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129 results on '"Yu, Guimei"'

4. An IgM-like inhalable ACE2 fusion protein broadly neutralizes SARS-CoV-2 variants

Author

Liu, Juan, Mao, Fengfeng, Chen, Jianhe, Lu, Shuaiyao, Qi, Yonghe, Sun, Yinyan, Fang, Linqiang, Yeung, Man Lung, Liu, Chunmei, Yu, Guimei, Li, Guangyu, Liu, Ximing, Yao, Yuansheng, Huang, Panpan, Hao, Dongxia, Liu, Zibing, Ding, Yu, Liu, Haimo, Yang, Fang, Chen, Pan, Sa, Rigai, Sheng, Yao, Tian, Xinxin, Peng, Ran, Li, Xue, Luo, Junmian, Cheng, Yurui, Zheng, Yule, Lin, Yongqing, Song, Rui, Jin, Ronghua, Huang, Baoying, Choe, Hyeryun, Farzan, Michael, Yuen, Kwok-Yung, Tan, Wenjie, Peng, Xiaozhong, Sui, Jianhua, and Li, Wenhui

Published
2023
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12. Inhibitory mechanism of CRISPR-Cas9 by AcrIIC4

Author

Li, Xuzichao, primary, Liao, Fumeng, additional, Gao, Jiaqi, additional, Song, Guangyong, additional, Zhang, Chendi, additional, Ji, Nan, additional, Wang, Xiaoshen, additional, Wen, Jing, additional, He, Jia, additional, Wei, Yong, additional, Zhang, Heng, additional, Li, Zhuang, additional, Yu, Guimei, additional, and Yin, Hang, additional

Published
2023
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18. PTP4A2 promotes lysophagy by dephosphorylation of VCP/p97 at Tyr805

Author

Bai, Yunpeng, primary, Yu, Guimei, additional, Zhou, Hong-Ming, additional, Amarasinghe, Ovini, additional, Zhou, Yuan, additional, Zhu, Peipei, additional, Li, Qinglin, additional, Zhang, Lujuan, additional, Nguele Meke, Frederick, additional, Miao, Yiming, additional, Chapman, Eli, additional, Tao, W. Andy, additional, and Zhang, Zhong-Yin, additional

Published
2022
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20. An IgM-like Inhalable ACE2 fusion protein broadly neutralizes SARS-CoV-2

Author

Li, Wenhui, primary, Liu, Juan, additional, Mao, Fengfeng, additional, Chen, Jianhe, additional, Lu, Shuaiyao, additional, Qi, Yonghe, additional, Sun, Yinyan, additional, Fang, Linqiang, additional, Yeung, Man Lung, additional, Liu, Chunmei, additional, Yu, Guimei, additional, Li, Guangyu, additional, Liu, Ximing, additional, Yao, Yuansheng, additional, Huang, Panpan, additional, Hao, Dongxia, additional, Liu, Zibing, additional, Ding, Yu, additional, Liu, Haimo, additional, Yang, Fang, additional, Chen, Pan, additional, Sa, Rigai, additional, Sheng, Yao, additional, Tian, Xinxin, additional, Peng, Ran, additional, Li, Xue, additional, Luo, Junmian, additional, Cheng, Yurui, additional, Zheng, Yule, additional, Lin, Yongqing, additional, Song, Rui, additional, Jin, Ronghua, additional, Huang, Baoying, additional, Choe, Hyeryun, additional, Farzan, Michael, additional, Yuen, Kwok-Yung, additional, Tan, Wenjie, additional, Peng, Xiaozhong, additional, and Sui, Jianhua, additional

Published
2022
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23. Structural insights into the viral proteins binding by TRIM7 reveal a general C-terminal glutamine recognition mechanism

Author

Liang, Xiao, primary, Xiao, Jun, additional, Li, Xuzichao, additional, Wen, Yanan, additional, Che, Xing, additional, Ma, Yongjian, additional, Zhang, Xingyan, additional, Zhang, Yi, additional, Jian, Deng, additional, Wang, Peihui, additional, Xuan, Chenghao, additional, Yu, Guimei, additional, Li, Long, additional, and Zhang, Heng, additional

Published
2022
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29. Structure of ArabidopsisSOQ1 lumenal region unveils C-terminal domain essential for negative regulation of photoprotective qH

Author

Yu, Guimei, Hao, Jingfang, Pan, Xiaowei, Shi, Lifang, Zhang, Yong, Wang, Jifeng, Fan, Hongcheng, Xiao, Yang, Yang, Fuquan, Lou, Jizhong, Chang, Wenrui, Malnoë, Alizée, and Li, Mei

Abstract

Non-photochemical quenching (NPQ) plays an important role for phototrophs in decreasing photo-oxidative damage. qH is a sustained form of NPQ and depends on the plastid lipocalin (LCNP). A thylakoid membrane-anchored protein SUPPRESSOR OF QUENCHING1 (SOQ1) prevents qH formation by inhibiting LCNP. SOQ1 suppresses qH with its lumen-located thioredoxin (Trx)-like and NHL domains. Here we report structural data, genetic modification and biochemical characterization of ArabidopsisSOQ1 lumenal domains. Our results show that the Trx-like and NHL domains are associated together, with the cysteine motif located at their interface. Residue E859, required for SOQ1 function, is pivotal for maintaining the Trx–NHL association. Importantly, the C-terminal region of SOQ1 forms an independent β-stranded domain that has structural homology to the N-terminal domain of bacterial disulfide bond protein D and is essential for negative regulation of qH. Furthermore, SOQ1 is susceptible to cleavage at the loops connecting the neighbouring lumenal domains both in vitro and in vivo, which could be a regulatory process for its suppression function of qH.

Published
2022
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32. Can rheumatoid arthritis ever cease to exist: a review of various therapeutic modalities to maintain drug-free remission?

Author

Liu, Di, Yuan, Na, Yu, Guimei, Song, Ge, and Chen, Yan

Subjects
Original Article
Abstract

Therapies for rheumatoid arthritis (RA) were mostly aimed at reducing the pain, stiffness and further progression of joint destruction. However, with the advent of biologic agents that act against specific inflammatory cytokines contributing to RA pathogenesis (treat-to-target strategy), the degree of remission achieved has been remarkably impressive. In particular, inhibition of tumor necrosis factor α (TNFα), interleukins-1 and -6 and receptor-activator of nuclear kappa B ligand by neutralizing antibodies in early diagnosed RA patients has resulted in lowering of disease activity to levels that enable them to function as in the pre-disease stage. There are other biologic approaches such as depletion of B cells and blocking T-cell co-stimulators that have been included successfully in RA therapy under the class of disease-modifying anti-rheumatic drugs (DMARD). Given the excellent clinical outcomes of biologic DMARDs when initiated early in RA, discontinuation or dose tapering is practised. Because biologic DMARDs are expensive and also known to make users vulnerable to viral infections, dose reduction and drug holiday are reasonable steps when sustained good clinical response has been achieved. Majority clinical studies have been done with TNF inhibitors and data suggest that sustained remission of RA is achieved in several multi-centric studies carried out worldwide. However, high flare rate and reappearance of disease has been reported in several cases. This review critically discusses response predictors of biologic DMARDs, the case for treatment relaxation, strategizing drug tapering considering patient eligibility and timing in light of available clinical practice guidelines of RA.

Published
2017

33. Affinity cryo-electron microscopy: Methods development and applications

Author

Yu, Guimei

Subjects
viruses, Biophysics, macromolecular substances, Microbiology, Molecular Biology
Abstract

Single particle cryo-electron microscopy (cryo-EM) is an emerging powerful tool for structural studies of macromolecular assemblies. Although less concentrated and smaller amounts of samples are required for single particle cryo-EM compared to X-ray crystallography, it remains challenging to study specimens that are low-abundance, low-yield, or short-lived. The recent development of affinity grid techniques holds great promise to tackle these challenging samples by combining the sample purification and freezing on TEM grids steps in cryo-EM grid preparation into a single step, revolutionize the grid preparation of cryo-EM, and extend single particle cryo-EM to a routine structural biology tool to characterize structures of a broad spectrum of macromolecules. In my PhD study, I have established a new design of the affinity cryo-EM approach, cryo-SPIEM that applies a traditional pathogen diagnosis tool Solid Phase Immune Electron Microscopy (SPIEM) to the single particle cryo-EM method, and also systematically explored the applications of affinity EM approaches and the potentials of affinity cryo-EM approaches for near-atomic single particle 3-D reconstruction. The cryo-SPIEM approach provides an alternative, largely simplified and easier to use affinity grid that directly works with most native macromolecular complexes with established antibodies, and enables cryo-EM studies of native samples directly from cell cultures. The application of the affinity cryo-EM approach for high-resolution cryo-EM has been demonstrated successfully by solving a 6.3 Å structure of Tulane virus using the polylysine-based affinity grid, and a 2.6 Å structure of Tulane virus using the antibody-based affinity grid with a sample of low concentrations that defies standard cryo-EM study. Moreover, we have applied the affinity grid technique to investigate the interaction between Tulane virus and its cellular receptor Histo-blood group antigens, which revealed the potential roles of HBGA receptors in mediating genome release.

Published
2016

45. Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies

Author

Yu, Guimei, primary, Vago, Frank, additional, Zhang, Dongsheng, additional, Snyder, Jonathan E., additional, Yan, Rui, additional, Zhang, Ci, additional, Benjamin, Christopher, additional, Jiang, Xi, additional, Kuhn, Richard J., additional, Serwer, Philip, additional, Thompson, David H., additional, and Jiang, Wen, additional

Published
2014
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47. Cryo-EM Structure of a Novel Calicivirus, Tulane Virus.

Author

Yu, Guimei, Zhang, Dongsheng, Guo, Fei, Tan, Ming, Jiang, Xi, Jiang, Wen, Yu, Guimei, Zhang, Dongsheng, Guo, Fei, Tan, Ming, Jiang, Xi, and Jiang, Wen

Abstract

Tulane virus (TV) is a newly isolated cultivatable calicivirus that infects juvenile rhesus macaques. Here we report a 6.3 Å resolution cryo-electron microscopy structure of the TV virion. The TV virion is about 400 Å in diameter and consists of a T = 3 icosahedral protein capsid enclosing the RNA genome. 180 copies of the major capsid protein VP1 (~57 KDa) are organized into two types of dimers A/B and C/C and form a thin, smooth shell studded with 90 dimeric protrusions. The overall capsid organization and the capsid protein fold of TV closely resemble that of other caliciviruses, especially of human Norwalk virus, the prototype human norovirus. These close structural similarities support TV as an attractive surrogate for the non-cultivatable human noroviruses. The most distinctive feature of TV is that its C/C dimers are in a highly flexible conformation with significantly reduced interactions between the shell (S) domain and the protruding (P) domain of VP1. A comparative structural analysis indicated that the P domains of TV C/C dimers were much more flexible than those of other caliciviruses. These observations, combined with previous studies on other caliciviruses, led us to hypothesize that the enhanced flexibility of C/C dimer P domains are likely required for efficient calicivirus-host cell interactions and the consequent uncoating and genome release. Residues in the S-P1 hinge between the S and P domain may play a critical role in the flexibility of P domains of C/C dimers.

Published
2013

50. Structural basis for the concerted antiphage activity in the SIR2-HerA system.

Author

Liao F, Yu G, Zhang C, Liu Z, Li X, He Q, Yin H, Liu X, Li Z, and Zhang H

Abstract

Recently, a novel two-gene bacterial defense system against phages, encoding a SIR2 NADase and a HerA ATPase/helicase, has been identified. However, the molecular mechanism of the bacterial SIR2-HerA immune system remains unclear. Here, we determine the cryo-EM structures of SIR2, HerA and their complex from Paenibacillus sp. 453MF in different functional states. The SIR2 proteins oligomerize into a dodecameric ring-shaped structure consisting of two layers of interlocked hexamers, in which each subunit exhibits an auto-inhibited conformation. Distinct from the canonical AAA+ proteins, HerA hexamer alone in this antiphage system adopts a split spiral arrangement, which is stabilized by a unique C-terminal extension. SIR2 and HerA proteins assemble into a ∼1.1 MDa torch-shaped complex to fight against phage infection. Importantly, disruption of the interactions between SIR2 and HerA largely abolishes the antiphage activity. Interestingly, binding alters the oligomer state of SIR2, switching from a dodecamer to a tetradecamer state. The formation of the SIR2-HerA binary complex activates NADase and nuclease activities in SIR2 and ATPase and helicase activities in HerA. Together, our study not only provides a structural basis for the functional communications between SIR2 and HerA proteins, but also unravels a novel concerted antiviral mechanism through NAD+ degradation, ATP hydrolysis, and DNA cleavage., (© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.)

Published
2024
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