Frontiers in Molecular Neuroscience最新文献

{"title":"Stress and the gut-brain axis: an inflammatory perspective","authors":"Julia Morys, Andrzej Małecki, Marta Nowacka-Chmielewska","doi":"10.3389/fnmol.2024.1415567","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1415567","url":null,"abstract":"The gut-brain axis (GBA) plays a dominant role in maintaining homeostasis as well as contributes to mental health maintenance. The pathways that underpin the axis expand from macroscopic interactions with the nervous system, to the molecular signals that include microbial metabolites, tight junction protein expression, or cytokines released during inflammation. The dysfunctional GBA has been repeatedly linked to the occurrence of anxiety- and depressive-like behaviors development. The importance of the inflammatory aspects of the altered GBA has recently been highlighted in the literature. Here we summarize current reports on GBA signaling which involves the immune response within the intestinal and blood-brain barrier (BBB). We also emphasize the effect of stress response on altering barriers' permeability, and the therapeutic potential of microbiota restoration by probiotic administration or microbiota transplantation, based on the latest animal studies. Most research performed on various stress models showed an association between anxiety- and depressive-like behaviors, dysbiosis of gut microbiota, and disruption of intestinal permeability with simultaneous changes in BBB integrity. It could be postulated that under stress conditions impaired communication across BBB may therefore represent a significant mechanism allowing the gut microbiota to affect brain functions.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"15 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-07-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141746193","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":"Calcium-dependent activator protein for secretion 2 is involved in dopamine release in mouse midbrain neurons","authors":"Hirotoshi Iguchi, Takumi Katsuzawa, Chihiro Saruta, Tetsushi Sadakata, Shota Kobayashi, Yumi Sato, Akira Sato, Yoshitake Sano, So Maezawa, Yo Shinoda, Teiichi Furuichi","doi":"10.3389/fnmol.2024.1444629","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1444629","url":null,"abstract":"The Ca<jats:sup>2+</jats:sup>-dependent activator protein for secretion (CAPS/CADPS) family protein facilitates catecholamine release through the dense-core vesicle exocytosis in model neuroendocrine cell lines. However, it remains unclear if it induces dopamine release in the central neurons. This study aimed to examine the expression and function of CADPS2, one of the two CADPS paralogs, in dopamine neurons of the mouse midbrain. This study shows that CADPS2 was expressed in tyrosine hydroxylase and the vesicular monoamine transporter 2 (VMAT2)-positive dopaminergic neurons of the midbrain samples and primary mesencephalic cell cultures. Subcellular fractions rich in dopamine were collected using immunoaffinity for CADPS2 from midbrain protein extracts. Cell imaging using fluorescent false neurotransmitter FFN511 as a substrate for VMAT2 showed decreased activity-dependent dopamine release in <jats:italic>Cadps2</jats:italic>-deficient cultures, compared to that in wild-type cultures. These results suggest that CADPS2 is involved in dopamine release from the central neurons, indicating its involvement in the central dopamine pathway.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"24 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-07-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141746289","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":"Quantitative mass spectrometry analysis of the injured proximal and distal human digital nerve ends","authors":"Drifa Frostadottir, Charlotte Welinder, Raquel Perez, Lars B. Dahlin","doi":"10.3389/fnmol.2024.1425780","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1425780","url":null,"abstract":"IntroductionProteomic analysis of injured human peripheral nerves, particularly focusing on events occurring in the proximal and distal nerve ends, remains relatively underexplored. This study aimed to investigate the molecular patterns underlying a digital nerve injury, focusing on differences in protein expression between the proximal and distal nerve ends.MethodsA total of 26 human injured digital nerve samples (24 men; 2 women; median age 47 [30–66] years), harvested during primary nerve repair within 48 h post-injury from proximal and distal nerve ends, were analyzed using mass spectrometry.ResultsA total of 3,914 proteins were identified, with 127 proteins showing significant differences in abundance between the proximal and the distal nerve ends. The downregulation of proteins in the distal nerve end was associated with synaptic transmission, autophagy, neurotransmitter regulation, cell adhesion and migration. Conversely, proteins upregulated in the distal nerve end were implicated in cellular stress response, neuromuscular junction stability and muscle contraction, neuronal excitability and neurotransmitter release, synaptic vesicle recycling and axon guidance and angiogenesis.DiscussionInvestigation of proteins, with functional annotations analysis, in proximal and the distal ends of human injured digital nerves, revealed dynamic cellular responses aimed at promoting tissue degeneration and restoration, while suppressing non-essential processes.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"50 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141523087","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":"Post-translational modifications in prion diseases","authors":"Chloé Bizingre, Clara Bianchi, Anne Baudry, Aurélie Alleaume-Butaux, Benoit Schneider, Mathéa Pietri","doi":"10.3389/fnmol.2024.1405415","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1405415","url":null,"abstract":"More than 650 reversible and irreversible post-translational modifications (PTMs) of proteins have been listed so far. Canonical PTMs of proteins consist of the covalent addition of functional or chemical groups on target backbone amino-acids or the cleavage of the protein itself, giving rise to modified proteins with specific properties in terms of stability, solubility, cell distribution, activity, or interactions with other biomolecules. PTMs of protein contribute to cell homeostatic processes, enabling basal cell functions, allowing the cell to respond and adapt to variations of its environment, and globally maintaining the constancy of the <jats:italic>milieu interieur</jats:italic> (the body’s inner environment) to sustain human health. Abnormal protein PTMs are, however, associated with several disease states, such as cancers, metabolic disorders, or neurodegenerative diseases. Abnormal PTMs alter the functional properties of the protein or even cause a loss of protein function. One example of dramatic PTMs concerns the cellular prion protein (PrP<jats:sup>C</jats:sup>), a GPI-anchored signaling molecule at the plasma membrane, whose irreversible post-translational conformational conversion (PTCC) into pathogenic prions (PrP<jats:sup>Sc</jats:sup>) provokes neurodegeneration. PrP<jats:sup>C</jats:sup> PTCC into PrP<jats:sup>Sc</jats:sup> is an additional type of PTM that affects the tridimensional structure and physiological function of PrP<jats:sup>C</jats:sup> and generates a protein conformer with neurotoxic properties. PrP<jats:sup>C</jats:sup> PTCC into PrP<jats:sup>Sc</jats:sup> in neurons is the first step of a deleterious sequence of events at the root of a group of neurodegenerative disorders affecting both humans (Creutzfeldt–Jakob diseases for the most representative diseases) and animals (scrapie in sheep, bovine spongiform encephalopathy in cow, and chronic wasting disease in elk and deer). There are currently no therapies to block PrP<jats:sup>C</jats:sup> PTCC into PrP<jats:sup>Sc</jats:sup> and stop neurodegeneration in prion diseases. Here, we review known PrP<jats:sup>C</jats:sup> PTMs that influence PrP<jats:sup>C</jats:sup> conversion into PrP<jats:sup>Sc</jats:sup>. We summarized how PrP<jats:sup>C</jats:sup> PTCC into PrP<jats:sup>Sc</jats:sup> impacts the PrP<jats:sup>C</jats:sup> interactome at the plasma membrane and the downstream intracellular controlled protein effectors, whose abnormal activation or trafficking caused by altered PTMs promotes neurodegeneration. We discussed these effectors as candidate drug targets for prion diseases and possibly other neurodegenerative diseases.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"12 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141551166","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":"SFRP4 protein expression is reduced in high grade astrocytomas which is not caused by the methylation of its promoter","authors":"Anja Kafka, Nives Pećina-Šlaus, Denis Drmić, Anja Bukovac, Niko Njirić, Kamelija Žarković, Antonia Jakovčević","doi":"10.3389/fnmol.2024.1398872","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1398872","url":null,"abstract":"IntroductionEpigenetics play a vital role in stratifying CNS tumors and gliomas. The importance of studying Secreted frizzled-related protein 4 (SFRP4) in gliomas is to improve diffuse glioma methylation profiling. Here we examined the methylation status of <jats:italic>SFRP4</jats:italic> promoter and the level of its protein expression in diffuse gliomas WHO grades 2–4.MethodsSFRP4 expression was detected by immunohistochemistry and evaluated semi-quantitatively. In the tumor hot-spot area, the intensity of protein expression in 200 cells was determined using ImageJ (National Institutes of Health, United States). The assessment of immunopositivity was based on the IRS score (Immunoreactivity Score). Promoter methylation was examined by methylation specific-PCR (MSP) in fifty-one diffuse glioma samples and appropriate controls. Isolated DNA was treated with bisulfite conversion and afterwards used for MSP. Public databases (cBioPortal, COSMIC and LOVD) were searched to corroborate the results.Results and discussionSFRP4 protein expression in glioblastomas was very weak or non-existent in 86.7% of samples, moderate in 13.3%, while strong expression was not observed. The increase in astrocytoma grade resulted in SFRP4 protein decrease (<jats:italic>p</jats:italic> = 0.008), indicating the loss of its antagonistic role in Wnt signaling. Promoter methylation of <jats:italic>SFRP4</jats:italic> gene was found in 16.3% of cases. Astrocytomas grade 2 had significantly more methylated cases compared to grade 3 astrocytomas (<jats:italic>p</jats:italic> = 0.004) and glioblastomas (<jats:italic>p</jats:italic> &amp;lt; 0.001), which may indicate temporal niche of methylation in grade 2. Furthermore, the expression levels of SFRP4 were high in samples with methylated <jats:italic>SFRP4</jats:italic> promoter and low or missing in unmethylated cases (Pearson’s R = −0.413; <jats:italic>p</jats:italic> = 0.003). We also investigated the association of SFRP4 changes to key Wnt regulators <jats:italic>GSK3β</jats:italic> and <jats:italic>DKK3</jats:italic> and established a positive correlation between methylations of <jats:italic>SFRP4</jats:italic> and <jats:italic>GSK3β</jats:italic> (Pearson’s R = 0.323; <jats:italic>p</jats:italic> = 0.03). Furthermore, SFRP4 expression was correlated to unmethylated <jats:italic>DKK3</jats:italic> (Chi square = 7.254; <jats:italic>p</jats:italic> = 0.027) indication that Wnt signaling antagonist is associated to negative regulator’s demethylation.ConclusionThe study contributes to the recognition of the significance of epigenetic changes in diffuse glioma indicating that restoring SFRP4 protein holds potential as therapeutic avenue. Reduced expression of SFRP4 in glioblastomas, not following promoter methylation pattern, suggests another mechanism, possible global methylation, that turns off SFRP4 expression in higher grades.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"17 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141551167","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":"Treadmill running on neuropathic pain: via modulation of neuroinflammation","authors":"Wei-Chun He, Shuang-Long Hou, Kai-Bin Wang, Ning Xu, Ke Li, Ting Xiong, Jing Luo","doi":"10.3389/fnmol.2024.1345864","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1345864","url":null,"abstract":"Neuropathic pain is a type of chronic pain caused by an injury or somatosensory nervous system disease. Drugs and exercise could effectively relieve neuropathic pain, but no treatment can completely stop neuropathic pain. The integration of exercise into neuropathic pain management has attracted considerable interest in recent years, and treadmill training is the most used among exercise therapies. Neuropathic pain can be effectively treated if its mechanism is clarified. In recent years, the association between neuroinflammation and neuropathic pain has been explored. Neuroinflammation can trigger proinflammatory cytokines, activate microglia, inhibit descending pain modulatory systems, and promote the overexpression of brain-derived neurotrophic factor, which lead to the generation of neuropathic pain and hypersensitivity. Treadmill exercise can alleviate neuropathic pain mainly by regulating neuroinflammation, including inhibiting the activity of pro-inflammatory factors and over activation of microglia in the dorsal horn, regulating the expression of mu opioid receptor expression in the rostral ventromedial medulla and levels of γ-aminobutyric acid to activate the descending pain modulatory system and the overexpression of brain-derived neurotrophic factor. This article reviews and summarizes research on the effect of treadmill exercise on neuropathic pain and its role in the regulation of neuroinflammation to explore its benefits for neuropathic pain treatment.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"39 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141551191","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":"Pharmacological HDAC3 inhibition alters memory updating in young and old male mice","authors":"Chad W. Smies, Lauren Bellfy, Destiny S. Wright, Sofia G. Bennetts, Mark W. Urban, Chad A. Brunswick, Guanhua Shu, Janine L. Kwapis","doi":"10.3389/fnmol.2024.1429880","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1429880","url":null,"abstract":"Long-term memories are not stored in a stable state but must be flexible and dynamic to maintain relevance in response to new information. Existing memories are thought to be updated through the process of reconsolidation, in which memory retrieval initiates destabilization and updating to incorporate new information. Memory updating is impaired in old age, yet little is known about the mechanisms that go awry. One potential mechanism is the repressive histone deacetylase 3 (HDAC3), which is a powerful negative regulator of memory formation that contributes to age-related impairments in memory formation. Here, we tested whether HDAC3 also contributes to age-related impairments in memory updating using the Objects in Updated Locations (OUL) paradigm. We show that blocking HDAC3 immediately after updating with the pharmacological inhibitor RGFP966 ameliorated age-related impairments in memory updating in 18-m.o. male mice. Surprisingly, we found that post-update HDAC3 inhibition in young (3-m.o.) male mice had no effect on memory updating but instead impaired memory for the original information, suggesting that the original and updated information may compete for expression at test and HDAC3 helps regulate which information is expressed. To test this idea, we next assessed whether HDAC3 inhibition would improve memory updating in young male mice given a weak, subthreshold update. Consistent with our hypothesis, we found that HDAC3 blockade strengthened the subthreshold update without impairing memory for the original information, enabling balanced expression of the original and updated information. Together, this research suggests that HDAC3 may contribute to age-related impairments in memory updating and may regulate the strength of a memory update in young mice, shifting the balance between the original and updated information at test.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"15 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141523088","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":"Downregulation of hsa-miR-132 and hsa-miR-129: non-coding RNA molecular signatures of Alzheimer’s disease","authors":"Siranjeevi Nagaraj, Carolina Quintanilla-Sánchez, Kunie Ando, Lidia Lopez-Gutierrez, Emilie Doeraene, Andreea-Claudia Kosa, Emmanuel Aydin, Jean-Pierre Brion, Karelle Leroy","doi":"10.3389/fnmol.2024.1423340","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1423340","url":null,"abstract":"Alzheimer’s disease (AD) affects the elderly population by causing memory impairments, cognitive and behavioral abnormalities. Currently, no curative treatments exist, emphasizing the need to explore therapeutic options that modify the progression of the disease. MicroRNAs (miRNAs), as non-coding RNAs, demonstrate multifaceted targeting potential and are known to be dysregulated in AD pathology. This mini review focuses on two promising miRNAs, hsa-miR-132 and hsa-miR-129, which consistently exhibit differential regulation in AD. By employing computational predictions and referencing published RNA sequencing dataset, we elucidate the intricate miRNA-mRNA target relationships associated with hsa-miR-132 and hsa-miR-129. Our review consistently identifies the downregulation of hsa-miR-132 and hsa-miR-129 in AD brains as a non-coding RNA molecular signature across studies conducted over the past 15 years in AD research.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"21 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141523089","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":"Methods for negating the impact of zinc contamination to allow characterization of positive allosteric modulators of glycine receptors","authors":"Casey I. Gallagher, David P. Bishop, Thomas E. Lockwood, Tristan Rawling, Robert J. Vandenberg","doi":"10.3389/fnmol.2024.1392715","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1392715","url":null,"abstract":"Zinc is a ubiquitous contaminant in many buffers, purified products and common labware that has previously been suggested to impact on the results of functional GlyR studies and may inadvertently cause the effectiveness of some GlyR modulators to be over-estimated. This could greatly impact the assessment of potential drug-candidates and contribute to the reduced effectiveness of compounds that reach clinical stages. This is especially true for GlyR modulators being developed for pain therapeutics due to the changes in spinal zinc concentrations that have been observed during chronic pain conditions. In this study we use two-electrode voltage clamp electrophysiology to evaluate the metal chelators tricine and Ca-EDTA, and show that tricine produces inhibitory effects at GlyRα<jats:sub>1</jats:sub> that are not mediated by zinc. We also utilized the zinc insensitive W170S mutation as a tool to validate metal chelators and confirm that zinc contamination has not impacted the examination of lipid modulators previously developed by our lab. This study helps to further develop methods to negate the impact of contaminating zinc in functional studies of GlyRs which should be incorporated into future studies that seek to characterize the activity of novel modulators at GlyRs.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"23 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141523090","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":"Ubiquitination contributes to the regulation of GDP-mannose pyrophosphorylase B activity","authors":"Patricia Franzka, Sonnhild Mittag, Abhijnan Chakraborty, Otmar Huber, Christian A. Hübner","doi":"10.3389/fnmol.2024.1375297","DOIUrl":"https://doi.org/10.3389/fnmol.2024.1375297","url":null,"abstract":"GDP-mannose pyrophosphorylase B (GMPPB) loss-of-function is associated with muscular dystrophy and variable additional neurological symptoms. GMPPB facilitates the catalytic conversion of mannose-1-phosphate and GTP to GDP-mannose, which serves as a mannose donor for glycosylation. The activity of GMPPB is regulated by its non-catalytic paralogue GMPPA, which can bind GDP-mannose and interact with GMPPB, thereby acting as an allosteric feedback inhibitor of GMPPB. Using pulldown, immunoprecipitation, turnover experiments as well as immunolabeling and enzyme activity assays, we provide first direct evidence that GMPPB activity is regulated by ubiquitination. We further show that the E3 ubiquitin ligase TRIM67 interacts with GMPPB and that knockdown of TRM67 reduces ubiquitination of GMPPB, thus reflecting a candidate E3 ligase for the ubiquitination of GMPPB. While the inhibition of GMPPB ubiquitination decreases its enzymatic activity, its ubiquitination neither affects its interaction with GMPPA nor its turnover. Taken together, we show that the ubiquitination of GMPPB represents another level of regulation of GDP-mannose supply.","PeriodicalId":12630,"journal":{"name":"Frontiers in Molecular Neuroscience","volume":"30 1","pages":""},"PeriodicalIF":4.8,"publicationDate":"2024-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141551168","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}