d8d3863c4ddef
https://doi.org/10.1074/jbc.m112.357368

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Crystal structure and SUMO binding of Slx1-Slx4 complex

Autor: Si Xie, Chengmin Qian, Fu-Ming Lian

Publikováno v: Scientific Reports

The SLX1-SLX4 complex is a structure-specific endonuclease that cleaves branched DNA structures and plays significant roles in DNA recombination and repair in eukaryotic cells. The heterodimeric interaction between SLX1 and SLX4 is essential for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::722dae9cd2bfec48ac5f808d383eff70
http://europepmc.org/articles/PMC4726241

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