7 results on '"Liu, Maili"'
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2. An auxiliary binding interface of SHIP2-SH2 for Y292-phosphorylated FcγRIIB reveals diverse recognition mechanisms for tyrosine-phosphorylated receptors involved in different cell signaling pathways
- Author
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Wang, Zi, Zhou, Heng, Yue, Xiali, Zhu, Jiang, Yang, Yunhuang, and Liu, Maili
- Published
- 2022
- Full Text
- View/download PDF
3. Enhancing protein dynamics analysis with hydrophilic polyethylene glycol cross-linkers.
- Author
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Sun, Min, Chen, Jing, Zhao, Chang, Zhang, Lihua, Liu, Maili, Zhang, Yukui, Zhao, Qun, and Gong, Zhou
- Subjects
POLYETHYLENE glycol ,PROTEIN analysis ,MASS spectrometry ,MITOGEN-activated protein kinase phosphatases ,NUCLEAR magnetic resonance ,THERMODYNAMICS ,CALMODULIN - Abstract
Cross-linkers play a critical role in capturing protein dynamics in chemical cross-linking mass spectrometry techniques. Various types of cross-linkers with different backbone features are widely used in the study of proteins. However, it is still not clear how the cross-linkers' backbone affect their own structure and their interactions with proteins. In this study, we systematically characterized and compared methylene backbone and polyethylene glycol (PEG) backbone cross-linkers in terms of capturing protein structure and dynamics. The results indicate the cross-linker with PEG backbone have a better ability to capture the inter-domain dynamics of calmodulin, adenylate kinase, maltodextrin binding protein and dual-specificity protein phosphatase. We further conducted quantum chemical calculations and all-atom molecular dynamics simulations to analyze thermodynamic and kinetic properties of PEG backbone and methylene backbone cross-linkers. Solution nuclear magnetic resonance was employed to validate the interaction interface between proteins and cross-linkers. Our findings suggest that the polarity distribution of PEG backbone enhances the accessibility of the cross-linker to the protein surface, facilitating the capture of sites located in dynamic regions. By comprehensively benchmarking with disuccinimidyl suberate (DSS)/bis-sulfosuccinimidyl-suberate(BS3), bis-succinimidyl-(PEG)
2 revealed superior advantages in protein dynamic conformation analysis in vitro and in vivo , enabling the capture of a greater number of cross-linking sites and better modeling of protein dynamics. Furthermore, our study provides valuable guidance for the development and application of PEG backbone cross-linkers. [ABSTRACT FROM AUTHOR]- Published
- 2024
- Full Text
- View/download PDF
4. Structural Insights into the Binding Propensity of Human SHIP2 SH2 to Oncogenic CagA Isoforms from Helicobacter pylori.
- Author
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Wang, Zi, Shan, Yubao, Wang, Ru, Zhou, Heng, Hu, Rui, Li, Ying, Zhu, Jiang, Yang, Yunhuang, and Liu, Maili
- Subjects
HELICOBACTER pylori ,PEPTIDES ,NUCLEAR magnetic resonance spectroscopy ,CELL communication ,CELL membranes ,PHOSPHOTYROSINE - Abstract
SHIP2 is a multi-domain inositol 5-phosphatase binding to a variety of phosphotyrosine (pY)-containing proteins through its SH2 domain, so as to regulate various cell signaling pathways by modulating the phosphatidylinositol level in the plasma membrane. Unfavorably, Helicobacter pylori can hijack SHIP2 through the CagA protein to induce gastric cell carcinogenesis. To date, the interaction between SHIP2 and CagA was not analyzed from a structural point of view. Here, the binding of SHIP2-SH2 with Tyr-phosphorylated peptides from four EPIYA motifs (A/B/C/D) in CagA was studied using NMR spectroscopy. The results showed that EPIYA-C and -D bind to a similar interface of SHIP2-SH2, including a pY-binding pocket and a hydrophobic pocket, to achieve high affinity, while EPIYA-A and -B bind to a smaller interface of SHIP2-SH2 with weak affinity. By summarizing the interface and affinity of SHIP2-SH2 for CagA EPIYA-A/B/C/D, c-MET and FcgR2B ITIM, it was proposed that, potentially, SHIP2-SH2 has a selective preference for L > I > V for the aliphatic residues at the pY+3 position in its ligand. This study reveals the rule of the ligand sequence bound by SHIP2-SH2 and the mechanism by which CagA protein hijacks SHIP2, which will help design a peptide inhibitor against SHIP2-SH2. [ABSTRACT FROM AUTHOR]
- Published
- 2022
- Full Text
- View/download PDF
5. NMR Reveals the Conformational Changes of Cytochrome C upon Interaction with Cardiolipin.
- Author
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Zhan, Jianhua, Zhang, Guangqing, Chai, Xin, Zhu, Qinjun, Sun, Peng, Jiang, Bin, Zhou, Xin, Zhang, Xu, and Liu, Maili
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CARDIOLIPIN ,CYTOCHROME c ,NUCLEAR magnetic resonance spectroscopy ,PEROXIDASE ,HEME ,PROTEINS - Abstract
Conformational change of cytochrome c (cyt c) caused by interaction with cardiolipin (CL) is an important step during apoptosis, but the underlying mechanism is controversial. To comprehensively clarify the structural transformations of cyt c upon interaction with CL and avoid the unpredictable alias that might come from protein labeling or mutations, the conformation of purified yeast iso–1 cyt c with natural isotopic abundance in different contents of CL was measured by using NMR spectroscopy, in which the trimethylated group of the protein was used as a natural probe. The data demonstrate that cyt c has two partially unfolded conformations when interacted with CL: one with Fe–His33 coordination and the other with a penta–coordination heme. The Fe–His33 coordination conformation can be converted into a penta–coordination heme conformation in high content of CL. The structure of cyt c becomes partially unfolded with more exposed heme upon interaction with CL, suggesting that cyt c prefers a high peroxidase activity state in the mitochondria, which, in turn, makes CL easy to be oxidized, and causes the release of cyt c into the cytoplasm as a trigger in apoptosis. [ABSTRACT FROM AUTHOR]
- Published
- 2021
- Full Text
- View/download PDF
6. Combined NMR and MS-based metabonomics and real-time PCR analyses reveal dynamic metabolic changes of Ganoderma lucidum during fruiting body growing.
- Author
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Liu, Caixiang, Chen, Fangfang, Fan, Xinyu, Liu, Biao, Chai, Xin, He, Sipei, Huang, Tao, Wang, Xiaohua, Liu, Laixing, Liu, Huili, Zeng, Danyun, Jiang, Bin, Zhang, Xu, and Liu, Maili
- Subjects
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GANODERMA lucidum , *FRUITING bodies (Fungi) , *FRUIT growing , *BUD development , *NUCLEAR magnetic resonance - Abstract
[Display omitted] • Over 40 metabolites were detected in G. lucidum extracts. Notably, we identified previously unreported metabolites. • Most metabolite contents increased rapidly from period I to II. Following this, they decreased until reaching period VII. • The optimal time to harvest G. lucidum is during period IV. • Cytochrome P450 genes GlCYP1 , GlCYP3 , GlCYP5 , GlCYP6 and GlCYP13 may have critical roles in the biosynthesis of GAs. Ganoderma lucidum (G. lucidum) is a rare medicinal fungus with various beneficial properties. One of its main components, ganoderic acids (GAs), are important triterpenoids known for their sedative and analgesic, hepatoprotective, and anti-tumor activities. Understanding the growth and development of the G. lucidum fruiting body is crucial for determining the optimal time to harvest them. In this study, we used nuclear magnetic resonance (NMR) spectroscopy to systematically characterize the metabolites of G. lucidum at seven distinct developmental stages. We also measured the contents of seven kinds of GAs using LC-MS/MS. A total of 49 metabolites were detected in G. lucidum , including amino acids, sugars, organic acids and GAs. During the transition from the bud development period (I) to the budding period (II), we observed a rapid accumulation of glucose, tyrosine, nicotinamide ribotide, inosine and GAs. After the budding period, the contents of most metabolites decreased until the mature period (VII). In addition, the contents of GAs showed an initial raising, followed by a decline during the elongation period, except for GAF, which exhibited a rapid raise during the mature stage. We also detected the expression of several genes involved in GA synthesis, finding that most genes including 16 cytochrome P450 monooxygenase were all down-regulated during periods IV and VII compared to period I. These findings provide valuable insights into the dynamic metabolic profiles of G. lucidum throughout its growth stage, and it is recommended to harvest G. lucidum at period IV. [ABSTRACT FROM AUTHOR]
- Published
- 2024
- Full Text
- View/download PDF
7. Combination of peak-picking and binning for NMR-based untargeted metabonomics study.
- Author
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Chai, Xin, Liu, Caixiang, Fan, Xinyu, Huang, Tao, Zhang, Xu, Jiang, Bin, and Liu, Maili
- Subjects
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MULTIVARIATE analysis , *LATENT structure analysis , *PRINCIPAL components analysis , *ORTHOGRAPHIC projection , *GANODERMA lucidum , *BIN packing problem - Abstract
[Display omitted] • The method is the combination of peak-picking and binning for NMR based untargeted metabonomics studies. • The method takes peak top as bin center. • The method improves the following PCA and OPLS-DA analysis. In NMR-based untargeted metabolomic studies, 1H NMR spectra are usually divided into equal bins/buckets to diminish the effects of peak shift caused by sample status or instrument instability, and to reduce the number of variables used as input for the multivariate statistical analysis. It was noticed that the peaks near bin boundaries may cause significant changes in integral values of adjacent bins, and the weaker peak may be obscured if it is allocated in the same bin with intense peaks. Several efforts have been taken to improve the performance of binning. Here we propose an alternative method, named P-Bin, based on the combination of the classic peak-picking and binning procedures. The location of each peak defined by peak-picking is used as the center of the individual bin. P-Bin is expected to keep all spectral information associated with the peaks and significantly reduce the data size as the spectral regions without peaks are not considered. In addition, both peak-picking and binning are routine procedures, making P-Bin easy to be implemented. To verify the performance, two sets of experimental data from human plasma and Ganoderma lucidum (G. lucidum) extracts were processed using the conventional binning method and the proposed method, before the principal component analysis (PCA) and the orthogonal projection to latent structures discriminant analysis (OPLS-DA). The results indicate that the proposed method has improved both the clustering performance of PCA score plots and the interpretability of OPLS-DA loading plots, and P-Bin could be an improved version of data preparation for metabonomic study. [ABSTRACT FROM AUTHOR]
- Published
- 2023
- Full Text
- View/download PDF
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