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  1. Article ; Online: Design, synthesis, and activity evaluation of novel multitargeted l-tryptophan derivatives with powerful antioxidant activity against Alzheimer's disease.

    Zeng, Xianghao / Cheng, Shaobing / Li, Huilan / Yu, Haiyang / Cui, Yushun / Fang, Yuanying / Yang, Shilin / Feng, Yulin

    Archiv der Pharmazie

    2024  Volume 357, Issue 5, Page(s) e2300603

    Abstract: Alzheimer's disease (AD) is a multifactorial neurological disease, and the multitarget directed ligand (MTDL) strategy may be an effective approach to delay its progression. Based on this strategy, 27 derivatives of l-tryptophan, 3a-1-3d-1, were designed, ...

    Abstract Alzheimer's disease (AD) is a multifactorial neurological disease, and the multitarget directed ligand (MTDL) strategy may be an effective approach to delay its progression. Based on this strategy, 27 derivatives of l-tryptophan, 3a-1-3d-1, were designed, synthesized, and evaluated for their biological activity. Among them, IC
    MeSH term(s) Alzheimer Disease/drug therapy ; Humans ; Antioxidants/pharmacology ; Antioxidants/chemical synthesis ; Antioxidants/chemistry ; Drug Design ; Cholinesterase Inhibitors/pharmacology ; Cholinesterase Inhibitors/chemical synthesis ; Cholinesterase Inhibitors/chemistry ; Structure-Activity Relationship ; Blood-Brain Barrier/metabolism ; Butyrylcholinesterase/metabolism ; Animals ; Tryptophan/pharmacology ; Tryptophan/chemistry ; Tryptophan/analogs & derivatives ; Tryptophan/chemical synthesis ; Amyloid beta-Peptides/antagonists & inhibitors ; Amyloid beta-Peptides/metabolism ; Rats ; Acetylcholinesterase/metabolism ; Molecular Structure ; PC12 Cells ; Dose-Response Relationship, Drug ; Models, Molecular
    Chemical Substances Antioxidants ; Cholinesterase Inhibitors ; Butyrylcholinesterase (EC 3.1.1.8) ; Tryptophan (8DUH1N11BX) ; Amyloid beta-Peptides ; Acetylcholinesterase (EC 3.1.1.7)
    Language English
    Publishing date 2024-01-30
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 6381-2
    ISSN 1521-4184 ; 0365-6233 ; 1437-1014
    ISSN (online) 1521-4184
    ISSN 0365-6233 ; 1437-1014
    DOI 10.1002/ardp.202300603
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  2. Article ; Online: Synthesis and Neuroprotective Evaluation of Substituted Indanone/Benzofuranone and Piperidine Hybrids.

    Zeng, Qing / Zhang, Ziwei / Cai, Zhifang / Hu, Pei / Yang, Zunhua / Wan, Yang / Li, Huilan / Xiong, Jian / Feng, Yulin / Fang, Yuanying

    ACS chemical neuroscience

    2024  Volume 15, Issue 10, Page(s) 2042–2057

    Abstract: Based on the neuroprotection of butylphthalide and donepezil, a series of indanone/benzofuranone and piperidine hybrids were designed and synthesized for assessment of their neuroprotective activities, aiming to enhance the bioavailability and ... ...

    Abstract Based on the neuroprotection of butylphthalide and donepezil, a series of indanone/benzofuranone and piperidine hybrids were designed and synthesized for assessment of their neuroprotective activities, aiming to enhance the bioavailability and therapeutic efficacy of natural phthalide analogues. Within this study, it was observed that most indanone derivatives bearing 1-methylpiperidine in the tail segment demonstrated superior neuroprotective effects on the oxygen glucose deprivation/reperfusion (OGD/R)-induced rat primary neuronal cell injury model in vitro compared to benzofuranone compounds. Among the synthesized compounds, 11 (
    MeSH term(s) Animals ; Neuroprotective Agents/pharmacology ; Neuroprotective Agents/chemical synthesis ; Piperidines/pharmacology ; Piperidines/chemical synthesis ; Piperidines/chemistry ; Indans/pharmacology ; Indans/chemical synthesis ; Indans/chemistry ; Benzofurans/pharmacology ; Benzofurans/chemical synthesis ; Rats ; Rats, Sprague-Dawley ; Reperfusion Injury/drug therapy ; Neurons/drug effects ; Neurons/metabolism ; Male ; Cell Survival/drug effects ; Blood-Brain Barrier/drug effects ; Blood-Brain Barrier/metabolism ; Infarction, Middle Cerebral Artery/drug therapy
    Language English
    Publishing date 2024-04-24
    Publishing country United States
    Document type Journal Article
    ISSN 1948-7193
    ISSN (online) 1948-7193
    DOI 10.1021/acschemneuro.4c00054
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  3. Article ; Online: Discovery of Selective Proteolysis-Targeting Chimera Degraders Targeting PTP1B as Long-Term Hypoglycemic Agents.

    Yang, Zunhua / Ying, Yuqi / Cheng, Shaobing / Wu, Jiamin / Zhang, Ziwei / Hu, Pei / Xiong, Jian / Li, Huilan / Zeng, Qing / Cai, Zhifang / Feng, Yulin / Fang, Yuanying

    Journal of medicinal chemistry

    2024  Volume 67, Issue 9, Page(s) 7569–7584

    Abstract: PTP1B, a promising target for insulin sensitizers in type 2 diabetes treatment, can be effectively degraded using proteolysis-targeting chimera (PROTAC). This approach offers potential for long-acting antidiabetic agents. We report potent bifunctional ... ...

    Abstract PTP1B, a promising target for insulin sensitizers in type 2 diabetes treatment, can be effectively degraded using proteolysis-targeting chimera (PROTAC). This approach offers potential for long-acting antidiabetic agents. We report potent bifunctional PROTACs targeting PTP1B through the E3 ubiquitin ligase cereblon. Western blot analysis showed significant PTP1B degradation by PROTACs at concentrations from 5 nM to 5 μM after 48 h. Evaluation of five highly potent PROTACs revealed compound
    MeSH term(s) Animals ; Humans ; Mice ; Adaptor Proteins, Signal Transducing/metabolism ; Drug Discovery ; Hep G2 Cells ; Hypoglycemic Agents/pharmacology ; Hypoglycemic Agents/chemistry ; Hypoglycemic Agents/chemical synthesis ; Protein Tyrosine Phosphatase, Non-Receptor Type 1/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 1/antagonists & inhibitors ; Proteolysis/drug effects ; Signal Transduction/drug effects ; Ubiquitin-Protein Ligases/metabolism
    Language English
    Publishing date 2024-05-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.4c00356
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  4. Article ; Online: Rapid Formation of Intramolecular Disulfide Bridges using Light: An Efficient Method to Control the Conformation and Function of Bioactive Peptides.

    He, Feng / Chai, Yu / Zeng, Zizhen / Lu, Fangling / Chen, Huanwen / Zhu, Jinhua / Fang, Yuanying / Cheng, Keguang / Miclet, Emeric / Alezra, Valérie / Wan, Yang

    Journal of the American Chemical Society

    2023  Volume 145, Issue 41, Page(s) 22639–22648

    Abstract: Disulfide bonds are widely found in natural peptides and play a pivotal role in stabilizing their secondary structures, which are highly associated with their biological functions. Herein, we introduce a light-mediated strategy to effectively control the ...

    Abstract Disulfide bonds are widely found in natural peptides and play a pivotal role in stabilizing their secondary structures, which are highly associated with their biological functions. Herein, we introduce a light-mediated strategy to effectively control the formation of disulfides. Our strategy is based on 2-nitroveratryl (
    MeSH term(s) Disulfides/chemistry ; Protein Structure, Secondary ; Sulfhydryl Compounds/chemistry
    Chemical Substances Disulfides ; Sulfhydryl Compounds
    Language English
    Publishing date 2023-10-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c07795
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  5. Article ; Online: Photobiocatalytic Decarboxylation for the Synthesis of Fatty Epoxides from Renewable Fatty Acids.

    Ge, Ran / Zhang, Pengpeng / Dong, Xuetian / Li, Yuanying / Sun, Zhoutong / Zeng, Yongyi / Chen, Bishuang / Zhang, Wuyuan

    ChemSusChem

    2022  Volume 15, Issue 20, Page(s) e202201275

    Abstract: Fatty epoxides are unique building blocks in organic transformations and materials production; however, their synthetic methodologies are currently not accessible from renewable fatty acids. Herein, a photoenzymatic decarboxylation of epoxy fatty acids ... ...

    Abstract Fatty epoxides are unique building blocks in organic transformations and materials production; however, their synthetic methodologies are currently not accessible from renewable fatty acids. Herein, a photoenzymatic decarboxylation of epoxy fatty acids into fatty epoxides was demonstrated using fatty acid photodecarboxylase (FAP) from Chlorella variabilis NC64A (CvFAP). Various fatty epoxides were synthesized in excellent selectivity by wild-type CvFAP. The decarboxylation reaction was also achieved with four new FAP homologues, potentially suggesting a broad availability of the biocatalysts for this challenging decarboxylation reaction. By combining CvFAP with lipase and peroxygenase, a multienzymatic cascade to transform oleic acid and its triglyceride into the corresponding fatty epoxides was established. The obtained fatty epoxides were further converted into rather unusual fatty compounds including diol, alcohol, ether, and chain-shortened carboxylic acids. The present photobiocatalytic synthesis of fatty epoxides from natural starting materials excels by its intrinsic selectivity, mild conditions, and independence of nicotinamide cofactors.
    MeSH term(s) Fatty Acids ; Epoxy Compounds ; Decarboxylation ; Chlorella ; Carboxylic Acids ; Alcohols ; Triglycerides ; Lipase ; Niacinamide ; Oleic Acids
    Chemical Substances Fatty Acids ; Epoxy Compounds ; Carboxylic Acids ; Alcohols ; Triglycerides ; Lipase (EC 3.1.1.3) ; Niacinamide (25X51I8RD4) ; Oleic Acids
    Language English
    Publishing date 2022-09-15
    Publishing country Germany
    Document type Journal Article
    ISSN 1864-564X
    ISSN (online) 1864-564X
    DOI 10.1002/cssc.202201275
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  6. Article ; Online: Dexmedetomidine relieves inflammatory pain by enhancing GABAergic synaptic activity in pyramidal neurons of the anterior cingulate cortex.

    Liu, Ling / Luo, Zhihao / Mai, Yuanying / Lu, Yi / Sun, Zhaoxia / Chen, Jianfeng / Zeng, Tianyu / Chen, Lei / Liu, Zihao / Yang, Hanyu / Xu, Qin / Lan, Lan / Tang, Chunzhi

    Neuropharmacology

    2023  Volume 240, Page(s) 109710

    Abstract: Pyramidal neuron (Pyn) hyperactivity in the anterior cingulate cortex (ACC) is involved in the modulation of pain. Previous studies indicate that the activation of α2 adrenoceptors (α2-ARs) by dexmedetomidine (DEX) is a safe and effective means of ... ...

    Abstract Pyramidal neuron (Pyn) hyperactivity in the anterior cingulate cortex (ACC) is involved in the modulation of pain. Previous studies indicate that the activation of α2 adrenoceptors (α2-ARs) by dexmedetomidine (DEX) is a safe and effective means of alleviating multiple types of pain. Here, we showed that systemically administered DEX can ameliorate the inflammatory pain induced by hindpaw injection of formalin (FA) and further examined the molecular and synaptic mechanisms of this DEX-elicited antinociceptive effect. We found that FA caused an increase in c-Fos expression in contralateral layer 2/3 (L2/3) ACC, and that intra-ACC infusion of DEX could also relieve phase 2 inflammatory pain behavior. DEX elicited an increase in the amplitude and frequency of miniature inhibitory post-synaptic currents (mIPSCs) and evoked IPSC amplitude, as well as a reduction in the hyperexcitability and both paired-pulse and excitation/inhibition ratios in contralateral L2/3 ACC Pyns of FA mice. These electrophysiological effects were associated with the upregulation of GABA A receptor (GABA
    Language English
    Publishing date 2023-09-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 218272-5
    ISSN 1873-7064 ; 0028-3908
    ISSN (online) 1873-7064
    ISSN 0028-3908
    DOI 10.1016/j.neuropharm.2023.109710
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  7. Article ; Online: Polymyxin B-inspired non-hemolytic tyrocidine A analogues with significantly enhanced activity against gram-negative bacteria: How cationicity impacts cell specificity and antibacterial mechanism.

    Zhu, Jibao / Hu, Chengfei / Zeng, Zizhen / Deng, Xiaoyu / Zeng, Lingbing / Xie, Saisai / Fang, Yuanying / Jin, Yi / Alezra, Valérie / Wan, Yang

    European journal of medicinal chemistry

    2021  Volume 221, Page(s) 113488

    Abstract: Naturally occurring cyclic antimicrobial peptides (AMPs) such as tyrocidine A (Tyrc A) and gramicidin S (GS) are appealing targets for the development of novel antibiotics. However, their therapeutic potentials are limited by undesired hemolytic activity ...

    Abstract Naturally occurring cyclic antimicrobial peptides (AMPs) such as tyrocidine A (Tyrc A) and gramicidin S (GS) are appealing targets for the development of novel antibiotics. However, their therapeutic potentials are limited by undesired hemolytic activity and relatively poor activity against Gram-negative bacteria. Inspired by polycationic lipopeptide polymyxin B (PMB), the so called 'last-resort' antibiotic for the treatment of infections caused by multidrug-resistant Gram-negative bacteria, we synthesized and biologically evaluated a series of polycationic analogues derived from Tyrc A. We were able to obtain peptide 8 that possesses 5 positive charges exhibiting potent activities against both Gram-negative and Gram-positive bacteria along with totally diminished hemolytic activity. Intriguingly, antibacterial mechanism studies revealed that, rather than the 'pore forming' model that possessed by Tyrc A, peptide 8 likely diffuses membrane in a 'detergent-like' manner. Furthermore, when treating mice with peritonitis-sepsis, peptide 8 showed excellent antibacterial and anti-inflammatory activities in vivo.
    MeSH term(s) Anti-Bacterial Agents/chemical synthesis ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Cell Line ; Dose-Response Relationship, Drug ; Drug Resistance, Bacterial/drug effects ; Escherichia coli/drug effects ; Humans ; Microbial Sensitivity Tests ; Molecular Structure ; Polymyxin B/chemistry ; Polymyxin B/pharmacology ; Staphylococcus aureus/drug effects ; Structure-Activity Relationship ; Tyrocidine/chemical synthesis ; Tyrocidine/chemistry ; Tyrocidine/pharmacology
    Chemical Substances Anti-Bacterial Agents ; Tyrocidine ; Polymyxin B (J2VZ07J96K)
    Language English
    Publishing date 2021-05-01
    Publishing country France
    Document type Journal Article
    ZDB-ID 188597-2
    ISSN 1768-3254 ; 0009-4374 ; 0223-5234
    ISSN (online) 1768-3254
    ISSN 0009-4374 ; 0223-5234
    DOI 10.1016/j.ejmech.2021.113488
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  8. Article ; Online: Phenanthraquinone-Doped Polymethyl Methacrylate Photopolymer for Holographic Recording.

    Li, Jinhong / Hu, Po / Zeng, Zeyi / Jin, Junchao / Wu, Junhui / Chen, Xi / Liu, Jie / Li, Qingdong / Chen, Mingyong / Zhang, Zuoyu / Zhang, Yuanying / Lin, Xiao / Tan, Xiaodi

    Molecules (Basel, Switzerland)

    2022  Volume 27, Issue 19

    Abstract: Phenanthraquinone-doped polymethyl methacrylate (PQ/PMMA) photopolymers are considered to be the most promising holographic storage media due to their unique properties, such as high stability, a simple preparation process, low price, and volumetric ... ...

    Abstract Phenanthraquinone-doped polymethyl methacrylate (PQ/PMMA) photopolymers are considered to be the most promising holographic storage media due to their unique properties, such as high stability, a simple preparation process, low price, and volumetric shrinkage. This paper reviews the development process of PQ/PMMA photopolymers from inception to the present, summarizes the process, and looks at the development potential of PQ/PMMA in practical applications.
    MeSH term(s) Holography ; Polymethyl Methacrylate
    Chemical Substances Polymethyl Methacrylate (9011-14-7)
    Language English
    Publishing date 2022-09-23
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules27196283
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  9. Article ; Online: The deubiquitinase USP10 restores PTEN activity and inhibits non-small cell lung cancer cell proliferation.

    He, Yuanming / Jiang, Shuoyi / Mao, Chenyu / Zheng, Hui / Cao, Biyin / Zhang, Zubin / Zhao, Jun / Zeng, Yuanying / Mao, Xinliang

    The Journal of biological chemistry

    2021  Volume 297, Issue 3, Page(s) 101088

    Abstract: The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) protein is a key player in tumorigenesis of non-small cell lung cancer (NSCLC) and was recently found to be inactivated by tripartite motif containing 25 (TRIM25)-mediated K63-linked ... ...

    Abstract The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) protein is a key player in tumorigenesis of non-small cell lung cancer (NSCLC) and was recently found to be inactivated by tripartite motif containing 25 (TRIM25)-mediated K63-linked polyubiquitination. However, the deubiquitinase (Dub) coordinate TRIM25 in PTEN ubiquitination is still elusive. In the present study, we found that this K63-linked polyubiquitination could be ablated by the ubiquitin-specific protease 10 (USP10) in a screen against a panel of Dubs. We found using coimmununoprecipitation/immunoblotting that USP10 interacted with PTEN and reduced the K63-linked polyubiquitination of PTEN mediated by TRIM25 in NSCLC cells. Moreover, USP10, but not its inactive C424A deubiquitinating mutant or other Dubs, abolished PTEN from K63-linked polyubiquitination mediated by TRIM25. In contrast to TRIM25, USP10 restored PTEN phosphatase activity and reduced the production of the secondary messenger phosphatidylinositol-3,4,5-trisphosphate, thereby inhibiting AKT/mammalian target of rapamycin progrowth signaling transduction in NSCLC cells. Moreover, USP10 was downregulated in NSCLC cell lines and primary tissues, whereas TRIM25 was upregulated. Consistent with its molecular activity, re-expression of USP10 suppressed NSCLC cell proliferation and migration, whereas knockout of USP10 promoted NSCLC cell proliferation and migration. In conclusion, the present study demonstrates that USP10 coordinates TRIM25 to modulate PTEN activity. Specifically, USP10 activates PTEN by preventing its K63-linked polyubiquitination mediated by TRIM25 and suppresses the AKT/mammalian target of rapamycin signaling pathway, thereby inhibiting NSCLC proliferation, indicating that it may be a potential drug target for cancer treatment.
    MeSH term(s) Adult ; Carcinoma, Non-Small-Cell Lung/metabolism ; Carcinoma, Non-Small-Cell Lung/physiopathology ; Cell Line, Tumor ; Cell Movement/genetics ; Cell Proliferation/genetics ; Deubiquitinating Enzymes/metabolism ; Female ; Gene Expression/genetics ; Gene Expression Regulation, Neoplastic/genetics ; Humans ; Lung Neoplasms/pathology ; Male ; Middle Aged ; PTEN Phosphohydrolase/metabolism ; Signal Transduction/genetics ; Transcription Factors/metabolism ; Tripartite Motif Proteins/metabolism ; Ubiquitin Thiolesterase/genetics ; Ubiquitin Thiolesterase/metabolism ; Ubiquitin Thiolesterase/physiology ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
    Chemical Substances Transcription Factors ; Tripartite Motif Proteins ; USP10 protein, human ; TRIM25 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; PTEN Phosphohydrolase (EC 3.1.3.67) ; PTEN protein, human (EC 3.1.3.67) ; Deubiquitinating Enzymes (EC 3.4.19.12) ; Ubiquitin Thiolesterase (EC 3.4.19.12)
    Language English
    Publishing date 2021-08-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2021.101088
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  10. Article ; Online: COVID-19 with cystic features on computed tomography ; A case report

    Liu, Kefu / Zeng, Yuanying / Xie, Ping / Ye, Xun / Xu, Guidong / Liu, Jian / Wang, Hao / Qian, Jinxian

    Medicine

    2020  Volume 99, Issue 18, Page(s) e20175

    Keywords General Medicine ; covid19
    Language English
    Publisher Ovid Technologies (Wolters Kluwer Health)
    Publishing country us
    Document type Article ; Online
    ZDB-ID 80184-7
    ISSN 1536-5964 ; 0025-7974
    ISSN (online) 1536-5964
    ISSN 0025-7974
    DOI 10.1097/md.0000000000020175
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