ACS Chemical Neuroscience最新文献

{"title":"","authors":"Zhi-Hong Wen, Ya-Jen Chiu, San-Nan Yang, Bo-Lin Guo, Chien-Wei Feng, Jimmy Ming-Jung Chunag, Nan-Fu Chen and Wu-Fu Chen*, ","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 13","pages":"XXX-XXX 962–968"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.5c00087","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144521688","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"","authors":"Spencer R. Pierce, Allison L. Germann, Yu Zhou, Saumith L. Menon, Xinghan Gu, Christopher J. Lingle, Alex S. Evers, Joe Henry Steinbach and Gustav Akk*, ","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 13","pages":"XXX-XXX 962–968"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.5c00256","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144521691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"","authors":"Kristoffer Sahlholm*, Peder Svensson, Marcus Malo, Daniel R Andersson and Nibal Betari*, ","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 13","pages":"XXX-XXX 962–968"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.5c00270","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144521692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"","authors":"Eman M. Elbaz, Sherehan M. Ibrahim, Eman Rashad, Noha A. E. Yasin, Heba R. Ghaiad* and Noha A. Mehana, ","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 13","pages":"XXX-XXX 962–968"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.5c00351","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144521699","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"","authors":"Yue-Rong Li, Lin-Lin Xie, Hao-Bin Cai, Zhao-Hui Dang, Li-Ling Li, Xu Wang, Yun-Wei Lu, Zi-Cheng Zhang, Song Gao, Jia-Ye Liu, Long-Sheng Xu, Qin-Li Feng*, Xiu-De Qin* and Fan Bu*, ","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 13","pages":"XXX-XXX 962–968"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.5c00371","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144521700","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Impact of Lysine Acetylation Mutations on the Structure of Full-Length Tau Fibrils.","authors":"Aurelio J Dregni, Mei Hong","doi":"10.1021/acschemneuro.5c00149","DOIUrl":"https://doi.org/10.1021/acschemneuro.5c00149","url":null,"abstract":"<p><p>The tau protein aggregates into amyloid fibrils in Alzheimer's disease and other neurodegenerative diseases. In these tauopathies, tau is decorated with posttranslational modifications, including phosphorylation and acetylation, suggesting that these modifications may cause tau to aggregate into specific pathological structures. Here, we investigate how pseudoacetylation of three lysine residues, K311Q, K321Q, and K369Q, affects the fibrilization and fibril structure of full-length four-repeat tau. These acetyl mimics are in addition to four phospho-mimetic glutamate mutations at the PHF1 epitope (4E tau). The joint mutant 4E3Q tau formed well-ordered amyloid fibrils without anionic cofactors. The 4E3Q tau fibrils lack twists, preventing structure determination by cryoelectron microscopy and necessitating characterization by solid-state NMR. ¹³C and ¹⁵N chemical shifts indicate that pseudoacetylation caused the protein to adopt a distinct fold from the parent 4E tau fibrils: the rigid core contains β-strands between R2 and R4 repeats and near the end of the C-terminal domain. Importantly, the C-terminal half of the R3 repeat containing the K321Q mutation is disordered, in qualitative contrast with 4E tau. Chemical shifts indicate that these structural changes likely result from the disruption of salt bridges between lysine and aspartate residues. 4E3Q tau contains an immobilized R2, which differs from that of AD tau. These results provide insights into the impact of acetylation on tau fibrilization and fibril structure and suggest that acetylation of these three lysine residues in AD may occur after the formation of the paired-helical filament structure.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":" ","pages":""},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144537388","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neuroprotective Effects of a Benzofuran-Containing Selenium in a Mouse Alzheimer's Disease Model: Molecular, Biochemical, and Behavioral Analyses.","authors":"Tácia Katiane Hall, Mariana Parron Paim, Pâmella da Costa, Amanda Rebelo de Azevedo, Vanessa Nascimento, José Sebastião Santos Neto, Fernanda Severo Sabedra Sousa, Tiago Veiras Collares, Fabiana Kommling Seixas, César Augusto Brüning, Cristiani Folharini Bortolatto","doi":"10.1021/acschemneuro.5c00139","DOIUrl":"10.1021/acschemneuro.5c00139","url":null,"abstract":"<p><p>Alzheimer's disease (AD) is a neurodegenerative disorder mainly characterized by progressive cognitive decline, for which effective treatments remain limited, and selenium is known for its neuroprotective actions. Thus, this study evaluated the neuroprotective effects of the compound 2-(((3-trifluoromethyl)phenyl(selenyl)methyl)-2,3-dihydrobenzofuran (TFSeB) in a streptozotocin (STZ)-induced AD model in male Swiss mice. The animals received intracerebroventricular injections of STZ (3 mg/kg, a neurotoxic agent) to induce cognitive deficits, followed by treatment with TFSeB (1 and 5 mg/kg, intragastrically). Behavioral tests revealed that, like positive control (memantine), the compound TFSeB improved memory performance in the Y-maze, novel object recognition, and passive avoidance tests, suggesting its ability to counteract STZ-induced memory impairments. Biochemical analyses showed that the compound reduced oxidative stress markers in the prefrontal cortex and cerebellum of mice exposed to STZ, including TBARS, ROS, and nitrite levels while increasing NPSH. STZ induced an increase in monoamine oxidase B (MAO-B) activity in the hippocampus and cortex, as well as in acetylcholinesterase (AChE) activity in the cortex and cerebellum, which were reverted by TFSeB. Hippocampal RT-qPCR molecular analyses revealed that TFSeB modulated apoptosis-related proteins by increasing BCL-2 and decreasing BAX expression, favoring neuronal survival. Moreover, TFSeB increased brain-derived neurotrophic factor (BDNF) and nuclear factor erythroid 2 (NRF2), targets associated with neuroprotection. The compound also decreased key inflammatory and neurodegenerative markers, including nuclear factor kappa B (NF-κB), interleukin-6 (IL-6), and glycogen synthase kinase 3 beta (GSK3B). In conclusion, the compound TFSeB demonstrates promising protective effects in a STZ-induced AD model by modulating key neurochemical, oxidative, and neuroinflammatory pathways.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":" ","pages":"2420-2434"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144309242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"","authors":"Ewelina Jalonicka,&nbsp;Konstantin Rusakov,&nbsp;Grzegorz Szwachta and Piotr Hanczyc*,&nbsp;","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 13","pages":"XXX-XXX 962–968"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.5c00274","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144521685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"","authors":"Diksha Rani,&nbsp;Nitesh Priyadarshi,&nbsp;Nitin Kumar Singhal* and Bhupesh Goyal*,&nbsp;","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 13","pages":"XXX-XXX 962–968"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.5c00269","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144521697","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Neuroprotective Effects of the Crinoid Natural Compound Rhodoptilometrin in Parkinson's Disease Experimental Models: Implications for ER Stress and Autophagy Modulation.","authors":"Zhi-Hong Wen, Ya-Jen Chiu, San-Nan Yang, Bo-Lin Guo, Chien-Wei Feng, Jimmy Ming-Jung Chunag, Nan-Fu Chen, Wu-Fu Chen","doi":"10.1021/acschemneuro.5c00087","DOIUrl":"10.1021/acschemneuro.5c00087","url":null,"abstract":"<p><p>The pathogenesis of Parkinson's disease (PD) involves cellular processes such as endoplasmic reticulum (ER) stress, unfolded protein response, autophagy imbalance, and apoptosis, and identifying drugs that can regulate these molecular mechanisms may be a potential therapeutic strategy for PD. This study aimed to investigate the potential neuroprotective effects of the marine crinoid-derived natural compound (+)-rhodoptilometrin (RDM). We utilized an <i>in vitro</i> PD experimental model and conducted a biochemical analysis to investigate its potential neuroprotective effects against 6-hydroxydopamine (6-OHDA)-induced toxicity. We also examined its underlying molecular mechanisms, confirmed using the autophagy inhibitor 3-methyladenine. We utilized an <i>in vivo</i> PD model to evaluate motor function and verified the therapeutic effectiveness of the RDM. RDM effectively inhibited apoptosis, reduced ER stress, and enhanced the viability and autophagy of 6-OHDA-induced SH-SY5Y cells. This was evidenced by reductions in GRP78, p-eIF2α/eIF2α, XBP-1s, and C/EBP homologous protein levels alongside enhancements in LC3-related autophagy pathways. <i>In vivo</i> experiments using zebrafish also showed that RDM significantly attenuated the decrease in locomotor activity caused by 6-OHDA, concurrently alleviating GRP78-related ER stress and promoting antiapoptotic BCL2 expression. These findings indicate that RDM exerted neuroprotective effects by attenuating apoptosis, alleviating ER stress, and promoting autophagy pathways. RDM may be a promising antineurodegenerative drug.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":" ","pages":"2376-2386"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144264755","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}