Cellular signalling最新文献

{"title":"RBM39 silence suppresses esophageal cancer proliferation and metastasis via FANCD2 mRNA destabilization.","authors":"Xin Yang, Chunyang Li, Chu Zhang, Liwen Zhang, Wei Wei, Mei Ji, Bo Jiang","doi":"10.1016/j.cellsig.2025.112047","DOIUrl":"10.1016/j.cellsig.2025.112047","url":null,"abstract":"<p><p>Esophageal cancer (ESCA) is a lethal malignancy with limited therapeutic options and poor survival outcomes. Here, we identify RBM39 as a novel oncoprotein that drives ESCA progression through post-transcriptional stabilization of Fanconi anemia, complementation group D2 (FANCD2) mRNA. RNA-binding motif protein 39 (RBM39) is significantly upregulated in ESCA tissues and cell lines, and its high expression correlates with poor overall survival (OS) and disease-free survival (DFS) in clinical cohorts. Functional studies demonstrate that RBM39 knockdown suppresses proliferation, migration, and invasion in ESCA cells (TE-1, TE-12) in vitro and impairs tumor growth and pulmonary metastasis in xenograft models. Mechanistically, RBM39 directly binds the 3' untranslated regions (3'-UTR) of FANCD2 mRNA (validated by RIP-qPCR and motif mutagenesis), extending its half-life (actinomycin D assay). ESCA transcriptomic profiling of TCGA database links RBM39 to the Fanconi anemia DNA repair pathway, with FANCD2 as its top target. Critically, FANCD2 overexpression rescues oncogenic phenotypes upon RBM39 silencing, restoring tumorigenesis in vivo. These findings establish the RBM39-FANCD2 axis as a therapeutic vulnerability, where targeting the RBM39-FANCD2 axis may offer a promising therapeutic strategy for the ESCA clinical treatment.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112047"},"PeriodicalIF":3.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144768465","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":"ACSS3 protein macromolecule regulates glycolysis in keloid through Wnt/β-catenin signaling pathway: Bioinformatics, machine learning, and experimental validation.","authors":"Pingping Huo, Sujie Wang, Zhouna Li, Zhehu Jin","doi":"10.1016/j.cellsig.2025.112056","DOIUrl":"10.1016/j.cellsig.2025.112056","url":null,"abstract":"<p><p>Keloids are fibroproliferative lesions resulting from abnormal wound healing, characterized by the excessive growth and metabolic reprogramming of keloid fibroblasts (KFs). The underlying mechanisms responsible for these metabolic abnormalities remain under debate. This research employed comprehensive bioinformatics techniques to pinpoint ACSS3 (Acetyl-CoA Synthetase Short-Chain Family Member 3) and the Wnt/β-Catenin pathway as pivotal contributors to keloid pathogenesis. ACSS3, a mitochondrial protein involved in metabolic regulation, is downregulated in keloid. Lentiviral transfection-induced overexpression of ACSS3 suppressed KFs activity, normalized glycolytic flux, and reduced the levels of critical glycolytic enzymes. Conversely, ACSS3 knockdown elicited opposite effects, which were reversed by ICG-001. Single-cell analysis demonstrates that fibroblasts are the primary cell type involved in the fibrotic process. An ACSS3 regulatory network was developed. Additionally, Molecular docking and dynamics simulations were conducted to identify potential drugs targeting ACSS3. In summary, this study demonstrates that ACSS3 modulates aerobic glycolysis and the activity of KFs via the Wnt/β-Catenin pathway, positioning ACSS3 as a promising therapeutic target for keloid treatment.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112056"},"PeriodicalIF":3.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144811861","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":"ALDH2 inhibits angiogenesis in esophageal squamous cell carcinoma by suppressing the NOTCH1/PI3K/Akt signaling pathway.","authors":"Jingchao Qiang, Tian Qiu, Yongliang Yang, Baoshi Xu, Hongyu Huang, Xinran Li, Rui Ma, Yingzhi Lu, Zibo Dong","doi":"10.1016/j.cellsig.2025.112025","DOIUrl":"10.1016/j.cellsig.2025.112025","url":null,"abstract":"<p><p>Esophageal Squamous Cell Carcinoma (ESCC) stands as the predominant form of esophageal cancer globally, bearing high morbidity and mortality rates attributed to its capacity for infiltration and metastasis. Angiogenesis emerges as a pivotal factor influencing ESCC progression. To explore how to modulate angiogenesis for anti-ESCC therapy effectively, here we evaluated the potential of acetaldehyde dehydrogenase 2 (ALDH2) as a targeted therapy for ESCC and elucidated the molecular mechanisms by which ALDH2 inhibits ESCC angiogenesis. Our findings reveal a correlation between low ALDH2 expression and the progression as well as poor prognosis of ESCC. Additionally, ESCC cell apoptosis was stimulated while ESCC cell proliferation, migration, invasion, and angiogenesis were all successfully suppressed by ALDH2 overexpression. Regarding the molecular mechanism, ALDH2 was observed to suppress NOTCH1, which in turn inhibited the PI3K/Akt pathway, thereby hindering the expression of hypoxia-inducible factor-1α (HIF-1α) and vascular endothelial growth factor A (VEGFA), which are both linked to angiogenesis, and ultimately exerting its inhibitory effect on ESCC through this regulatory cascade. Importantly, we established a subcutaneous xenograft tumor model in BALB/c nude mice using ESCC cell lines with ALDH2 overexpression. Our results demonstrated that ALDH2 overexpression significantly inhibited tumor growth and angiogenesis, further supporting ALDH2 as a potential therapeutic target in ESCC. Finally, we screened Tectoridin (TEC), an agonist of ALDH2, and demonstrated its ability to inhibit ESCC. These findings provide an empirical basis for the development of novel therapeutic strategies for ESCC.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112025"},"PeriodicalIF":3.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144741342","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":"Post-translational modifications of Stat3: The state of the art.","authors":"Jiaxu Chen, Caiyun Mao, Ning Han, Qi Zhou, Chenhao Feng, Xutao Sun, Yunjia Song","doi":"10.1016/j.cellsig.2025.112048","DOIUrl":"10.1016/j.cellsig.2025.112048","url":null,"abstract":"<p><p>Signal transducer and activator of transcription 3 (Stat3), a critical transcription factor, plays an essential role in cellular processes such as proliferation, development, and differentiation. It also significantly contributes to the pathogenesis of cardiovascular diseases and various cancers, including breast cancer, pancreatic cancer, and renal cell carcinoma. The functional dynamics of Stat3 are intricately regulated by post-translational modifications (PTMs) such as phosphorylation, sulfenylation, acetylation, sulfhydrylation, and SUMOylation. These modifications, triggered by pathophysiological signals, induce structural changes in Stat3 across different cell types, thereby regulating distinct gene expression programs. Such modifications can either enhance or inhibit Stat3's transcriptional activity and affect its DNA-binding stability. This review explores the various PTMs that modulate Stat3 function, offering a comprehensive analysis of the regulatory mechanisms that govern Stat3 within cellular signaling networks. The findings are expected to provide valuable insights into the development of novel therapeutic agents targeting these pathways, ultimately revealing new targets and innovative strategies for treating a range of diseases.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112048"},"PeriodicalIF":3.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144793526","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":"TRIM10β upregulation promotes microtubule destabilization and triggers proteotoxic stress.","authors":"Heesoo Kim, Wonji Shin, Byunghoon Jeon, Sungwook Lee, Boyoun Park","doi":"10.1016/j.cellsig.2025.112052","DOIUrl":"10.1016/j.cellsig.2025.112052","url":null,"abstract":"<p><p>Microtubule stability is critical for maintaining cytoskeletal integrity and is finely tuned by post-translational modifications of tubulin and its associated regulatory factors. However, it remains unclear how microtubules become destabilized under stress or disease conditions and contribute to pathogenesis. Here, we identify TRIM10β, a previously uncharacterized splice variant of TRIM10, as a microtubule-associated protein that disrupts the interaction between tubulin and End Binding protein 1 (EB1), which plays a critical role in microtubule stabilization. Moreover, TRIM10β promotes tubulin SUMOylation and cleavage of LIM domain kinase 1 (LIMK1), both of which contribute to microtubule destabilization. TRIM10β binds to calmodulin-regulated spectrin-associated protein 2 (CAMSAP2), a key regulator of non-centrosomal microtubules, and modulates its protein levels via its E3 ligase activity. Notably, TRIM10β depletion attenuates p38 phosphorylation in erythroblasts, which is essential for microtubule disassembly and polarization during enucleation, whereas its ectopic expression aberrantly enhances p38 activity, promoting microtubule disassembly in non-erythroid cells. Importantly, persistent overexpression of TRIM10β is recognized as a proteotoxic burden and rapidly degraded via the unfolded protein response (UPR) under cellular stress, thereby serving as a protective mechanism. Our findings reveal a novel role for TRIM10β in microtubule dynamics and highlight a potential regulatory mechanism in maintaining proteostasis, with its low endogenous expression possibly reflecting an evolutionary strategy to minimize proteostatic stress.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112052"},"PeriodicalIF":3.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144803680","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":"Kindlin-1 promotes mitophagy by inhibiting PINK1 degradation to enhance hepatocellular carcinoma progression and modulates sensitivity to donafenib.","authors":"Huaxing Ma, Guangling Ou, Bibo Wu, Hongwei Ding, Yijie Zhang, Fei Xia, Zixuan Shen, Kunyang Zhao, Chaochun Chen, Long Wu, Jin Lei, Yuan Xu, Xueke Zhao, Kun Cao, Haiyang Li","doi":"10.1016/j.cellsig.2025.112032","DOIUrl":"10.1016/j.cellsig.2025.112032","url":null,"abstract":"<p><p>Mitophagy, essential for mitochondrial homeostasis, may affect hepatocellular carcinoma (HCC) progression and drug sensitivity, though its precise role remains unclear. Kindlin-1 is an adhesion protein which can regulate the function of integrins, resulting in an aggressive phenotype in certain solid malignant tumors.This study explored the clinical significance and cellular functions of Kindlin-1 in HCC. The role of Kindlin-1 in HCC progression was assessed, along with its effects on mitophagy and sensitivity to donafenib. Its impact on HCC cell proliferation and metastasis was analyzed using CCK8, colony formation, EdU incorporation, flow cytometry, Immunohistochemistry, Transwell assays, wound healing assays, and subcutaneous tumorigenesis in nude mice. The interactions of Kindlin-1 with other proteins and its main functions and pathways were investigated through RNA sequencing, enrichment analysis, immunohistochemical co-localization, Co-IP and mass spectrometry. Additionally, the effects of Kindlin-1 on PINK1 stability and mitophagy were evaluated, and the impact of Kindlin-1 inhibition on donafenib sensitivity was tested in vitro and in vivo. Kindlin-1 was found to be highly expressed in HCC tissues and correlated with a poor prognosis. Kindlin-1 promotes mitophagy by stabilizing full-length PINK1 and prevents ubiquitin induced degradation of PINK1 by interacting with it, thus promoting HCC cell proliferation. Inhibition of Kindlin-1 expression or mitophagy synergistically enhances the anti-tumor effects of donafenib in vitro and in xenograft mouse models. Our study demonstrates that Kindlin-1 significantly influences HCC progression by regulating mitophagy through the PINK1/Parkin pathway. Inhibiting Kindlin-1 may represent a promising therapeutic strategy to enhance the efficacy of donafenib, thereby providing novel insights into improving treatment outcomes for HCC patients.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112032"},"PeriodicalIF":3.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144759294","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":"Elevated P4HB expression in hepatocellular carcinoma and its role in UCA1-mediated malignant progression.","authors":"Song Huang, Yuehong Cai, Xueqing Zhao, Xiaohong Du, Haijun Hu","doi":"10.1016/j.cellsig.2025.112131","DOIUrl":"https://doi.org/10.1016/j.cellsig.2025.112131","url":null,"abstract":"<p><p>Hepatocellular carcinoma (HCC) is a leading cause of cancer-related mortality worldwide, underscoring the urgent need for improved diagnostic and therapeutic strategies. In this study, we investigated the role of Prolyl 4-hydroxylase subunit beta (P4HB) in HCC progression and its potential as a diagnostic biomarker. Single-cell sequencing analysis revealed that P4HB is highly expressed in malignant HCC cell populations. Serum analysis demonstrated that P4HB levels were significantly elevated in HCC patients compared to healthy controls and those with benign liver diseases, with ROC analysis showing a high diagnostic performance, particularly when combined with alpha-fetoprotein (AFP). Functional assays, both in vitro and in vivo, confirmed that P4HB promotes the proliferation, migration, and invasion of HCC cells. Furthermore, we identified a novel interaction between P4HB and the lncRNA UCA1, which enhances glycolysis and malignant behavior in HCC cells. These findings suggest that P4HB is a promising biomarker for HCC diagnosis and a potential therapeutic target, particularly in the context of its interaction with UCA1.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112131"},"PeriodicalIF":3.7,"publicationDate":"2025-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145058313","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":"Hispolon reduces mitochondrial dysfunction and improves fibrosis of diabetes nephropathy by activating AMPK signal and inhibiting mPTP opening.","authors":"Yapeng Wang, Ajau Danis, Xueyi Wang, Jia Ren, Teng Ma, Ruixiao Wang","doi":"10.1016/j.cellsig.2025.112130","DOIUrl":"https://doi.org/10.1016/j.cellsig.2025.112130","url":null,"abstract":"<p><p>Diabetic nephropathy progression is linked to the AMPK/SIRT1/PGC-1α signaling pathway. Hispolon's potential in improving mitochondrial function and treating diabetic nephropathy via this pathway was unclear. This study used db/db mice and high glucose-induced SV40 MES 13 cells to explore Hispolon's renoprotective mechanisms. In vivo, db/db mice showed glomerular damage, collagen deposition, glycoprotein accumulation, and elevated serum creatinine and urea nitrogen. Hispolon intervention improved these features and parameters. It reduced renal MDA levels, enhanced SOD activity, suppressed pro-inflammatory mediators, and downregulated fibrosis markers. Western blot analysis showed Hispolon restored p-AMPK, SIRT1, and PGC-1α protein levels. In vitro, Hispolon enhanced cell viability, inhibited apoptosis, and reversed high glucose-induced oxidative stress and inflammation in SV40 MES 13 cells. It improved mitochondrial energy metabolism by restoring mitochondrial membrane potential, increasing ATP production, and inhibiting abnormal mPTP opening. Mechanistic studies confirmed that the AMPK/SIRT1/PGC-1α signaling cascade is key for Hispolon's regulation of mPTP dynamics. In conclusion, Hispolon slows diabetic nephropathy progression by activating the AMPK/SIRT1/PGC-1α pathway, inhibiting mPTP opening, and improving mitochondrial dysfunction.</p>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":" ","pages":"112130"},"PeriodicalIF":3.7,"publicationDate":"2025-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145058302","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":"Targeting ferroptosis in cervical cancer: Mechanistic insights and therapeutic opportunities","authors":"Shunji An ,&nbsp;Anna Han ,&nbsp;Zhenhua Lin ,&nbsp;Haiyan Quan","doi":"10.1016/j.cellsig.2025.112122","DOIUrl":"10.1016/j.cellsig.2025.112122","url":null,"abstract":"<div><div>Cervical cancer is the fourth most common malignancy among women worldwide. Despite standard chemoradiotherapy, a significant number of patients experience recurrence or distant metastasis. Accumulating evidence highlights ferroptosis—an iron-dependent form of regulated cell death driven by lipid peroxidation (LPO)—as a key mechanism influencing cervical carcinogenesis and treatment outcomes. Ferroptosis is marked by intracellular iron overload, excessive reactive oxygen species (ROS) production, and loss of redox balance. This review provides a comprehensive overview of the emerging roles of ferroptosis in the initiation, progression, and therapeutic resistance of cervical cancer. We outline the regulatory networks and signaling pathways that control ferroptosis in cervical cancer cells and assess the therapeutic potential of inducing ferroptosis using small-molecule compounds and nanomedicine approaches. Additionally, we discuss the prognostic value of ferroptosis-related genes (FRGs), their association with immune infiltration, and their implications for personalized immunotherapy. Collectively, these insights emphasize the translational promise of targeting ferroptosis as a novel strategy for precision oncology and targeted therapy in cervical cancer.</div></div>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":"136 ","pages":"Article 112122"},"PeriodicalIF":3.7,"publicationDate":"2025-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145045753","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":"Tenvermectin B, a novel macrocyclic lactone antibiotic, suppresses glioblastoma progression by targeting RhoJ","authors":"Chenyi Nie ,&nbsp;Hongsheng Liang ,&nbsp;Jiaxin Zhou ,&nbsp;Hefei Liu ,&nbsp;Ruiqiang Shang ,&nbsp;Hongge Yang ,&nbsp;Wang Jiang ,&nbsp;Huan Qi ,&nbsp;Jidong Wang ,&nbsp;Aili Gao","doi":"10.1016/j.cellsig.2025.112117","DOIUrl":"10.1016/j.cellsig.2025.112117","url":null,"abstract":"<div><h3>Background</h3><div>The migratory and invasive behavior of glioblastoma (GBM) poses significant challenges for treatment, and the underlying mechanisms require further exploration. While macrolide antibiotics exhibit antitumor activity, the antitumor effects and molecular mechanisms of the novel macrolide TVM B remain unclear. This study aimed to investigate its efficacy against GBM and elucidate the mechanisms by which it modulates GBM cell migration and invasion.</div></div><div><h3>Methods</h3><div>First, the cytotoxicity of TVM B was evaluated using the MTT assay. In vivo, a xenograft mouse model was established, and the drug was administered via intraperitoneal injection. Western blot and pathological staining were performed to investigate the effects of TVM B on tumor growth. Used RNA-seq data to explore its potential mechanism of action, and performed molecular docking to identify potential targets. In vitro validation experiments included the wound healing assay, Transwell migration and invasion assays, Tube formation Assay, RT-qPCR, Western blot, flow cytometry for apoptosis detection, and immunofluorescence staining.</div></div><div><h3>Results</h3><div>In vitro, TVM B inhibited GBM cells proliferation, induced apoptosis, and suppressed migration and invasion. TVM B abrogated the angiogenic capacity of HUVECs. In vivo xenograft experiments showed that TVM B treatment reduced Ki67 positivity, decreased the expression of MMP9, MMP2, and p-FAK in tumor tissues, and HE staining of various organs revealed no obvious toxicity. Mechanistic studies showed TVM B regulated RhoJ to inhibit cytoskeletal dynamics and FAK/Src signaling, thereby suppressing cell migration and invasion via focal adhesion modulation.</div></div><div><h3>Conclusion</h3><div>This study for the first time demonstrates that TVM B regulates cytoskeletal homeostasis via RhoJ, inhibits cell proliferation, and affects the FAK/Src pathway to ultimately suppress migration and invasion of GBM cells.</div></div>","PeriodicalId":9902,"journal":{"name":"Cellular signalling","volume":"136 ","pages":"Article 112117"},"PeriodicalIF":3.7,"publicationDate":"2025-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145045754","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}