PLoS Pathogens最新文献

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Insect-borne non-enveloped bluetongue virus utilizes discrete small vesicles for non-lytic release and cell-to-cell transmission. 昆虫传播的非包膜蓝舌病病毒利用离散的小囊泡进行非溶性释放和细胞间传播。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 DOI: 10.1371/journal.ppat.1013582
Weining Wu, Ulrike Laugks, Kay Grünewald, Polly Roy
{"title":"Insect-borne non-enveloped bluetongue virus utilizes discrete small vesicles for non-lytic release and cell-to-cell transmission.","authors":"Weining Wu, Ulrike Laugks, Kay Grünewald, Polly Roy","doi":"10.1371/journal.ppat.1013582","DOIUrl":"https://doi.org/10.1371/journal.ppat.1013582","url":null,"abstract":"<p><p>Bluetongue virus (BTV) is one of the most economically relevant orbiviruses and is the only example of a large complex, but non-enveloped arbovirus. In addition to cell lysis, BTV is known to employ a 'budding' process analogous to that used by enveloped viruses for cell exit, in which the viral glycosylated NS3 protein plays a key role. Recent reports have demonstrated that BTV can also induce non-lytic release via extracellular vesicles (EVs), however, details of the type and origin of the EV used and the role of NS3 in the process remain incompletely understood. In this study we undertook biochemical studies on the non-lytic release of BTV particles in different forms of EVs from several types of host cells and complemented this by comprehensive microscopic analyses using fluorescence microscopy, transmission electron microscopy and electron cryo-tomography. We discovered that BTV particles use both large EVs (LEVs) and smaller size EVs (SEVs) for non-lytic release and that, in each cell type studied, SEV fractions were particularly enriched with NS3. Non-enveloped BTV particles initially released in SEVs were highly infectious and promote efficient cell-to-cell transmission. This discovery highlights the complex mechanisms utilized by a non-enveloped arbovirus for egress and the significance of different EV types in this process.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013582"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259480","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Vimig: The virus-induced migrasome as a novel mechanism for viral transmission and communication. Vimig:病毒诱导的迁移体是一种新的病毒传播和交流机制。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013557
Mingyan Feng, Leiliang Zhang
{"title":"Vimig: The virus-induced migrasome as a novel mechanism for viral transmission and communication.","authors":"Mingyan Feng, Leiliang Zhang","doi":"10.1371/journal.ppat.1013557","DOIUrl":"10.1371/journal.ppat.1013557","url":null,"abstract":"<p><p>Vimig, defined as \"virus-induced migrasome,\" represents a novel class of extracellular vesicles that originate from virus-infected cells. The mechanisms underlying vimig formation involve actin remodeling and upregulation of phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2). Vimig not only encapsulates viral particles but also aids in the transport of damaged organelles, including mitochondria, thereby contributing to cellular homeostasis and potentially enhancing viral spread and infection. Characterized by their unique contents, which includes viral particles, lipids, proteins, and cellular debris, vimig serves as a transmission route for viruses, possibly allowing them to evade host immune responses. This pearl summarizes the biogenesis, functional significance, and implications of vimig in viral pathogenesis, emphasizing its potential as a target for therapeutic interventions aimed at mitigating viral infections. Understanding the role of vimig may pave the way for novel strategies in clinical drug development and deepen our insights into virus-host interactions.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013557"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12510583/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259630","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Murine leukemia virus glycoGag antagonizes SERINC5 via ER-phagy receptor RETREG1. 小鼠白血病病毒糖gag通过er吞噬受体RETREG1拮抗SERINC5。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013023
Iqbal Ahmad, Jing Zhang, Rongrong Li, Wenqiang Su, Weiqi Liu, You Wu, Ilyas Khan, Xiaomeng Liu, Lian-Feng Li, Sunan Li, Yong-Hui Zheng
{"title":"Murine leukemia virus glycoGag antagonizes SERINC5 via ER-phagy receptor RETREG1.","authors":"Iqbal Ahmad, Jing Zhang, Rongrong Li, Wenqiang Su, Weiqi Liu, You Wu, Ilyas Khan, Xiaomeng Liu, Lian-Feng Li, Sunan Li, Yong-Hui Zheng","doi":"10.1371/journal.ppat.1013023","DOIUrl":"10.1371/journal.ppat.1013023","url":null,"abstract":"<p><p>Serine incorporator 5 (SERINC5) is a host restriction factor that inhibits the infectivity of certain enveloped viruses, including human immunodeficiency virus type 1 (HIV-1) and murine leukemia virus (MLV), by incorporating into the viral envelope and blocking viral entry. To counteract this, HIV-1 and MLV encode accessory proteins-Nef and glycoGag, respectively-that downregulate SERINC5 expression in producer cells. Here, we demonstrate that glycoGag employs more complex and effective mechanisms than Nef to antagonize SERINC5. Despite being a type II integral membrane protein, glycoGag primarily localizes to the cytoplasm, while Nef is mainly associated with the plasma membrane. Additionally, glycoGag is rapidly degraded by proteasomes, in contrast to the greater stability of Nef, and becomes stabilized after binding to SERINC5. While both proteins downregulate SERINC5 at the cell surface, glycoGag also targets SERINC5 at the endoplasmic reticulum (ER). We further show that this ER-specific downregulation is mediated by reticulophagy regulator 1 (RETREG1), an ER-phagy receptor, through micro-ER-phagy. These findings reveal that retroviruses hijack a selective autophagy pathway to counteract host restriction and promote productive infection.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013023"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12530543/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259459","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins. 鸟腺病毒结构:在缺乏稳定蛋白的情况下具有高度热稳定性的衣壳。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013553
Marta Pérez-Illana, Anna Schachner, Mercedes Hernando-Pérez, Gabriela N Condezo, Alberto Paradela, Marta Martínez, Roberto Marabini, Michael Hess, Carmen San Martín
{"title":"Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins.","authors":"Marta Pérez-Illana, Anna Schachner, Mercedes Hernando-Pérez, Gabriela N Condezo, Alberto Paradela, Marta Martínez, Roberto Marabini, Michael Hess, Carmen San Martín","doi":"10.1371/journal.ppat.1013553","DOIUrl":"10.1371/journal.ppat.1013553","url":null,"abstract":"<p><p>High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, the poultry pathogen fowl adenovirus serotype 4 (FAdV-C4). FAdV-C4 virions are highly thermostable, despite lacking minor coat and core proteins shown to stabilize the mast- and atadenovirus particles, having no genus-specific cementing proteins, and packaging a 25% longer genome. Unique structural features of the FAdV-C4 hexon include a large insertion at the trimer equatorial region, and a long N-terminal tail. Protein IIIa conformation is closer to atadenoviruses than to mastadenoviruses, while protein VIII diverges from all previously reported structures. We interpret these differences in light of adenovirus evolution. Finally, we discuss the possible role of core composition in determining capsid stability properties. These results enlarge our view on the structural diversity of adenoviruses, and provide useful information to counteract fowl pathogens or use non-human adenoviruses as vectors.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013553"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12517501/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259388","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
"Pour some sugar on me"-Environmental Candida albicans isolates and the evolution of increased pathogenicity and antifungal resistance through sugar adaptation. “给我倒点糖”——环境白色念珠菌分离株和通过糖适应而增加的致病性和抗真菌耐药性的进化。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013542
Theresa Lange, Jakob L Sprague, Raghav Vij, Raquel Alonso-Roman, Nadja Jablonowski, Silvia Radosa, Thomas Krüger, Olaf Kniemeyer, Falk Hillmann, Axel A Brakhage, Stefanie Allert, Sascha Brunke, Bernhard Hube
{"title":"\"Pour some sugar on me\"-Environmental Candida albicans isolates and the evolution of increased pathogenicity and antifungal resistance through sugar adaptation.","authors":"Theresa Lange, Jakob L Sprague, Raghav Vij, Raquel Alonso-Roman, Nadja Jablonowski, Silvia Radosa, Thomas Krüger, Olaf Kniemeyer, Falk Hillmann, Axel A Brakhage, Stefanie Allert, Sascha Brunke, Bernhard Hube","doi":"10.1371/journal.ppat.1013542","DOIUrl":"10.1371/journal.ppat.1013542","url":null,"abstract":"<p><p>Candida albicans is an opportunistic fungal pathogen that colonizes mucosal surfaces of most humans. Only in rare cases, C. albicans isolates are found in the environment. This study investigated whether environmental isolates differ in their virulence potential from clinical strains and how adaptation to a human diet influences key virulence attributes. We examined three C. albicans isolates from oak trees in the United Kingdom, and observed that one exhibited high host cell damage, increased hypha formation, invasion capacity, and candidalysin production, along with an intrinsic resistance to amphotericin B. The other two showed lower virulence which was still similar to most tested clinical isolates. All oak tree isolates showed an increased resistance to fluconazole. To mimic the more recent evolution of C. albicans to a sugar-rich diet, we evolved a low-damaging isolate in sugar-rich medium, which unexpectedly enhanced its metabolic flexibility, epithelial damage potential, and antifungal resistances, including a new resistance to amphotericin B. These findings suggest that C. albicans isolates can develop high virulence potential and antifungal resistance in the environment, and that adaptation of C. albicans to sugar-rich diets, as in westernized countries, can affect fungal pathogenicity and drug resistance.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013542"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12510538/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259483","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Correction: IRF6 controls Epstein-Barr virus (EBV) lytic reactivation and differentiation in EBV-infected epithelial cells. 更正:IRF6在eb病毒感染的上皮细胞中控制eb病毒(EBV)裂解再激活和分化。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013564
{"title":"Correction: IRF6 controls Epstein-Barr virus (EBV) lytic reactivation and differentiation in EBV-infected epithelial cells.","authors":"","doi":"10.1371/journal.ppat.1013564","DOIUrl":"10.1371/journal.ppat.1013564","url":null,"abstract":"<p><p>[This corrects the article DOI: 10.1371/journal.ppat.1013236.].</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013564"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12510547/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259444","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Avian leukosis virus subgroup J evades innate immunity by activating miR-155 to dually target TRAF3 and STAT1. 禽白血病病毒J亚群通过激活miR-155双重靶向TRAF3和STAT1来逃避先天免疫。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013552
Xinyue Zhang, Defang Zhou, Jing Zhou, Xiaoyang Liu, Longying Ding, Tianxing Yan, Mengyuan Shi, Shuhai He, Ziqiang Cheng
{"title":"Avian leukosis virus subgroup J evades innate immunity by activating miR-155 to dually target TRAF3 and STAT1.","authors":"Xinyue Zhang, Defang Zhou, Jing Zhou, Xiaoyang Liu, Longying Ding, Tianxing Yan, Mengyuan Shi, Shuhai He, Ziqiang Cheng","doi":"10.1371/journal.ppat.1013552","DOIUrl":"10.1371/journal.ppat.1013552","url":null,"abstract":"<p><p>Avian leukosis virus subgroup J (ALV-J) causes immunosuppression and myelocytomas in poultry. While ALV-J evades innate immunity to sustain infection, the mechanisms remain unclear. Here, we show that ALV-J upregulates microRNA-155 (miR-155) to suppress type I interferon (IFN-I) responses, facilitating viral replication. Mechanistically, the ALV-J p27 protein reduced DEAD-box helicase 3X (DDX3X) promoter activity, repressing its expression and promoting MIR155 host gene (MIR155HG) processing into mature miR-155. miR-155 directly targets the tumor necrosis factor receptor-associated factor 3 (TRAF3) and the signal transducer and activator of transcription 1 (STAT1), both of which are key regulators of IFN-I response. Silencing TRAF3 or STAT1 rescues ALV-J replication suppressed by miR-155 inhibition. These findings reveal a novel miRNA-mediated innate immune evasion strategy employed by ALV-J, enhancing our understanding of retroviral pathogenesis.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013552"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12510514/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Reoviruses hijack the SMARCB1-MYC transcriptional regulation complex to activate autophagy for persistent viral infection in leafhopper vector. 呼肠孤病毒劫持SMARCB1-MYC转录调控复合体激活叶蝉载体持续病毒感染的自噬。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-09 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013569
Hui Wang, Runfa Liu, Guangming Xiao, Yanan Li, Bozhong Li, Qian Chen, Taiyun Wei
{"title":"Reoviruses hijack the SMARCB1-MYC transcriptional regulation complex to activate autophagy for persistent viral infection in leafhopper vector.","authors":"Hui Wang, Runfa Liu, Guangming Xiao, Yanan Li, Bozhong Li, Qian Chen, Taiyun Wei","doi":"10.1371/journal.ppat.1013569","DOIUrl":"10.1371/journal.ppat.1013569","url":null,"abstract":"<p><p>Autophagy plays a crucial role in virus-host interactions, as viral components and particles can be degraded by the host's autophagic machinery. Additionally, some viruses can hijack autophagy for their own benefit. However, the mechanisms underlying the transcriptional regulation of autophagy by arboviruses in insect vectors remain largely unexplored. In this study, we found that rice dwarf virus (RDV) infection activates the autophagy pathway in the leafhopper vector, Nephotettix cincticeps, and this autophagy activation also facilitates viral infection in the leafhopper. We identified that MYC transcription factor regulates the expression of autophagy proteins ATG5 and ATG8 by directly targeting their promoters. A transcription regulator SMARCB1 binds to MYC and impedes its recognition of the ATG5 and ATG8 promoters, thus negatively regulating their expression. Moreover, NcSMARCB1 negatively regulates ATG5 expression by directly binding to its promoter. RDV major outer capsid protein P8 blocks the nuclear translocation of SMARCB1, disrupting the SMARCB1-MYC interaction and thereby relieving the transcriptional inhibition of ATG5 and ATG8, which leads to autophagy activation. Furthermore, major outer capsid protein P8 of rice gall dwarf virus (RGDV), same to RDV belonging to plant reoviruses, also interacts with SMARCB1 in leafhopper Recilia dorsalis, preventing its nuclear translocation. Similarly, suppression of SMARCB1 expression enhances autophagy formation and promotes RGDV infection. These findings highlight the critical role of insect vector SMARCB1 and MYC in regulating autophagy in response to arbovirus infection.</p>","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013569"},"PeriodicalIF":4.9,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12510602/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145259428","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Regulation of arbuscular mycorrhiza development by environmental stimuli: Many roads lead to strigolactones. 环境刺激对丛枝菌根发育的调节:许多途径通向独角酯内酯。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-08 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013555
Kees Buhrman, Caroline Gutjahr
{"title":"Regulation of arbuscular mycorrhiza development by environmental stimuli: Many roads lead to strigolactones.","authors":"Kees Buhrman, Caroline Gutjahr","doi":"10.1371/journal.ppat.1013555","DOIUrl":"10.1371/journal.ppat.1013555","url":null,"abstract":"","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013555"},"PeriodicalIF":4.9,"publicationDate":"2025-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12507211/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145253335","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Promiscuity and specificity in ligand sensing by plant cell surface receptors. 植物细胞表面受体对配体感知的混杂性和特异性。
IF 4.9 1区 医学
PLoS Pathogens Pub Date : 2025-10-08 eCollection Date: 2025-10-01 DOI: 10.1371/journal.ppat.1013548
Christina E Steidele, Julien Gronnier, Martin Stegmann, Ralph Hückelhoven, Martina K Ried-Lasi
{"title":"Promiscuity and specificity in ligand sensing by plant cell surface receptors.","authors":"Christina E Steidele, Julien Gronnier, Martin Stegmann, Ralph Hückelhoven, Martina K Ried-Lasi","doi":"10.1371/journal.ppat.1013548","DOIUrl":"10.1371/journal.ppat.1013548","url":null,"abstract":"","PeriodicalId":48999,"journal":{"name":"PLoS Pathogens","volume":"21 10","pages":"e1013548"},"PeriodicalIF":4.9,"publicationDate":"2025-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12507258/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145253337","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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