Cell Biochemistry and Biophysics最新文献

{"title":"Brusatol Triggers Cell Cycle Arrest and Apoptosis, Disrupts Sterol Biosynthesis, and Enhances the Anti-Leukemic Activity of Venetoclax in AML Cells.","authors":"Xuan Chu, Zhangyin Ren, Jiaojiao Deng, Ting Xiao, Dongfang Jiang, Chen Wang, Jiangbo Liu","doi":"10.1007/s12013-026-02165-2","DOIUrl":"https://doi.org/10.1007/s12013-026-02165-2","url":null,"abstract":"<p><p>Acute myeloid leukemia (AML) is an aggressive hematologic malignancy with poor prognosis. Although chemotherapy and targeted therapies have advanced significantly, relapse and chemoresistance continue to be the major clinical challenges, which emphasizes the need for novel treatments. Brusatol, a natural quassinoid compound, has been reported to exert anti-tumor effects in various solid tumors; however, its anti-leukemic activity and potential mechanism in AML remain poorly characterized. THP-1 and KG-1a cells were treated with brusatol alone or combined with venetoclax. Proliferation was evaluated by CCK-8, cell counting and morphological observation. Apoptosis was detected by flow cytometry, Western blot, morphological changes and TUNEL staining. RNA-seq with GO, KEGG, and GSEA was used to identify key pathways. Cell cycle was analyzed by flow cytometry. DNA synthesis was detected by EdU assay. mRNA expression was measured by qPCR. Protein levels were determined by Western blot. Brusatol significantly suppressed the proliferation of AML cells. Moreover, brusatol notably increased the apoptotic rate, upregulated the expression of cleaved‑PARP and Bax, downregulated MCL1, and induced typical apoptotic morphological changes. Transcriptomic analysis demonstrated that brusatol primarily modulated pathways related to the cell cycle and steroid biosynthesis. Brusatol downregulated the expression of MCM2, PCNA, and CDK2, thereby inducing cell cycle arrest and inhibiting DNA replication. Brusatol also significantly reduced the expression of key genes involved in steroid biosynthesis, including DHCR7, SQLE, EBP, and FDFT1. Furthermore, co-treatment with brusatol and venetoclax strengthens cell cycle arrest, proliferation inhibition and apoptosis induction in AML cells compared with single drug treatment. Brusatol inhibits AML cell proliferation, induces apoptosis, triggers cell‑cycle dysregulation, and downregulates sterol‑biosynthesis‑related gene expression. Brusatol also enhances the anti-leukemic activity of venetoclax. This study preliminarily elucidates the underlying mechanisms and provides experimental evidence supporting the potential therapeutic value of brusatol for acute myeloid leukemia.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148910365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"RBM4 Promotes Nasopharyngeal Carcinoma Growth and Metastasis by Stabilizing HOXB13 mRNA.","authors":"Zhi Chen, Dan Liang, Zhai Liu, Yu Ren, Zhimei Wang, Jun Wan, Yi Tang, Yibo Zhou","doi":"10.1007/s12013-026-02139-4","DOIUrl":"https://doi.org/10.1007/s12013-026-02139-4","url":null,"abstract":"<p><p>Nasopharyngeal carcinoma (NPC) remains a major clinical challenge, particularly at advanced stages. RNA-binding proteins (RBPs) are important post-transcriptional regulators of tumorigenesis, but their roles in NPC remain poorly understood. This study investigated whether RNA-binding motif protein 4 (RBM4) stabilizes homeobox B13 (HOXB13) mRNA and thereby activates oncogenic signaling to promote NPC progression. Bioinformatics analysis identified differentially expressed genes in NPC. ENCORI was used to predict potential RNA-binding proteins (RBPs) targeting the candidate gene, and the predicted interaction was validated by RNA immunoprecipitation. Functional effects of HOXB13 and RBM4 in NPC cells were examined using colony formation and Transwell assays, along with modulating RBM4, HOXB13, nuclear factor kappa B (NF-κB) p65, and β-catenin expression. In vivo, effects of the RBM4/HOXB13 axis on NPC tumor growth and metastasis were evaluated using murine xenograft and lung metastasis models. HOXB13 was among the most strongly upregulated genes in NPC, and RBM4 was predicted to be a candidate RBP targeting HOXB13 mRNA. RBM4 was also upregulated in NPC models and increased HOXB13 mRNA stability. RBM4 silencing suppressed NPC cell proliferation, migration, invasion, and epithelial-mesenchymal transition (EMT), while increasing apoptosis and reducing HOXB13 expression and NF-κB and Wnt/β-catenin signaling. Overexpression of HOXB13, NF-κB p65, or β-catenin partially reversed these effects. In vivo, RBM4 silencing inhibited xenograft growth and experimental lung metastasis, and these effects were partially reversed by HOXB13 overexpression. RBM4 acts as a pro-tumorigenic RBP in NPC by stabilizing HOXB13 mRNA and activating the NF-κB and Wnt/β-catenin pathways. The RBM4/HOXB13 axis therefore warrants further investigation as a potential molecular target in NPC.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148910343","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"From Glycation to Toxicity: α-Synuclein Oligomers, Oxidative Stress, and Multi-Targeted Protection by Trans-Ferulic Acid.","authors":"Murtaza Hussain, Md Nadir Hassan, Rizwan Ahmad, Gul E Zehra, Amrit Kaur, Umme Kulsum Baliyavi, Tariq Aziz, Rizwan Hasan Khan, Waseem Ahmad Siddiqui","doi":"10.1007/s12013-026-02150-9","DOIUrl":"https://doi.org/10.1007/s12013-026-02150-9","url":null,"abstract":"<p><p>Glycation, a spontaneous reaction between sugars and biomolecules, is a central driver of oxidative stress and protein dysfunction in metabolic and neurodegenerative disorders. α-Synuclein (α-Syn), a key protein implicated in Parkinson's disease, is particularly susceptible to modification by reactive carbonyl species such as methylglyoxal (Me) due to its lysine-rich structure. These modifications result in the formation of advanced glycation end products (AGEs), which promote protein aggregation, impair cellular clearance, and induce oxidative and inflammatory damage via the AGE-RAGE axis. This cascade, characterised by increased reactive oxygen and nitrogen species, mitochondrial dysfunction, and metabolic imbalance, accelerates neuronal degeneration and disease progression.This study investigates trans-ferulic acid (TF) as a multifunctional therapeutic candidate targeting this interconnected network. TF effectively inhibited glycation in both ribose and Me-induced α-Syn systems, demonstrating strong antiglycation potential. Additionally, TF exhibited significant scavenging activity against hydrogen peroxide and nitric oxide, underscoring its capacity to reduce oxidative and nitrosative stress. TF also inhibited α-glucosidase, indicating a further mechanism for controlling glucose availability and limiting the formation of reactive intermediates. Collectively, these findings identify TF as a promising multi-target agent capable of disrupting the glycation-oxidative stress cycle at multiple levels. By concurrently reducing reactive species, suppressing carbonyl formation, and limiting protein aggregation, TF represents a compelling strategy to mitigate glycation-driven toxicity and its pathological consequences.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148910324","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Thymoquinone as a Multi-Target Modulator of Inflammatory and Immunometabolic Signaling: Mechanisms and Therapeutic Implications.","authors":"Abdullah Faisal Albukhari","doi":"10.1007/s12013-026-02162-5","DOIUrl":"https://doi.org/10.1007/s12013-026-02162-5","url":null,"abstract":"<p><p>Thymoquinone, the principal bioactive constituent of Nigella sativa, has been extensively investigated for its anti-inflammatory, antioxidant, and metabolic effects. However, these activities are often examined separately, limiting understanding of their broader biological integration. This review examines thymoquinone through three interconnected immunometabolic axes: NF-κB-mediated inflammation, AMPK/mTOR-driven metabolic regulation, and ROS/Nrf2-dependent redox balance. Preclinical evidence indicates that thymoquinone modulates each of these pathways and may influence the crosstalk linking oxidative stress, metabolic reprogramming, and inflammation. Based on these findings, we propose a conceptual framework positioning thymoquinone as a multi-target immunometabolic modulator. This framework is hypothesis-generating and requires further validation through integrated experimental and clinical studies.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148910388","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"UCHL1 Promotes M1 Macrophage Polarization and Inflammation in Chronic Rhinosinusitis by Stabilizing HIF-1α.","authors":"Yu Zhang","doi":"10.1007/s12013-026-02098-w","DOIUrl":"https://doi.org/10.1007/s12013-026-02098-w","url":null,"abstract":"<p><p>While the persistent inflammation in chronic rhinosinusitis (CRS) is closely linked to M1 macrophage polarization, the mechanisms that control this polarization have not been fully elucidated. A positive correlation was observed between UCHL1 (a significantly upregulated deubiquitinating enzyme in CRS tissues) and M1 macrophage markers in our bioinformatic analysis. Suppression of UCHL1, via genetic knockdown or pharmacologic inhibition (6RK73), attenuated M1 macrophage polarization and curtailed the production of IL‑1β, TNF‑α and IL‑6 in both cellular and animal models. Mechanistically, UCHL1 interacts with HIF‑1α and stabilizes it by deubiquitinating it, thereby blocking its proteasomal degradation. This stabilization is functionally relevant, as HIF‑1α activation reversed the suppression of M1 polarization induced by UCHL1 knockdown. Furthermore, conditioned medium from UCHL1‑deficient macrophages mitigated epithelial cell damage-an effect that was abolished by HIF‑1α agonism. In a murine CRS model, pharmacological inhibition of UCHL1 significantly ameliorated histopathological injury, reduced behavioral symptoms such as sneezing and nasal scratching, and lowered IgE levels, and pro‑inflammatory cytokines, while downregulating the UCHL1/HIF‑1α axis and M1 marker expression. Collectively, these findings indicate that UCHL1 drives M1 macrophage polarization and exacerbates CRS inflammation by stabilizing HIF‑1α through deubiquitination, highlighting UCHL1 as a potential therapeutic target in CRS.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148878851","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"FASN Promotes Malignant Progression of Bladder Cancer by Regulating Lipid Metabolism via the ERK/PPAR Pathway.","authors":"Liang Wei, Yishuang Guo, Yuedong Hao, Lina Ji","doi":"10.1007/s12013-026-02104-1","DOIUrl":"10.1007/s12013-026-02104-1","url":null,"abstract":"<p><p>Among urological cancers, bladder cancer (BC) is one of the main causes of morbidity and death. Although the lipogenic enzyme fatty acid synthase (FASN) is known to aid in the growth of tumors, its precise role and mechanism in bladder cancer remain unclear. The effects and mechanisms of FASN in BC are examined in this study. Using information from The Cancer Genome Atlas (TCGA), the expression and prognostic significance of FASN were examined. Functional assays, including CCK-8, apoptosis, Transwell, and scratch-wound experiments, were conducted in BIU-87 and T24 cells after FASN knockdown and treatment with the ERK activator TBHQ. Western blot analysis assessed key proteins of the ERK/PPARγ pathway, such as PPARα, PPARγ, and p-ERK1/2, along with the lipid metabolism marker CD36. Metabolite levels, including free fatty acids, acyl-coenzyme A, and triglycerides, were quantified. Finally, an in vivo subcutaneous xenograft model was established to validate these findings. In BC tissues, FASN expression was markedly increased and associated with lower overall survival. FASN knockdown increased apoptosis while inhibiting BC cell motility, invasion, and proliferation. These phenotypic changes were associated with downregulation of the ERK/PPARγ pathway and reduced fatty acid uptake and metabolite levels. Both in vitro and in vivo, treatment with TBHQ effectively reversed the tumor-suppressive effects and metabolic alterations induced by FASN knockdown, confirming the involvement of ERK signaling. This study therefore demonstrates that FASN promotes BC progression by modulating the ERK/PPARγ pathway and lipid metabolism. Targeting FASN or its upstream activator ERK could thus provide a therapeutic strategy to inhibit BC growth.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":"4055-4069"},"PeriodicalIF":3.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148314873","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"METTL3-Mediated m6A Modification of ACTR2 Promotes Trophoblast Cell Growth, Migration and Invasion in Unexplained Recurrent Spontaneous Abortion.","authors":"Maohua Ren, Lina Wang, Rongqin Li, Jianrong Liu","doi":"10.1007/s12013-026-02152-7","DOIUrl":"10.1007/s12013-026-02152-7","url":null,"abstract":"<p><p>Actin-related protein 2 (ACTR2) is an important factor in the regulation of cell function and is considered to be a potential therapeutic target for RSA. However, whether ACTR2 mediates unexplained RSA by regulating trophoblast cell function remains unclear. The expression of ACTR2 and methyltransferase-like 3 (METTL3) in the villous tissues of unexplained RSA patients and trophoblast cells (HTR-8/SVneo) was detected by qRT-PCR or western blot. Cell proliferation, apoptosis, invasion, and migration were examined by CCK8 assay, EdU assay, flow cytometry, transwell assay and wound healing assay. MeRIP assay, RIP assay or RNA pull-down assay was used to confirm the interaction between METTL3/YTHDF2 and ACTR2. The regulation of METTL3/YTHDF2 on the mRNA stability of ACTR2 was confirmed by actinomycin D assay. β-catenin and Wnt3A protein levels were tested by western blot. ACTR2 was downregulated in unexplained RSA patients, and its overexpression promoted HTR-8/SVneo cell proliferation, migration, invasion and reduced apoptosis. However, ACTR2 knockdown suppressed HTR-8/SVneo cell functions. ACTR2 had m6A modification sites, and METTL3 could enhance the m6A modification of ACTR2 to reduce its mRNA stability and expression. METTL3-mediated the m6A modification of ACTR2 could be recognized by m6A reader YTHDF2. METTL3 knockdown increased HTR-8/SVneo cell growth, migration and invasion, as well as β-catenin and Wnt3A protein levels, while these effects could be reversed by ACTR2 silencing. METTL3 might inhibit trophoblast cell functions by inactivating Wnt/β-catenin pathway through enhancing the m6A modification of ACTR2, providing a novel target for unexplained RSA.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":"4613-4626"},"PeriodicalIF":3.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786562","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Berberine Modulates Mitophagy-Related Gene Expression and Suppresses Breast Cancer Cells: A Multi-Omics and Experimental Study.","authors":"Hong Wang, Yingjin Luo, Kaihua Zheng, Xiaoqing Wu, Jiale Lv, Yongliang Mei, Wei Ren","doi":"10.1007/s12013-026-02156-3","DOIUrl":"10.1007/s12013-026-02156-3","url":null,"abstract":"<p><p>Breast cancer became the most commonly diagnosed cancer worldwide in 2020. Mitophagy, as a key mechanism for selectively clearing damaged mitochondria, plays an important role in breast cancer-related processes. Berberine has shown its anti-tumor ability in multiple types of tumors, but whether berberine exerts its anti-breast cancer effects through modulating mitophagy-related genes remains to be elucidated. This study integrated the Gene Expression Omnibus (GEO) database and single-cell sequencing, explored the key genes that interfere with breast cancer, evaluated and verified the efficacy of berberine against breast cancer by molecular docking and in vitro experiments, and provided a novel direction to breast cancer prevention and therapy and drug development. Screening autophagy-related targets through the GEO database combined with the autophagy gene library and revealing the relationship within cancerous cells with immunological cells through single-cell sequencing. Using molecular docking and in vitro tests to evaluate and confirm the efficacy of berberine against breast cancer. In this study, 20 pivotal genes were screened and identified. These genes are mainly involved in autophagy-related pathways that are significantly activated in breast cancer. Enrichment analysis showed that autophagy and mitophagy pathways were obvious in breast cancer. The immune microenvironment of single-cell shows that pathological changes of fibroblasts and NK cells mediated by macrophage invasion in tumor tissue may be an important molecular mechanism of breast cancer. Molecular docking and in vitro experiments suggest that berberine can effectively inhibit breast cancer by targeting BECN1, BCL2, HIF1A, MYC, PINK1, and FOXO3 to regulate autophagy initiation and mitochondrial quality control, while CASP3 was assessed only at the mRNA level due to the intrinsic CASP3 deficiency in MCF-7 cells. Through GEO data combined with single-cell sequencing and in vitro experimental verification, this study revealed the pivotal gene of mitophagy in breast cancer and provides evidence that berberine modulates mitophagy-related genes and induces mitochondrial damage. These findings offer a theoretical basis for further investigation into berberine in breast cancer therapy.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":"4645-4668"},"PeriodicalIF":3.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148823978","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Dual Role of TGF-β and Hypoxia on MMP14-Mediated Invasion in PC3 Cells.","authors":"Derya Okuyan, Hanife Aktaş, Fatma Poyrazlı, Sümeyye Aydoğan Türkoğlu","doi":"10.1007/s12013-026-02102-3","DOIUrl":"10.1007/s12013-026-02102-3","url":null,"abstract":"<p><p>The MMP14 gene, which encodes the only membrane-bound collagenase, is highly expressed in malignant tumors and plays a decisive role in invasiveness. This study investigated the transcriptional regulation of MMP14 by the TGF-β cytokine and hypoxia in PC3 prostate carcinoma cells. Bioinformatic analysis confirmed the presence of key regulatory elements in the MMP14 promoter, specifically the HRE (for HIF-1α) and SMAD binding sites. Three 5' deletion fragments of the MMP14 promoter (P1: -1251/+75; P2: -649/+75; P3: -176/+75) were cloned for functional analysis. PC3 cells were treated with TGF-β, the hypoxia-mimetic CoCl₂, and the combination. Gene and protein expression were analyzed using Real-Time PCR and Immunofluorescence Cytochemistry (IFC), respectively, while promoter activities were assessed via a Luciferase reporter assay. COL1A expression was also evaluated to explore its association with MMP14-mediated extracellular matrix remodeling. Hypoxia emerged as the dominant inductive factor. MMP14 mRNA and protein levels were significantly elevated under hypoxic and combined TGF-β/CoCl₂ conditions. Promoter analysis revealed that the full-length P1 construct was consistently upregulated by all treatments. However, the shorter P2 and P3 fragments exhibited a decrease in activity with TGF-β alone, suggesting a complex, region-specific regulation predominantly influenced by hypoxic signaling. Critically, COL1A1 mRNA expression was observed in hypoxic groups with elevated MMP14 levels, indicating a possible inverse relationship between MMP14 induction and COL1A-associated extracellular matrix remodeling. Hypoxia is the primary driver of MMP14 induction and protein accumulation in PC3 cells, with TGF-β acting as a complex co-regulator whose activating effect is potentiated under low-oxygen stress. These findings highlight the contribution of the HIF/MMP14 axis to invasion-associated molecular regulation in prostate cancer.</p>","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":"4025-4034"},"PeriodicalIF":3.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13585980/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315102","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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: Peroxiredoxins in the Developmental Origins of Health and Disease: Insights from Maternal Under and Overnutrition - A Critical Interpretative Scoping Review.","authors":"Matheus Naia Fioretto, Luísa Correia Gomes, Flávia Alessandra Maciel, Ana Luiza Silva de Abreu, Ana Luiza Romano Gabriel, Sérgio Luis Felisbino, Luis Antonio Justulin","doi":"10.1007/s12013-026-02086-0","DOIUrl":"10.1007/s12013-026-02086-0","url":null,"abstract":"","PeriodicalId":510,"journal":{"name":"Cell Biochemistry and Biophysics","volume":" ","pages":"4683"},"PeriodicalIF":3.0,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13585905/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147759075","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}