The FEBS journal最新文献

{"title":"Transcriptome-wide alternative mRNA splicing analysis reveals post-transcriptional regulation of neuronal differentiation.","authors":"Yuan Zhou, Sherif Rashad, Kuniyasu Niizuma","doi":"10.1111/febs.17408","DOIUrl":"https://doi.org/10.1111/febs.17408","url":null,"abstract":"<p><p>Alternative splicing (AS) plays an important role in neuronal development, function, and disease. Efforts to analyze the transcriptome of AS in neurons on a wide scale are currently limited. We characterized the transcriptome-wide AS changes in SH-SY5Y neuronal differentiation model, which is widely used to study neuronal function and disorders. Our analysis revealed global changes in five AS programs that drive neuronal differentiation. Motif analysis revealed the contribution of RNA-binding proteins (RBPs) to the regulation of AS during neuronal development. We concentrated on the primary alternative splicing program that occurs during differentiation, specifically on events involving exon skipping (SE). Motif analysis revealed motifs for polypyrimidine tract-binding protein 1 (PTB) and ELAV-like RNA binding protein 1 (HuR/ELAVL1) to be the top enriched in SE events, and their protein levels were downregulated after differentiation. shRNA knockdown of either PTB and HuR was associated with enhanced neuronal differentiation and transcriptome-wide exon skipping events that drive the process of differentiation. At the level of gene expression, we observed only modest changes, indicating predominant post-transcriptional effects of PTB and HuR. We also observed that both RBPs altered cellular responses to oxidative stress, in line with the differentiated phenotype observed after either gene knockdown. Our work characterizes the AS changes in a widely used and important model of neuronal development and neuroscience research and reveals intricate post-transcriptional regulation of neuronal differentiation.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143034934","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transketolase promotes osteosarcoma progression through the YY1-PAK4 axis.","authors":"Doudou Jing, Wei Wu, Xin Huang, Zhenhao Zhang, Xuanzuo Chen, Fuhua Huang, Jianxiang Liu, Zhicai Zhang, Zengwu Shao, Feifei Pu","doi":"10.1111/febs.17375","DOIUrl":"https://doi.org/10.1111/febs.17375","url":null,"abstract":"<p><p>Osteosarcoma, a malignant bone tumor that occurs in adolescents, proliferates and is prone to pulmonary metastasis. Osteosarcoma is characterized by high genotypic heterogeneity, making it difficult to identify reliable anti-osteosarcoma targets. The genotype of osteosarcoma may be highly dynamic, but its high dependence on energy remains constant. Fortunately, tumors tend to have relatively consistent metabolic types. Targeting metabolism with anti-tumor therapies is a new strategy for treating tumors. Genes related to carbohydrate metabolism are widely and highly expressed in tumor tissues. Transketolase (TKT), a key enzyme at the non-oxidative stage of the pentose phosphate pathway, is up-regulated in various tumors. In the present study, TKT promoted osteosarcoma cell proliferation non-metabolically. Specifically, TKT bound directly to amino acid residues of Yin Yang 1 (YY1) at amino acids 201-228, stimulating YY1 to bind to the promoter of P21 activated kinase 4 (PAK4) and resulting in PAK4 expression and activation of the phosphoinositide 3-kinase-Akt signaling pathway. Additionally, we designed a peptide, YY1-PEP, based on the exact mechanism of how TKT promotes osteosarcoma. Per in vivo and in vitro experiments, YY1-PEP displayed anti-osteosarcoma properties. The present study provides a new feasible strategy against osteosarcoma progression.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143034935","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"I \"Gut\" Rhythm: the microbiota as a modulator of the stress response and circadian rhythms.","authors":"Gabriel S S Tofani, Gerard Clarke, John F Cryan","doi":"10.1111/febs.17400","DOIUrl":"https://doi.org/10.1111/febs.17400","url":null,"abstract":"<p><p>Modern habits are becoming more and more disruptive to health. As our days are often filled with circadian disruption and stress exposures, we need to understand how our responses to these external stimuli are shaped and how their mediators can be targeted to promote health. A growing body of research demonstrates the role of the gut microbiota in influencing brain function and behavior. The stress response and circadian rhythms, which are essential to maintaining appropriate responses to the environment, are known to be impacted by the gut microbiota. Gut microbes have been shown to alter the host's response to stress and modulate circadian rhythmicity. Although studies demonstrated strong links between the gut microbiota, circadian rhythms and the stress response, such studies were conducted in an independent manner not conducive to understanding the interface between these factors. Due to the interconnected nature of the stress response and circadian rhythms, in this review we explore how the gut microbiota may play a role in regulating the integration of stress and circadian signals in mammals and the consequences for brain health and disease.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143026244","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fine-tuned calcium homeostasis is crucial for murine erythropoiesis.","authors":"Shujing Zhang, Yuanzhen Zhang, Yanxia Li, Zhiyue Zhang, Hui Li, Miaomiao Xu, Zhiyuan Lu, Yuan Li, Baobing Zhao","doi":"10.1111/febs.17401","DOIUrl":"https://doi.org/10.1111/febs.17401","url":null,"abstract":"<p><p>Intracellular calcium (Ca²⁺) is a crucial signaling molecule involved in multiple cellular processes. However, the functional role of Ca²⁺ in terminal erythropoiesis remains unclear. Here, we uncovered the dynamics of intracellular Ca²⁺ levels during mouse erythroid development. By using the calcium ionophore ionomycin, we found that low Ca²⁺ levels are required for the expansion of erythroid progenitors, whereas higher Ca²⁺ levels led to the differentiation and proliferation of early-stage erythroblasts. Intracellular Ca²⁺ levels were then gradually reduced, which is required for the nuclear condensation and polarisation at the late stage of erythroid differentiation. However, elevated Ca²⁺ levels in late-stage erythroblasts, achieved by using ionomycin, promoted erythroid enucleation via calmodulin (CaM)/calcium/calmodulin-dependent protein kinase kinase 1 (CaMKK1)/AMPK signaling. These data suggest that the reduction of intracellular Ca²⁺ plays a double-edged role at the late stage of erythroid differentiation, which is beneficial for nuclear condensation but compromises terminal enucleation. Our study highlighted the importance of the fine-tuned regulation of intracellular Ca²⁺ during terminal erythropoiesis, providing cues for the efficient generation of mature and enucleated erythrocytes in vitro.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143019111","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Succinate receptor 1 signaling mutually depends on subcellular localization and cellular metabolism.","authors":"Aenne-Dorothea Liebing, Philipp Rabe, Petra Krumbholz, Christian Zieschang, Franziska Bischof, Angela Schulz, Susan Billig, Claudia Birkemeyer, Thanigaimalai Pillaiyar, Mikel Garcia-Marcos, Robert Kraft, Claudia Stäubert","doi":"10.1111/febs.17407","DOIUrl":"https://doi.org/10.1111/febs.17407","url":null,"abstract":"<p><p>Succinate is a pivotal tricarboxylic acid cycle metabolite but also specifically activates the G_i- and G_q-coupled succinate receptor 1 (SUCNR1). Contradictory roles of succinate and succinate-SUCNR1 signaling include reports about its anti- or pro-inflammatory effects. The link between cellular metabolism and localization-dependent SUCNR1 signaling qualifies as a potential cause for the reported conflicts. To systematically address this connection, we used a diverse set of methods, including several bioluminescence resonance energy transfer-based biosensors, dynamic mass redistribution measurements, second messenger and kinase phosphorylation assays, calcium imaging, and metabolic analyses. Different cellular metabolic states were mimicked using glucose (Glc) or glutamine (Gln) as available energy substrates to provoke differential endogenous succinate (SUC) production. We show that SUCNR1 signaling, localization, and metabolism are mutually dependent, with SUCNR1 showing distinct spatial and energy substrate-dependent G_i and G_q protein activation. We found that Gln-consumption associated with a higher rate of oxidative phosphorylation causes increased extracellular SUC concentrations, accompanied by a higher rate of SUCNR1 internalization, reduced miniG_q protein recruitment to the plasma membrane, and lower Ca²⁺ signals. In Glc, under basal conditions, SUCNR1 causes stronger G_q than G_i protein activation, while the opposite is true upon stimulation with an agonist. In addition, SUCNR1 specifically interacts with miniG proteins in endosomal compartments. In THP-1 cells, polarized to M2-like macrophages, endogenous SUCNR1-mediated G_i signaling stimulates glycolysis, while G_q signaling inhibits the glycolytic rate. Our results suggest that the metabolic context determines spatially dependent SUCNR1 signaling, which in turn modulates cellular energy homeostasis and mediates adaptations to changes in SUC concentrations.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143019094","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lack of TRIC-B dysregulates cytoskeleton assembly, trapping β-catenin at osteoblast adhesion sites.","authors":"Barbara Maria Contento, Nadia Garibaldi, Alessandra Sala, Erika Palladino, Amanda Oldani, Alessandra Carriero, Antonella Forlino, Roberta Besio","doi":"10.1111/febs.17399","DOIUrl":"https://doi.org/10.1111/febs.17399","url":null,"abstract":"<p><p>The trimeric intracellular cation channel B (TRIC-B), encoded by TMEM38B, is a potassium (K⁺) channel present in the endoplasmic reticulum membrane, where it counterbalances calcium (Ca²⁺) exit. Lack of TRIC-B activity causes a recessive form of the skeletal disease osteogenesis imperfecta (OI), namely OI type XIV, characterized by impaired intracellular Ca²⁺ flux and defects in osteoblast (OB) differentiation and activity. Taking advantage of the OB-specific Tmem38b knockout mouse (Runx2Cre;Tmem38b^fl/fl; cKO), we investigated how the ion imbalance affects the osteogenetic process. We found an abnormal cytoskeleton in the cKO OBs, with actin accumulation at OB adhesion sites. The reduced amount of active Ca²⁺-dependent actin-binding proteins myristoylated alanine-rich C-kinase substrate (MARCKS) and fascin, which modulate cytoskeletal actin dynamics, explains the altered cytoskeletal assembly. The actin clusters at adhesion sites trap β-catenin, a key structural protein at cell-cell junction sites, that abnormally accumulates despite the significant reduction in both N- and E-cadherins. Besides its structural fuction at cell borders, β-catenin also has a pivotal role as a transcription factor for proper osteoblastogenesis. Immunofluorescence of cKO nuclei revealed impaired nuclear β-catenin translocation, further validated in human fetal OB knocked out for TMEM38B, which was not rescued by specifically stimulating the canonical Wnt pathway. Thus, we demonstrated in vitro that alterations of intracellular Ca²⁺ homeostasis, as a consequence of lack of TRIC-B, cause cytoskeleton disorganization in cKO OBs, resulting in abnormal β-catenin accumulation at cell adhesion sites and reduced nuclear β-catenin translocation, contributing to impaired osteoblastogenesis.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143019129","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"LDHAα, a lactate dehydrogenase A isoform, promotes glycolysis and tumor progression.","authors":"Bingqing Huang, Wencui Shen, Yujiao Jia, Li Qin, Haoxu Wang, Qi Sun, Zhijian Xiao, Rongxin Zhang, Huijun Wang","doi":"10.1111/febs.17374","DOIUrl":"https://doi.org/10.1111/febs.17374","url":null,"abstract":"<p><p>Lactate dehydrogenase A (LDHA) is upregulated in multiple cancer types and contributes to the Warburg effect. Several studies have found that many tumor-related genes have subtypes and play important roles in promoting cancer development. Here, we identified a novel LDHA transcript, which produced a new protein 3 kDa larger than LDHA, which we named LDHAα. We found that multiple cancer cell lines express LDHAα, and ectopic expression of LDHAα led to a higher proliferation and migration rate in vitro. Ectopic expression of LDHAα could also promote tumor cell growth in vivo. Conversely, deletion of LDHAα by CRISPR-sgRNA significantly inhibited the growth of tumor cells. LDHAα was found to be mainly located in the cytoplasm, and overexpression or deletion of LDHAα could significantly affect the glucose uptake and lactate production of tumor cells. Further investigation showed that c-MYC and FOXM1 could markedly modulate the expression of both LDHA and LDHAα, especially c-MYC. We found that a small molecular compound targeting LDHA could also inhibit the enzyme activity of LDHAα. LDHAα, LDHA and c-MYC expression was significantly higher in human acute lymphocytic leukemia and colorectal cancer tissue specimens compared to normal controls. In conclusion, our study identified LDHAα as a subtype of LDHA and highlighted its critical role in tumor metabolism, providing a potential new therapeutic target for tumor diagnosis and treatment.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143019132","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PI5P4K inhibitors: promising opportunities and challenges.","authors":"Koh Takeuchi, Lisa Nagase, Shun Kageyama, Hirotaka Kanoh, Masashi Oshima, Aki Ogawa-Iio, Yoshiki Ikeda, Yuki Fujii, Sei Kondo, Natsuki Osaka, Takeshi Masuda, Tsukasa Ishihara, Yoshikazu Nakamura, Yoshihisa Hirota, Takehiko Sasaki, Toshiya Senda, Atsuo T Sasaki","doi":"10.1111/febs.17393","DOIUrl":"https://doi.org/10.1111/febs.17393","url":null,"abstract":"<p><p>Phosphatidylinositol 5-phosphate 4-kinases (PI5P4K), also known as type II PIPKs or PIPKIIs, convert the lipid second messenger PI5P to PI(4,5)P₂. The PI5P4K family consists of three isozymes in mammals-PI5P4Kα, β, and γ-which notably utilize both GTP and ATP as phosphodonors. Unlike the other two isozymes, which can utilize both ATP and GTP, PI5P4Kβ exhibits a marked preference for GTP over ATP, acting as an intracellular GTP sensor that alters its kinase activity in response to physiological changes in GTP concentration. Knockout studies have demonstrated a critical role for PI5P4Kα and β in tumorigenesis, while PI5P4Kγ has been implicated in regulating immune and neural systems. Pharmacological targeting of PI5P4K holds promise for the development of new therapeutic approaches against cancer, immune dysfunction, and neurodegenerative diseases. Although several PI5P4K inhibitors have already been developed, challenges remain in PI5P4K inhibitor development, including a discrepancy between in vitro and cellular efficacy. This discrepancy is attributable to mainly three factors. (a) Most PI5P4K inhibitors were developed at low ATP levels, where these enzymes exhibit minimal activity. (b) Non-catalytic functions of PI5P4K require careful interpretation of PI5P4K depletion studies, as their scaffolding roles suppress class I PI3K signaling. (c) The lack of pharmacodynamic markers for in vivo assessment complicates efficacy assessment. To address these issues and promote the development of effective and targeted therapeutic strategies, this review provides an analytical overview of the distinct roles of individual isozymes and recent developments in PI5P4K inhibitors, emphasizing structural insights and the importance of pharmacodynamic marker identification.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143019135","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"TNFAIP3-interacting protein 1 (ABIN-1) negatively regulates caspase-8/FADD-dependent pyroptosis.","authors":"Xueyi Li, Daoyong Wang, Zhenyi Su, Xiaohua Mao","doi":"10.1111/febs.17404","DOIUrl":"https://doi.org/10.1111/febs.17404","url":null,"abstract":"<p><p>TNFAIP3-interacting protein 1 (TNIP1; also known as ABIN-1) is a ubiquitin-binding protein that suppresses death-receptor- or Toll-like receptor-mediated apoptosis and necroptosis; however, it remains unclear whether ABIN-1 is capable of regulating pyroptosis. In the present study, we found that, in mouse embryonic fibroblasts and macrophages, ABIN-1 deficiency sensitized cells to poly(I:C) + TAK1 inhibitor 5Z-7-oxozeaenol-induced pyroptosis besides apoptosis and necroptosis. The sensitizing effect of ABIN-1 deficiency on pyroptosis depended on caspase-8 and its adaptor molecule FAS-associated death domain protein. In a mouse model of polymicrobial sepsis, myeloid-specific deletion of Abin-1 rendered mice more sensitive to pyroptosis, apoptosis and necroptosis, and exacerbated disease severity. Interestingly, ABIN-1 deficiency triggered gasdermin-E-mediated pyroptosis in mouse embryonic fibroblasts, but induced gasdermin-D-mediated pyroptosis in macrophages, both in a caspase-8-dependent manner. Furthermore, we demonstrated that, upon poly(I:C) + 5Z-7-oxozeaenol stimulation, ABIN-1 deficiency facilitates FAS-associated death domain protein recruitment to caspase-8; thus, the mechanism by which ABIN-1 downregulates caspase-8 activity is conserved in tumor necrosis factor receptor type 1 and Toll-like receptor 3 signaling-induced cell death. Together, our work identifies a previously unrecognized role for ABIN-1 as a negative regulator of pyroptosis in addition to apoptosis and necroptosis, suggesting that ABIN-1 represents a promising molecule to halt or reverse progression of refractory inflammatory disorders whose pathogenesis involves multiple forms of programmed cell death.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143019100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fatty-acid amide hydrolase inhibition mitigates Alzheimer's disease progression in mouse models of amyloidosis.","authors":"Sergio Oddi, Lucia Scipioni, Antonio Totaro, Giacomo Giacovazzo, Francesca Ciaramellano, Daniel Tortolani, Alessandro Leuti, Rita Businaro, Federica Armeli, Andras Bilkei-Gorzo, Roberto Coccurello, Andreas Zimmer, Mauro Maccarrone","doi":"10.1111/febs.17403","DOIUrl":"https://doi.org/10.1111/febs.17403","url":null,"abstract":"<p><p>The endocannabinoid N-arachidonoylethanolamine (AEA) is a pro-homeostatic bioactive lipid known for its anti-inflammatory, anti-oxidative, immunomodulatory, and neuroprotective properties, which may contrast/mitigate Alzheimer's disease (AD) pathology. This study explores the therapeutic potential of targeting fatty acid amide hydrolase (FAAH), the major enzyme degrading AEA, in mouse models of amyloidosis (APP/PS1 and Tg2576). Enhancing AEA signaling by genetic deletion of FAAH delayed cognitive deficits in APP/PS1 mice and improved cognitive symptoms in 12-month-old AD-like mice. Chronic pharmacological FAAH inhibition fully reverted neurocognitive decline, attenuated neuroinflammation, and promoted neuroprotective mechanisms in Tg2576 mice. Additionally, pharmacological FAAH inhibition robustly suppressed β-amyloid production and accumulation, associated with decreased expression of β-site amyloid precursor protein cleaving enzyme 1 (BACE1), possibly through a cannabinoid receptor 1-dependent epigenetic mechanism. These findings improve our understanding of AEA signaling in AD pathogenesis and provide proof of concept that selective targeting of FAAH activity could be a promising therapeutic strategy against AD.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143019107","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}