Cellular and Molecular Life Sciences最新文献

{"title":"Identification of a human mitochondrial isoform of TRPV1: a thermostat regulating mitochondrial maximal temperature?","authors":"Florian Beignon, Sylvie Ducreux, Artur Wardaszka, Joanna K Bujak, Léa Tuifua, Camille Blaecke, Caroline Bosson, Lucie Maujean, Florentin Moulin, Yannick Le Dantec, Morgane LeMao, Adélie Mellinger, Méline Wery, David Goudenège, Arnaud Chevrollier, Salim Khiati, Hélène Tricoire-Leignel, Naig Gueguen, Nathalie Roux-Buisson, Julien Fauré, Piotr Bednarczyk, Guy Lenaers, César Mattei","doi":"10.1007/s00018-026-06360-5","DOIUrl":"10.1007/s00018-026-06360-5","url":null,"abstract":"<p><p>Mitochondria are well known to produce ATP for cell energy requirements and thermogenesis simultaneously by the respiratory chain, with a potential optimum temperature of 50 °C, while deleterious overheating should be prevented by a yet unknown system. Here, we report the identification of a human Transient Receptor Potential Vanilloid 1 (mitoTRPV1) alternative isoform located in the mitochondrial inner membrane, which acts as a thermostat regulating mitochondrial maximal temperature. The ubiquitously expressed mitoTRPV1 open reading frame overlaps TRPV1 exons 1 and 2 and intron 2 in a + 1 frame, encoding for an effective 150 amino-acid N-terminal mitochondrial targeting sequence (MTS) conserved amongst mammalian species, followed by the 687 amino acids of the TRPV1 C-terminal sequence. Pharmacological activation of mitoTRPV1 induces a low cytoplasmic Ca²⁺ increase and mitochondrial cooling without modification of mitochondrial respiration and ATP production. We conclude that, in our experimental conditions, mitoTRPV1 acts as a thermostat to promote mitochondrial thermolysis without impairing respiration and ATP production. They point to the potential implication of mitoTRPV1 in human diseases related to temperature dysregulation, and should be further studied in physiological conditions in cellular and animal models expressing mitoTRPV1 endogenously.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13594010/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149012060","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":"Oxidative protein folding and Ca²⁺ homeostasis under redox control.","authors":"Jiro Ogura, Junichi Fujii, Hiroaki Yamaguchi","doi":"10.1007/s00018-026-06263-5","DOIUrl":"10.1007/s00018-026-06263-5","url":null,"abstract":"<p><p>Secretory and membrane proteins undergo oxidative folding, the process of forming disulfide bonds between cysteine side chains to construct a stable higher-order structure, primarily in the endoplasmic reticulum (ER) followed by further post-translational modification in the Golgi apparatus, after which proteins proceed to pathways for secretion and membrane localization. Proteins involved in transferring oxidizing power to target proteins possess a pair of highly reactive forms of cysteine residue that mediate reduction-oxidation (redox) reactions. Oxidizing power, which is generally provided in the form of reactive oxygen/reactive nitrogen oxide species. Endoplasmic reticulum oxidoreductin 1 (ERO1) is the ancient ER oxidase that utilizes molecular oxygen to produce hydrogen peroxide, which is then utilized for thiol oxidation to form a disulfide bridge in target proteins. Excessive elevation of these species could promote aberrant oxidation of susceptible molecules, which could lead to an accumulation of misfolded proteins and consequent ER stress. The ER is also involved in cellular Ca²⁺ signaling in which Ca²⁺-pump ATPase and Ca²⁺ release channels coordinate to play essential roles. Ca²⁺ regulates the activity of some redox-reactive proteins, which are largely in the family of protein disulfide isomerase. Thus, the Ca²⁺ status indirectly associates with the oxidative folding of nascent proteins. Upon extensive oxidation, inactivation of the Ca²⁺-pump ATPase and inappropriate Ca²⁺ leak via the Ca²⁺ channels causes a depletion of Ca²⁺ in the ER lumen. When intracellular calcium is depleted, stromal interaction molecules (STIM) in the ER membrane sense the Ca²⁺ status within the ER lumen. STIM differentially regulates two types of Ca²⁺ channels in the plasma membrane: Ca²⁺-release-activated Ca²⁺ channel (ORAI), and voltage-operated Ca²⁺ channel (CaV1.2). This regulation coordinately maintains Ca²⁺ homeostasis within cells. Moreover, Zn²⁺ and H⁺ indirectly affect the potential of redox responses through controlling ER chaperone molecules. The redox capacity of the ER is maintained by resident proteins and small compounds, which include cations Ca²⁺, Zn²⁺ and H⁺, and hence the comprehensive care of them is necessary in order to maintain normal ER function.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":" ","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13672763/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148548080","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":"Deciphering the heterogeneity of chicken gonadal primordial germ cells via single-cell RNA sequencing.","authors":"Xiaomin Wang, Shenghu Zhang, Kaipeng Wang, Qianru Li, Yihang Yang, Xingnan Huang, Zhuangfei Wang, Mengmeng Guo, Bo Chen, Zheting Zhang, Bo Wang, Duanqing Pei, Chengchen Zhao","doi":"10.1007/s00018-026-06331-w","DOIUrl":"https://doi.org/10.1007/s00018-026-06331-w","url":null,"abstract":"<p><p>Chicken primordial germ cells (PGCs) are valuable for breeding, germplasm preservation, and genetic modifications. Here, using single-cell transcriptome analysis, we found that three transcriptionally distinct PGC subtypes were exist in chicken embryonic gonads PGCs. We further demonstrated that in vitro-cultured PGCs could integrate into recipient gonads via blood vessel injection. Additionally, the gene-modified PGCs could be re-established and integrated into recipient gonads after the PGCs were cultured for long-term use by a second blood-vessel injection. Together, these results provide evidence for substantial heterogeneity among chicken gonadal PGCs, which were previously considered a homogeneous cell population. This diversity could be leveraged to establish and expand PGCs for long-term in vitro culture from differentiated gonads.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149223364","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dissecting the functional and spatial roles of peroxiredoxins as H₂O₂ scavengers and redox transducers.","authors":"Laura de Cubas, Adrian Konopko, Susanna Boronat, José Ayté, Elena Hidalgo","doi":"10.1007/s00018-026-06356-1","DOIUrl":"https://doi.org/10.1007/s00018-026-06356-1","url":null,"abstract":"<p><p>Since their discovery in the late 1980s as peroxidases that eliminate hydrogen peroxide (H₂O₂), peroxiredoxins (Prxs) have been recognized not only for detoxification but also for roles in redox signaling. In fission yeast, the main Prx, Tpx1, maintains steady-state H₂O₂ below toxic levels through its scavenging activity. Under excess peroxides, Tpx1 switches to a signaling role, transmitting oxidative signals to the transcription factor Pap1. Dissecting the relative contributions of Tpx1's peroxidase and sensor functions is challenging. To address this, we used a synthetic biology strategy to separate these dual roles. Tpx1 or catalase (Ctt1) was expressed in distinct subcellular compartments, and their capacity to remove H₂O₂ and activate Pap1 was assessed. Both scavengers can complement the growth defects of cells lacking Tpx1 in high oxygen. Combined with H₂O₂ biosensors, our results show that Tpx1 efficiently controls H₂O₂ levels from any compartment, whereas Ctt1 does not. However, cells expressing mitochondrial- or nuclear-targeted Tpx1 display reduced oxidative stress tolerance because Pap1 activation requires cytosolic Tpx1. Overall, Tpx1 is a highly effective peroxidase throughout the cell, but its subcellular localization is essential for proper redox signaling regulation.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149223375","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transcription factors as essential regulators of myometrial smooth muscle cell function during pregnancy and labor.","authors":"Sabrina Martini, Palak Gujral, Eduardo Orozco-Alonso, James Saliba, Volker Blank","doi":"10.1007/s00018-026-06341-8","DOIUrl":"10.1007/s00018-026-06341-8","url":null,"abstract":"<p><p>Parturition is a tightly regulated process coordinated by myometrial smooth muscle cells, which generate the uterine contraction required for birth. Preterm labor, defined as labor occurring before 37 weeks of gestation, remains a significant clinical challenge due to its association with adverse short and long-term risks on neonatal and maternal health. Earlier and recent studies provide strong evidence that transcription factors are performing crucial functions in uterine smooth muscle cells. In this review, we focus on the PR/ER, PPAR, NF-κB, AP-1, NFE2L2, and MAFF transcription factors and provide a comprehensive overview of their respective roles in myometrial smooth muscle cell function and the labor process. We also briefly discuss other transcriptional regulators that have been linked to uterine quiescence during pregnancy, to activation of the labor process or to both functions. Collectively, these transcription factors control various cellular processes, including inflammation, regulation of cytokine, chemokine and metalloproteinase expression, oxidative stress response, prostaglandin synthesis, calcium signaling, and contractility. Monitoring and targeting these transcription factors and associated pathways in the uterus are key for delaying or preventing preterm labor through the design of novel diagnostic and therapeutic tools to improve birth outcomes.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":" ","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13672739/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148535384","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":"Reduced KLF4 expression in endothelial cells triggers pulmonary vascular abnormalities associated with experimental congenital diaphragmatic hernia.","authors":"Heleen M Kool, Petra E Bürgisser, Gabriela G Edel, Anne Boerema-de Munck, Marjon Buscop-van Kempen, Panagiotis Liakopoulos, Petros Kolovos, Wilfred F J van Ijcken, Robbert J Rottier","doi":"10.1007/s00018-026-06319-6","DOIUrl":"10.1007/s00018-026-06319-6","url":null,"abstract":"<p><p>Congenital diaphragmatic hernia (CDH) is a rare anomaly with an incidence of 1 in 3000 live births and characterized by defective closure of the diaphragm, lung hypoplasia, and pulmonary vascular remodeling. Although several genes associated with the occurrence of CDH, no clear genetic component has been identified. Previously, we showed that CDH patients have vascular abnormalities already early in development, and that perivascular cells are affected in CDH. In the current study, we focused on early abnormalities in the nitrofen-induced CDH mouse model. Transcriptome analysis of FACS-sorted perivascular and endothelial cell populations from lungs of control and experimental mouse CDH revealed a high similarity in GO terms of differentially expressed genes (DEGs) between these populations, suggesting a disturbed interaction between endothelial cells and pericytes. The disturbed interaction is the basis for the aberrant development of the pulmonary vasculature in CDH. Furthermore, the RNA sequence data revealed reduced expression of the Kruppel like factor 4 (Klf4) gene in endothelial cells of CDH, which was confirmed with protein expression analysis. Furthermore, we show that KLF4 is an important up stream regulator of genes associated with vascular development and confirm that members of the NOTCH signaling pathway are differentially expressed, indicating that NOTCH signaling is disturbed in CDH. Collectively, our data support the importance of KLF4 in pulmonary angiogenesis and contribute to our previous data that pulmonary vessels in CDH patients are already affected before birth, which in turn may impact therapeutic strategies to reduce pulmonary hypertension associated with CDH.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":" ","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13669280/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148520017","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":"SOX10-mediated regulation of the MiR-106a/363 cluster drives RAF inhibitor resistance in BRAF-mutant melanoma.","authors":"Ying Li, Yu-le Yong, Zhe Zhi, ZhenZhen Lu, Zongguan Huang, Lanlan Cui, Mo Zhang, Zihao Wu, Yiming Hu, Guanfei Zhang, Xiaofei Zhao, Shujun Han, Yan Zheng, Yongping Shao","doi":"10.1007/s00018-026-06354-3","DOIUrl":"10.1007/s00018-026-06354-3","url":null,"abstract":"<p><p>Adaptive resistance to MAPK inhibitors remains a major clinical obstacle in BRAF-mutant melanoma, driven by reversible transcriptional and epigenetic reprogramming. Previous studies have implicated loss of SRY-box transcription factor 10 (SOX10) and concurrent activation of TGF-β signaling in this process, but the molecular link between them has remained unresolved. Here, we identify a SOX10-miR-106a/363-TGFBR2 regulatory axis that governs adaptive resistance. SOX10 directly activates transcription of the miR-106a/363 cluster through a distal cis-regulatory element. In turn, the miR-106a/363 cluster members miR-106a-5p and miR-20b-5p suppress TGFBR2 post-transcriptionally, while miR-363-3p indirectly reduces TGFBR2 expression by targeting SOX4, a transcriptional activator of TGFBR2. This dual-layered repression restrains TGF-β signaling and maintains drug sensitivity. Loss of SOX10 diminishes miR-106a/363 expression, derepresses TGFBR2, and promotes a mesenchymal-like, drug-tolerant state. Restoring miR-106a/363 expression partially re-sensitizes melanomas to RAF inhibitors in vivo. These findings reveal a previously unrecognized regulatory circuit linking SOX10 to TGF-β signaling and highlight the miR-106a/363 cluster as a potential therapeutic target to overcome adaptive resistance in melanoma.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":" ","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13661844/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148497353","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 expanding landscape of Deltex: signaling crosstalk and clinical implications.","authors":"Vartika Sharma, Pratikshya Sahoo, Mousumi Mutsuddi, Ashim Mukherjee","doi":"10.1007/s00018-026-06353-4","DOIUrl":"10.1007/s00018-026-06353-4","url":null,"abstract":"<p><p>The deltex (DTX) gene family encodes RING-type E3 ubiquitin ligases that are central to the regulation of the Notch signaling pathway, a mechanism governing cell fate, differentiation, proliferation, and apoptosis during development and adult tissue homeostasis. In Drosophila melanogaster, the Deltex (Dx) fine-tunes Notch signaling by modulating receptor endocytosis and degradation, acting as either an enhancer or a suppressor depending on the context. Insights from flies have revealed the evolutionary conservation of the Dx-Notch interaction across species, including humans. However, recent studies have expanded this view, identifying Dx as a regulator of multiple signaling pathways beyond Notch, specifically Wingless, Decapentaplegic, and Toll, underscoring its role as a hub for cellular communication. Through its broad regulatory network, Dx influences fundamental processes including cell growth, differentiation, apoptosis, and homeostasis. Dysregulation of Dx expression and function has been implicated in several diseases, ranging from cancer to immunological disorders and congenital abnormalities, positioning it as a promising therapeutic target. Despite these advances, important gaps remain in our understanding of Dx substrates, molecular mechanisms, and their full spectrum of physiological and pathological roles. Future research will be crucial to uncovering the broader biology of DTX family proteins and enabling their clinical application as diagnostic and prognostic markers. This review consolidates current knowledge and emerging insights on Dx, providing a framework to guide future research and therapeutic exploration.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":" ","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13658767/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148497045","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 to: Knockdown of Foxg1 in supporting cells increases the trans‑differentiation of supporting cells into hair cells in the neonatal mouse cochlea.","authors":"Shasha Zhang, Yuan Zhang, Ying Dong, Lingna Guo, Zhong Zhang, Buwei Shao, Jieyu Qi, Han Zhou, Weijie Zhu, Xiaoqian Yan, Guodong Hong, Liyan Zhang, Xiaoli Zhang, Mingliang Tang, Chunjie Zhao, Xia Gao, Renjie Chai","doi":"10.1007/s00018-026-06289-9","DOIUrl":"10.1007/s00018-026-06289-9","url":null,"abstract":"","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":"83 1","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13379533/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148469267","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":"Upregulation of PTPRO by WT1 alleviates podocyte injury in diabetic nephropathy through inhibiting the c-Abl/p53 pathway.","authors":"Hengjiang Guo, Li Wang, Yiru Tong, Yan Jiang, Xingmei Yao, Limin Lu, Rong Wei","doi":"10.1007/s00018-026-06343-6","DOIUrl":"10.1007/s00018-026-06343-6","url":null,"abstract":"<p><p>Podocyte injury plays a central role in the pathogenesis of diabetic nephropathy (DN). Protein tyrosine phosphatase receptor type O (PTPRO) has been implicated in glomerular disease, yet its specific role and regulatory mechanism in DN remain poorly understood. Here, we demonstrated that PTPRO expression was significantly downregulated in the glomeruli of DN mice and patients with DN, as well as in cultured podocytes exposed to diabetic stressors. Functional studies revealed that Ptpro knockdown induced podocyte injury, characterized by reduced Nephrin and Podocin expression, increased apoptosis, actin cytoskeleton disruption, enhanced migration, and reduced adhesion. Conversely, PTPRO overexpression ameliorated high glucose (HG)-induced podocyte damage. Mechanistically, PTPRO interacted with and dephosphorylated c-Abl, thereby suppressing the c-Abl/p53 signaling pathway. Pharmacological activation of c-Abl abolished the protective effects of PTPRO. Furthermore, we identified PTPRO as a direct transcriptional target of WT1, a podocyte master transcription factor downregulated in DN. WT1 overexpression restored PTPRO expression, suppressed c-Abl/p53 signaling, and ameliorated HG-induced podocyte injury in vitro. In vivo, podocyte-specific overexpression of WT1 via adeno-associated virus delivery in db/db mice attenuated proteinuria, glomerulosclerosis, and podocyte foot process effacement, accompanied by restored PTPRO expression and inhibition of the c-Abl/p53 pathway. Collectively, these findings establish that PTPRO functions downstream of WT1 to protect podocytes in DN by suppressing c-Abl/p53 signaling. Targeting the WT1-PTPRO-c-Abl-p53 axis may represent a novel therapeutic strategy for DN.</p>","PeriodicalId":10007,"journal":{"name":"Cellular and Molecular Life Sciences","volume":" ","pages":""},"PeriodicalIF":6.5,"publicationDate":"2026-07-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13658761/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148469279","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}