Cellular and Molecular Life Sciences最新文献

{"title":"From HPV infection to cervical precancer: Molecular mechanisms, immune microenvironment and emerging technologies.","authors":"Yubing Zhou, Yunxiao Ge, Kangdong Liu, Hui Liu, Zigang Dong","doi":"10.1007/s00018-026-06473-x","DOIUrl":"10.1007/s00018-026-06473-x","url":null,"abstract":"<p><p>Cervical cancer remains a leading cause of cancer-related mortality among women globally, with persistent high-risk human papillomavirus (HPV) infection as the primary etiological factor. Cervical precancerous lesions, including high-grade squamous intraepithelial lesions and adenocarcinoma in situ, represent the critical window for intervention prior to invasive cancer development. However, additional factors such as immunosuppression, smoking, and microbiome composition also play crucial roles in the development of cervical precancerous lesions. While HPV vaccination, screening, and treatment have reduced cancer incidence, these must be complemented by personalized approaches that target the molecular mechanisms driving carcinogenesis. Key dysregulated tumor suppressors (e.g., p16) and signaling pathways (PI3K/AKT/mTOR, Wnt/β-catenin) highlight the need for advanced therapeutic strategies. The immune microenvironment also plays a critical role in cancer progression, suggesting potential for immunotherapy. Promising biomarkers like p16, Ki67, and microRNAs require integration with technologies such as single-cell RNA sequencing and spatial transcriptomics for deeper insights into tumor heterogeneity and microenvironment dynamics. Additionally, while deep learning models hold promise in improving diagnostic accuracy for cervical intraepithelial neoplasia (CIN), challenges such as data variability and interpretability need addressing. In conclusion, incorporating genomics, transcriptomics, immunotherapy, and artificial intelligence will enable more personalized and effective interventions, ultimately reducing the global burden of cervical cancer.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13675427/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149206550","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insulin-mediated ciliary remodeling in the choroid plexus epithelium.","authors":"Marleen Trapp, L Aurica Ritter, Greta Döking, James Cleland, Anthony D Hill, Annarita Patrizi","doi":"10.1007/s00018-026-06486-6","DOIUrl":"10.1007/s00018-026-06486-6","url":null,"abstract":"<p><p>The choroid plexus (ChP) epithelium plays a crucial role in cerebrospinal fluid production and brain homeostasis. ChP is mainly composed of multiciliated epithelial cells that exhibit a noncanonical ciliary organization whose function is still debated. Insulin signaling is known to be important for central nervous system function, but its role in ChP function and ciliary organization has not been elucidated yet. To investigate how prolonged insulin exposure modulates ChP cells, we treated primary murine choroid plexus epithelial cells (pCPECs) with insulin for up to six days and used a combination of immunohistochemistry, RT-qPCR, RNA fluorescence in situ hybridization, single cell analysis and Western Blot to explore underlying molecular mechanisms. We demonstrated that prolonged insulin treatment significantly increased the percentage of multiciliated clustered pCPECs and their axoneme length. Prolonged insulin treatment selectively induced translocation of IFT20, a key component of the intraflagellar transport system, to the ciliary axoneme by increasing the cytoplasmatic surface area covered by IFT20. To note, the expression of insulin receptors (IRs) in ex vivo ChP epithelial cells started during late embryogenesis and localized predominantly to the apical membrane, but not in the cilium. Our study suggests that insulin signaling may promote ciliary remodeling in choroid plexus epithelial cells, most likely by modulating intraflagellar transport dynamics involving IFT20. These findings reveal a novel role of insulin signaling in ChP cilia organization and function, with potential implications for cerebrospinal fluid (CSF) regulation and neurodevelopmental processes.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13675167/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149206560","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biphasic SMN condensates safeguard stress-induced cytoplasmic mislocalization of splicing RNPs.","authors":"Yannick L Riedel, Jessica Dressler, Maximilian T Schilling, Oliver J Gruss","doi":"10.1007/s00018-026-06459-9","DOIUrl":"https://doi.org/10.1007/s00018-026-06459-9","url":null,"abstract":"<p><p>Biogenesis of UsnRNPs occurs in distinct steps in the nucleus and the cytoplasm. Sequential cytoplasmic actions of CLNS1A in the PRMT5 complex and of the SMN complex assemble the Sm core structure consisting of RNA and proteins. Nuclear SMN, condensed in Cajal Bodies, promotes late maturation steps. Whether cytoplasmic SMN undergoes condensation, and how this contributes to UsnRNP biogenesis or homeostasis, is poorly defined. Here, we show that molecular crowding stress induces rapid, reversible condensation of cytoplasmic SMN into droplets and filamentous assemblies, S-bodies, that sequester mislocalized cytoplasmic UsnRNPs along microtubules. During stress recovery, S-bodies undergo microtubule-dependent reorganization into split SMN-CLNS1A condensates, Janus bodies, that promote clearance of mislocalized UsnRNPs. Strikingly, cellular models of the SMN-associated disease spinal muscular atrophy fail to assemble S-bodies and to clear cytoplasmic UsnRNPs. Our findings identify stress-induced SMN condensation as a mechanism to buffer and resolve cytoplasmic UsnRNP mislocalization and reveal impaired tolerance to molecular crowding as a hallmark of spinal muscular atrophy.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13627572/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149104685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dosage-sensitive regulation of Cofilin-1 and LIMK signaling controls myoblast differentiation and fusion.","authors":"Dora Gjirlić, Anja Weber, Guido Posern, Anurag Kumar Singh","doi":"10.1007/s00018-026-06437-1","DOIUrl":"10.1007/s00018-026-06437-1","url":null,"abstract":"<p><p>Skeletal muscle differentiation requires coordinated cytoskeletal remodeling and transcriptional reprogramming. Members of the actin-depolymerizing factor/Cofilin family regulate actin filament turnover, yet the isoform-specific functions of Cofilin-1 and Cofilin-2 during myogenesis remain incompletely understood. Murine C2C12 myoblasts were used to investigate the expression and function of Cofilin isoforms during differentiation. CRISPR/Cas9-mediated knockout, shRNA-mediated knockdown, immunofluorescence, gene expression analyses, MRTF reporter assays, and pharmacological inhibition of LIM kinase were used to assess myogenic progression and signaling. Myogenic differentiation was accompanied by a pronounced isoform transition characterized by progressive downregulation of Cofilin-1 and Actin-Depolymerizing Factor together with increased expression of Cofilin-2. Loss of Cofilin-1 resulted in marked morphological abnormalities, impaired cell-cycle exit, elevated MRTF activity, and reduced myotube formation, whereas Cofilin-2 deficiency produced comparatively mild effects during early differentiation. Importantly, partial reduction of Cofilin-1 enhanced myoblast fusion, while stronger depletion impaired differentiation, demonstrating a dosage-sensitive requirement for Cofilin-1. In addition, Cofilin-1 activity was dynamically regulated by transient LIM kinase-mediated phosphorylation during early differentiation, and inhibition of this pathway disrupted myogenic progression. Analyses of mRNA and protein stability indicated that isoform switching is primarily regulated at the level of gene expression. Cofilin-1 functions as a dosage-sensitive regulator of myogenic progression that links cytoskeletal remodeling to signaling pathways controlling proliferation and differentiation. Coordinated regulation of Cofilin-1 expression and activity, together with the transition to Cofilin-2, is required for efficient myoblast fusion and muscle formation.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13589735/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149007840","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"NPY promotes macrophage polarization and hepatic fibrogenesis via PI3K/MAPK-dependent neuroimmune mechanisms.","authors":"Qiang Lin, Xuyang Zheng, Weijia Dou, Qiangshan Bai, Shiyang Liang, Zhifu Kou, Hongwei Guo, Yao Ding, Shuguang Zhao, Jingjie Wang, Jikai Yin, Zhenxiong Liu","doi":"10.1007/s00018-026-06428-2","DOIUrl":"10.1007/s00018-026-06428-2","url":null,"abstract":"<p><strong>Background: </strong>Neuropeptide Y (NPY) is a key regulator of neuroimmune homeostasis. However, its role in the intrahepatic immune microenvironment and hepatic fibrosis remains unclear. We aimed to elucidate whether NPY participates in hepatic fibrogenesis via neuroimmune crosstalk and to dissect the underlying molecular mechanisms.</p><p><strong>Methods: </strong>Liver tissues from cirrhotic and non-cirrhotic human subjects were collected. Hepatic fibrosis was induced in mice via intraperitoneal carbon tetrachloride (CCl₄) injection or the 3,5-diethoxycarbonyl-1,4-dihydrocollidine (DDC) diet. The distribution of NPY and its receptors was detected in human and mouse hepatic tissues. NPY-knockout mice were used to evaluate the impact of NPY deletion on hepatic fibrosis, inflammation, and macrophage polarization. Hepatic NPY receptors were silenced in vivo, and the corresponding receptors or downstream kinases were blocked in vitro, to define the underlying signaling mechanisms.</p><p><strong>Results: </strong>NPY was elevated in fibrotic human and mouse livers and primarily secreted by intrahepatic sympathetic nerves. NPY1R and NPY2R (but not NPY4R/NPY5R) were increased and localized in hepatic macrophages. NPY deletion mitigated liver injury, collagen deposition, and inflammation, and suppressed both M1 and M2 macrophage polarization. In vivo knockdown of NPY1R or NPY2R recapitulated these protective effects. In vitro, NPY enhanced M1 polarization via NPY1R/NPY2R-coupled PI3K-PAK1-c-Jun signaling, whereas it promoted M2 polarization through the PI3K-PAK1-RSK cascade.</p><p><strong>Conclusion: </strong>NPY drives both M1 and M2 macrophage polarization and accelerates hepatic fibrogenesis through NPY1R/NPY2R-PI3K-MAPK-dependent neuroimmune signaling. These findings identify NPY and its receptors as potential therapeutic targets for hepatic fibrosis.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13615958/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149058946","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting METTL3/m6A/SOCS3 axis reprograms tumor-associated macrophage polarization to potentiate the efficacy of anti-PD-1 therapy in multiple myeloma.","authors":"Gang Wang, Fangyu Zhou, Xuefen Yan, Jiaheng Wang, Mengni Yan, Jinle Liu, Li Yu","doi":"10.1007/s00018-026-06421-9","DOIUrl":"10.1007/s00018-026-06421-9","url":null,"abstract":"<p><strong>Background: </strong>This study investigated the immunomodulatory roles of suppressor of cytokine signaling 3 (SOCS3) in macrophage polarization and cytotoxic T-cell activation within the tumor microenvironment (TME) of multiple myeloma (MM).</p><p><strong>Methods: </strong>SOCS3 expression was evaluated in clinical MM specimens and healthy controls. Gain- and loss-of-function assays and a MM cell-macrophage co-culture system were designed to elucidate the effects of SOCS3 on MM cell malignant progression and macrophage polarization. Mechanistic investigations focused on methyltransferase-like 3 (METTL3)-mediated N⁶-methyladenosine (m6A) modulation of SOCS3 and regulation of the Janus kinase 2 (JAK2)/signal transducer and activator of transcription 3 (STAT3) signaling pathway. Additionally, the antitumor efficacy of combined SOCS3 overexpression and anti-programmed cell death protein 1 (anti-PD-1) therapy was evaluated in a syngeneic subcutaneous tumor mouse model.</p><p><strong>Results: </strong>SOCS3 was downregulated in clinical MM samples and cell lines, a silencing mechanism driven by METTL3-mediated m6A modification. SOCS3 overexpression inhibited MM cell proliferation and migration while inducing apoptosis. Co-culture with SOCS3-overexpressing MM cells promoted M1-like macrophage polarization, accompanied by suppression of the JAK2/STAT3 signaling pathway. Conversely, SOCS3 silencing promoted malignant behaviors in MM cells and inhibited the M1-like macrophage phenotype. Furthermore, METTL3 silencing exerted tumor-suppressive and immunomodulatory effects similar to those of SOCS3 overexpression, which were reversed by SOCS3 knockdown. In vivo, SOCS3 overexpression potentiated the antitumor efficacy of anti-PD-1 therapy by driving M1-like macrophage polarization and CD8⁺ T-cell activation.</p><p><strong>Conclusion: </strong>SOCS3 exerts dual antitumor efficacy in MM by suppressing malignant tumor progression and reprogramming the TME toward M1-like macrophage polarization and CD8⁺ T-cell activation. Combining SOCS3 restoration with anti-PD-1 therapy provides a preclinical proof-of-concept for potential combinatorial strategies to enhance immune responses in MM.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13594075/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149012145","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The isolated HEPN domain of SACSIN exhibits RNA-binding activity.","authors":"Lisa Longo, Irene Mariani, Antonella Cusimano, Rita Carrotta, Elsa Zacco, Roberta Vazzana, Giuseppe Cappelli, Maria R Mangione, Maria A Costa, Nicola Cuscino, Rosa Passantino, Silvia Vilasi, Alessia Gallo, Vincenzo Martorana, Roberto Giambruno","doi":"10.1007/s00018-026-06369-w","DOIUrl":"10.1007/s00018-026-06369-w","url":null,"abstract":"<p><p>Autosomal Recessive Spastic Ataxia of Charlevoix-Saguenay (ARSACS) is a neurodegenerative disorder caused by mutations in the SACS gene, though the molecular function of its protein product, SACSIN, remains elusive. Therapeutic strategies for ARSACS are limited, mostly due to the exceptionally large size of SACSIN (~ 520 kDa), which precludes conventional gene therapy and standard molecular delivery methods. Over 200 pathogenic variants, including missense, nonsense and frameshift mutations, have been identified. Regardless of variant type, patients uniformly exhibit cerebellar ataxia, spasticity and peripheral neuropathy. Among them, patients with homozygous frameshift or missense mutations within the SACSIN higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain, suggesting that the alteration of the functional role of the SACSIN HEPN domain could be linked to the manifestation of ARSACS symptoms. Here, we show that the SACSIN HEPN domain can bind RNA in overexpression, corroborating the hypothesis that SACSIN functions as an RNA-binding protein. The interaction of the SACSIN HEPN domain with the RNA regulates the cellular compartmentalization of this domain as well as its propensity to form protein condensates. Conversely, an ARSACS mutated version of the SACSIN HEPN domain (F4574C) showed an impaired RNA-binding activity, a nuclear mis-localization and the predisposition to form protein condensates. Overall, our study unveils an unknown molecular function of the SACSIN HEPN domain that, if formally confirmed also for the full-length SACSIN, can pave the way for innovative therapeutic approaches for ARSACS patients.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13669270/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149179716","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rhomboid protease RHBDL2 is a calcium-activated suppressor of EGFR signalling in keratinocytes.","authors":"Nicholas Johnson, Jan Dohnálek, Jana Březinová, Josef Čáslavský, Aneta Škarková, Njainday Jobe, Monika Fliegl, Květa Trávníčková, Emma Burbridge, Vahap Canbay, Chatpakorn Rassameena Christiansen, Ulrich Auf dem Keller, Juraj Lábaj, Olha Fedosieieva, Jan Procházka, Daniel Rösel, Jan Brábek, Tomáš Vomastek, Colin Adrain, Kvido Stříšovský","doi":"10.1007/s00018-026-06377-w","DOIUrl":"10.1007/s00018-026-06377-w","url":null,"abstract":"<p><p>Signalling via the epidermal growth factor receptor (EGFR) is indispensable for morphogenesis and tissue homeostasis. It is activated by extracellular ligands, typically released from transmembrane precursors by proteolysis. Ligand shedding activity is provided by the conserved rhomboid intramembrane serine proteases in Drosophila, but by the unrelated ADAM family metalloproteases in mammals, leaving the functions of mammalian non-mitochondrial rhomboids underexplored. Using quantitative proteomics, we show that EGFR is the main endogenous substrate of the human rhomboid protease RHBDL2 in keratinocytes. By shedding the EGFR ectodomain, thus producing a decoy receptor, RHBDL2 suppresses EGFR signalling, limiting cell migration and invasion. Conspicuously, RHBDL2 activity is upregulated by elevated intracellular calcium concentration, a condition typical of keratinocyte differentiation. These effects are recapitulated in primary human keratinocytes, and human skin equivalents deficient in RHBDL2 display incomplete differentiation and are morphologically disordered compared to wild-type cells. We propose that context-specific fine-tuning of EGFR signalling and sensitivity to cross-talk from other signalling pathways could be important and hitherto overlooked roles of rhomboid proteases in mammals.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13597478/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149015924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative analysis of neuronal proteolytic pathways reveals neuron-specific and sub-compartmental-specific capacities with aging.","authors":"Mira Sleiman, Dimitra Ranti, Sudarson Baskaran, Patricia Kreis, Saskia Muth, Christian Gallrein, Agnieszka Münster-Wandowski, Norman Rahnis, Emilio Cirri, Britta J Eickholt, Janine Kirstein","doi":"10.1007/s00018-026-06383-y","DOIUrl":"https://doi.org/10.1007/s00018-026-06383-y","url":null,"abstract":"<p><p>Proteostasis is essential for maintaining neuronal function, and its dysregulation is a hallmark of aging and neurodegeneration. The ubiquitin-proteasome system (UPS) and macroautophagy are the two major proteolytic pathways responsible for protein degradation. However, their capacity and regulation differ between cell types and across aging. To elucidate the activity of both proteolytic pathways with aging, we performed a comparative analysis of the activity of UPS and macroautophagy in distinct neuronal subcellular compartments, in the soma and at synaptic terminals, across aging in neurons of Mus musculus (mouse) and Caenorhabditis elegans (nematode). In mice, our results identified differences between brain areas. While the cortical proteasomal activity declined with aging in both the somatic as well as synaptic-enriched neuronal subcompartments, the cerebellar proteasomal activity decreased only in the somatic-enriched compartments with aging. In C. elegans, we detected a decrease of proteasomal activity in both somatic and synaptic compartments of neurons. Interestingly, we observed an age-dependent change in several markers of autophagy in different fractions and brain areas of mice and a reduction of autophagosomes and autolysosomes with aging in C. elegans. Thus, we uncovered neuron-specific and subcompartmental-specific proteolytic capacities with aging that could manifest in different neuronal vulnerabilities for proteotoxic challenges with aging.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13481654/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788836","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction: Trimerization of CD40L-specific affibody molecules using collagen domains enhances target binding and CD40 blockade.","authors":"Cornelia Westerberg, Chiara Sorini, Mariam Al-Haddad, Hanna Mehari, Charlotta Preger, Stefan Ståhl, Maja Jagodic, John Löfblom","doi":"10.1007/s00018-026-06384-x","DOIUrl":"10.1007/s00018-026-06384-x","url":null,"abstract":"","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13457816/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148700810","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}