Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Muyun Xie"'
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
Autor:
Xinrui Gui, Feng Luo, Yichen Li, Heng Zhou, Zhenheng Qin, Zhenying Liu, Jinge Gu, Muyun Xie, Kun Zhao, Bin Dai, Woo Shik Shin, Jianhua He, Lin He, Lin Jiang, Minglei Zhao, Bo Sun, Xueming Li, Cong Liu, Dan Li
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Low complexity (LC) domains can drive the formation of both amyloid fibrils and protein droplets. Here, the authors identify reversible amyloid cores from the LC of hnRNPA1, based on which they elucidate the structural basis of reversible fibrillatio
Externí odkaz:
https://doaj.org/article/a160475f7cbf47d1b2ddb73a38f8b907
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
Autor:
Minglei Zhao, Jianhua He, Lin Jiang, Xueming Li, Zhenheng Qin, Muyun Xie, Bo Sun, Woo Shik Shin, Zhenying Liu, Jinge Gu, Xinrui Gui, Kun Zhao, Heng Zhou, Bin Dai, Dan Li, Yang Li, Cong Liu, Lin He, Feng Luo
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Subcellular membrane-less organelles consist of proteins with low complexity domains. Many of them, such as hnRNPA1, can assemble into both a polydisperse liquid phase and an ordered solid phase of amyloid fibril. The former mirrors biological granul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9965c8533765fd5283d03fc717317810
https://doaj.org/article/a160475f7cbf47d1b2ddb73a38f8b907
https://doaj.org/article/a160475f7cbf47d1b2ddb73a38f8b907
Autor:
Bo Sun, Muyun Xie, Pei Huang, Jianhua He, Minjun Li, Zhijun Wang, Gang Zuo, Feng Yu, Haojie Guo, Huan Zhou, Qisheng Wang, Chunyan Xu, Qin Xu
Publikováno v:
The Biochemical journal. 473(23)
TleD is a SAM (S-adenosyl-l-methionine)-dependent methyltransferase and acts as one of the key enzymes in the teleocidin B biosynthesis pathway. Besides methyl transferring, TleD also rearranges the geranyl and indole moieties of the precursor to for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6980781b6d9bed68b2dad46c42aad4e2
https://pubmed.ncbi.nlm.nih.gov/27613858
https://pubmed.ncbi.nlm.nih.gov/27613858
Publikováno v:
The Journal of Physical Chemistry B. 116:2927-2933
Our previous study has shown that the self-assembly of several neurodegenerative-disease-related peptides in ambient water nanofilm condensed on mica is very sensitive to the amount of water on the surface. In this paper, we will demonstrate our hypo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09d6af2565bb5ec2cd685cf243a76ace
https://doi.org/10.1021/jp2089438
https://doi.org/10.1021/jp2089438
Publikováno v:
The Journal of Physical Chemistry B. 114:15759-15765
An ambient water nanofilm condensed on a solid surface provides a good model system to study the self-assembling behaviors of peptides in a confined environment. In this paper, the self-assembly of three short amyloid-related peptides in a water nano
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ce8627e236152a85373016ee37a0b6b
https://doi.org/10.1021/jp105501x
https://doi.org/10.1021/jp105501x
Autor:
Feng Zhang, Bo Zhou, Jun Hu, Sheng-fu Chen, Ming Ye, Haiping Fang, Yi Zhang, Yu-Zhao Tang, Muyun Xie, Haijun Yang, Hai Li, Jianhua He
Publikováno v:
The journal of physical chemistry. B. 113(26)
Ambient water nanofilms confined on solid surfaces usually show properties not seen in bulk and play unique roles in many important processes. Here we report diffusion and self-assembly of peptides in ambient water nanofilms on mica, based on "drying
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dca8a2e259b8e5640784cc5f984cac71
https://pubmed.ncbi.nlm.nih.gov/19496603
https://pubmed.ncbi.nlm.nih.gov/19496603
Autor:
Feng Yu, Minjun Li, Chunyan Xu, Bo Sun, Huan Zhou, Zhijun Wang, Qin Xu, Muyun Xie, Gang Zuo, Pei Huang, Haojie Guo, Qisheng Wang, Jianhua He
Publikováno v:
Biochemical Journal; Dec2016, Vol. 473 Issue 23, p4385-4397, 13p