Phytopathology Research最新文献

How to improve crop pathogen resistance with epigenetics. 如何利用表观遗传学提高作物抗病性。

IF 3.5 2区农林科学

Phytopathology Research Pub Date : 2026-01-01 Epub Date: 2026-01-27 DOI: 10.1186/s42483-025-00393-7

Litsa Ampntelnour, Amelia Burton, Vardis Ntoukakis

{"title":"How to improve crop pathogen resistance with epigenetics.","authors":"Litsa Ampntelnour, Amelia Burton, Vardis Ntoukakis","doi":"10.1186/s42483-025-00393-7","DOIUrl":"https://doi.org/10.1186/s42483-025-00393-7","url":null,"abstract":"Crop losses due to pathogens are a critical global challenge threatening food security and agricultural sustainability. Recent advances in plant science have highlighted the role of epigenetic regulation in plant immunity. This review examines current insights into how plants utilize epigenetic modifications, focusing on histone modifications, DNA methylation changes, and chromatin remodelling, to modulate defence gene expression and adapt to biotic stress. We explore how histone modifications influence both basal and induced immune responses through key enzymes and we examine the dual roles of DNA methylation in transcriptional activation and repression. Additionally, the review discusses ATP-dependent chromatin remodelling complexes and non-coding RNA to highlight their contribution in fine tuning plant immunity. Finally, we discuss emerging technologies involved in epigenome editing and identify the knowledge gaps that must be addressed before translating our findings into making resilient agricultural systems.Supplementary information: The online version contains supplementary material available at 10.1186/s42483-025-00393-7.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"8 1","pages":"5"},"PeriodicalIF":3.5,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12835110/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146093677","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The PP2A-like phosphatase SsPpe1 regulates Ssrot1 to modulate sexual mating and virulence in Sporisorium scitamineum pp2a样磷酸酶SsPpe1通过调控Ssrot1调节甘蔗孢菌的性交配和毒力

2区农林科学

Phytopathology Research Pub Date : 2025-12-18 DOI: 10.1186/s42483-025-00384-8

Jinfeng Qiu, Haoming Wu, Qianyi Wei, Shan Lu, Jiaorong Meng, Ru Li, Baoshan Chen

{"title":"The PP2A-like phosphatase SsPpe1 regulates Ssrot1 to modulate sexual mating and virulence in Sporisorium scitamineum","authors":"Jinfeng Qiu, Haoming Wu, Qianyi Wei, Shan Lu, Jiaorong Meng, Ru Li, Baoshan Chen","doi":"10.1186/s42483-025-00384-8","DOIUrl":"https://doi.org/10.1186/s42483-025-00384-8","url":null,"abstract":"Abstract Protein phosphatase 2A (PP2A) is a heterotrimer enzyme composed of a catalytic subunit (C), a scaffolding subunit (A), and a regulatory subunit (B). PP2A phosphatases play crucial roles in many biological processes, including protein synthesis, cellular signaling, cell cycle regulation, apoptosis, virulence, and stress responses. However, the roles of PP2A in the pathogenic fungi Sporisorium scitamineum remain unclear. In this study, we report the identification of a homologue of PP2A-like phosphatase designated as SsPpe1. We found that Ssppe1 is required for sexual mating/filamentation and virulence in S. scitamineum . Reintroducing the wild-type Ssppe1 allele with its native promoter into the mutant strain restored the wild-type phenotypes. Additionally, the deletion of Ssppe1 resulted in a significant decrease in the transcript levels of the pheromone pathway-related genes. Global transcriptome analysis revealed that SsPpe1 was involved in the intrinsic component of the membrane, oxidoreductase activity, sulfur amino acid biosynthetic process, carbon–carbon lyase activity, and glutamine family amino acid metabolic process. Moreover, Ssppe1 modulated the transcriptional expression of the cell wall integrity-related gene Ssrot1 . Deletion of Ssrot1 resulted in defects in sexual mating and filamentation, as well as reduced virulence. Our results provide insight into the regulatory roles of SsPpe1 in S. scitamineum and contribute to our understanding of the function of the PP2A-like in plant-pathogenic fungi.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-12-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1186/s42483-025-00384-8.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147896440","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The two-component system RstB/RstA regulates virulence through the Fe3+-siderophore transport operon lpfetABC in the poplar canker bacterium Lonsdalea populi RstB/RstA双组分系统通过Fe3+-铁载体转运操纵子lpfetABC调控杨树溃疡病细菌的毒力

2区农林科学

Phytopathology Research Pub Date : 2025-12-02 DOI: 10.1186/s42483-025-00377-7

Sha Zeng, Ruirui Yang, Zexu Ming, Aining Li

{"title":"The two-component system RstB/RstA regulates virulence through the Fe3+-siderophore transport operon lpfetABC in the poplar canker bacterium Lonsdalea populi","authors":"Sha Zeng, Ruirui Yang, Zexu Ming, Aining Li","doi":"10.1186/s42483-025-00377-7","DOIUrl":"https://doi.org/10.1186/s42483-025-00377-7","url":null,"abstract":"Abstract Poplar bacterial canker, caused by Lonsdalea populi , seriously threatens the health of poplar plantations. The two-component system is one of the most important signal transduction pathways in bacteria, playing a crucial role in numerical traits including growth, stress tolerance, and pathogenicity; however, their functions in L. populi remain poorly understood. Here, we identified a two-component system (RstB/RstA) in L. populi . The deletion of either rstB or rstA led to a decrease in L. populi virulence, biofilm formation, and tolerance to H 2 O 2 and iron stresses. Based on transcriptomic data of the rstB or rstA mutants, an electrophoretic mobility shift assay confirmed that RstA directly binds to the promoter of lpfetA . Given that lpfetA , lpfetB , and lpfetC are co-transcribed as an operon, these results suggested that RstA likely regulates the lpfetABC operon. The overexpression of either lpfetA , lpfetB , or lpfetC almost abolished bacterial virulence, while resulted in decreased biofilm formation and tolerance to H 2 O 2 . These findings demonstrated that RstA modulates L. populi virulence, at least in part, by regulating the lpfet operon. Overall, our work indicated that RstB/RstA plays an important role in bacterial virulence and stress tolerance.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1186/s42483-025-00377-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147913033","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1

The p29 silencing suppressor of Cryphonectria hypovirus 1 inhibits dcl2 gene transcription by directly binding to the promoter region cryphonecia hypovirus 1的p29沉默抑制子通过直接结合启动子区抑制dcl2基因转录

2区农林科学

Phytopathology Research Pub Date : 2025-10-08 DOI: 10.1186/s42483-025-00356-y

Shiyu Zhai, Tianxing Pang, Binglei Wang, Shiyu Peng, Ruiling Bian, Huan Ren, Ida Bagus Andika, Liying Sun

{"title":"The p29 silencing suppressor of Cryphonectria hypovirus 1 inhibits dcl2 gene transcription by directly binding to the promoter region","authors":"Shiyu Zhai, Tianxing Pang, Binglei Wang, Shiyu Peng, Ruiling Bian, Huan Ren, Ida Bagus Andika, Liying Sun","doi":"10.1186/s42483-025-00356-y","DOIUrl":"https://doi.org/10.1186/s42483-025-00356-y","url":null,"abstract":"Abstract RNA silencing is an innate immune response against viral infections in eukaryotic organisms. Dicer or dicer-like protein (DCL) is a key component of the RNA silencing pathway for the generation of small interfering RNAs, and its expression is often elevated during viral infections. This upregulation reflects the host cell’s attempt to mount an effective antiviral response. However, viruses have evolved diverse strategies to suppress the host’s RNA silencing responses. Previous studies revealed that the p29 silencing suppressor of the mycovirus Cryphonectria hypovirus 1 (CHV1) suppresses the transcriptional upregulation of the dcl2 gene in its fungal host, Cryphonectria parasitica , but the molecular mechanism underlying this suppression remains unclear. In this study, we observed that like dcl2 in C. parasitica , dcl2 in Fusarium graminearum plays a crucial role in combating CHV1 infection. Moreover, p29 inhibits dcl2 expression in F. graminearum . This was further validated by a dcl2 promoter-driven GFP reporter system used to monitor dcl2 promoter activity. Yeast one-hybrid assay, dot blot protein-DNA binding assay, and electrophoretic mobility shift assay indicated that p29 directly binds to the dcl2 promoter region in C. parasitica and F. graminearum to inhibit dcl2 transcription. In particular, the putative MYB cis- regulatory element sequence in the dcl2 promoter is essential for binding with p29 and the repression of promoter activity by p29. Overall, the results of this study provide a novel example in which a viral RNA silencing suppressor operates at the transcriptional level through DNA–protein interactions.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://phytopatholres.biomedcentral.com/counter/pdf/10.1186/s42483-025-00356-y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147891638","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Selective autophagy limits ‘Candidatus Liberibacter asiaticus’ infection by ATG8 mediated targeting of a virulence effector 选择性自噬通过ATG8介导的毒力效应物靶向限制亚洲自由候选菌的感染

2区农林科学

Phytopathology Research Pub Date : 2025-09-22 DOI: 10.1186/s42483-025-00360-2

Xuejin Cui, Li Ren, Yingzhe Yuan, Yali Wang, Xueyi Li, Siu-Kit Ma, Shimin Fu, Changyong Zhou, Xuefeng Wang

引用次数: 1

A Fusarium graminearum UDP-galactofuranose transporter, FgUgtD, affects cell wall integrity, virulence, and reproduction 谷草镰刀菌udp -半乳糖呋喃糖转运蛋白FgUgtD影响细胞壁完整性、毒力和繁殖

2区农林科学

Phytopathology Research Pub Date : 2025-09-08 DOI: 10.1186/s42483-025-00382-w

Xi Liu, Mengru Wang, Xiaoyu Wang, Fenglin Deng, Zhengwu Fang, Aiguo Gu, Tian Yang, Junliang Yin, Dongfang Ma

{"title":"A Fusarium graminearum UDP-galactofuranose transporter, FgUgtD, affects cell wall integrity, virulence, and reproduction","authors":"Xi Liu, Mengru Wang, Xiaoyu Wang, Fenglin Deng, Zhengwu Fang, Aiguo Gu, Tian Yang, Junliang Yin, Dongfang Ma","doi":"10.1186/s42483-025-00382-w","DOIUrl":"https://doi.org/10.1186/s42483-025-00382-w","url":null,"abstract":"Abstract Fusarium graminearum , the predominant causal agent of Fusarium head blight (FHB) in wheat, severely impacts global food security by reducing crop yields and contaminating grains with health-threatening mycotoxins. Galactofuranose (Galf), a critical cell wall component, is vital for fungal cellular integrity, virulence, and stress tolerance. Notably, the activated form UDP-Galf is synthesized in the cytoplasm but requires translocation to the Golgi lumen, implying the existence of an unidentified transporter. This study identified and characterized FgUgtD, a putative UDP-Galf transporter from F . graminearum belonging to the nucleotide-sugar transporter family. Through subcellular localization, gene knockout, and functional complementation assays, we investigated its role in fungal biology and virulence. FgUgtD localized to the Golgi and endoplasmic reticulum. Its disruption caused severe phenotypic defects: (1) impaired hyphal growth and asexual reproduction, (2) complete loss of ascospore formation, (3) cell wall disorganization with chitin depletion, (4) hypersensitivity to galactose, and (5) > 80% reduction in virulence on wheat and maize—all rescued by genetic complementation. Crucially, the absence of UDP-Galf biosynthesis in plants and animals highlights FgUgtD as a promising antifungal target for controlling FHB.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://phytopatholres.biomedcentral.com/counter/pdf/10.1186/s42483-025-00382-w","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147921433","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Identification of critical interaction sites in the coat protein of Areca palm velarivirus 1 (APV1) and its pathogenicity 槟榔掌velarivirus 1 （APV1）外壳蛋白关键相互作用位点的鉴定及其致病性

2区农林科学

Phytopathology Research Pub Date : 2025-09-08 DOI: 10.1186/s42483-025-00354-0

Rui Meng, Tao Chen, Xiaoyan Feng, Jianhua Wang, Muhammad Zeeshan Hyder, Hongxing Wang, Naitong Yu

{"title":"Identification of critical interaction sites in the coat protein of Areca palm velarivirus 1 (APV1) and its pathogenicity","authors":"Rui Meng, Tao Chen, Xiaoyan Feng, Jianhua Wang, Muhammad Zeeshan Hyder, Hongxing Wang, Naitong Yu","doi":"10.1186/s42483-025-00354-0","DOIUrl":"https://doi.org/10.1186/s42483-025-00354-0","url":null,"abstract":"Abstract Areca palm velarivirus 1 (APV1), a member of the genus Velarivirus (family Closteroviridae ), is an economically significant pathogen associated with yellow leaf disease in Areca palm ( Areca catechu L.), causing substantial declines in both yield and quality decline. The APV1 genome comprises 11 open reading frames (ORFs), with ORF6 and ORF7 encoding the coat protein (CP) and minor coat protein (CPm), respectively. In this study, the interaction between the APV1 CP and CPm proteins was identified by yeast two-hybrid (Y2H) and bimolecular fluorescence complementation (BiFC) assays. To clarify critical interaction sites, a double mutant (CP R211A−R212A ) was generated through site-directed mutagenesis for both Y2H and BiFC analyses. The result demonstrated that these residues were determined to be key amino acid sites. Furthermore, subcellular localization analysis revealed that the CP R211A−R212A mutation did not alter the functional localization of the CP protein in Nicotiana benthamiana leaves, as it remained present in both the nucleus and cytoplasm. The pathogenicity of the APV1 CP protein and its mutant was investigated using the potato virus X (PVX) expression system. Experimental results showed that N. benthamiana plants infected with PVX-CP exhibited severe chlorosis symptoms. Intriguingly, N. benthamiana plants infected with PVX-CP R211A−R212A showed markedly reduced chlorosis. Our findings indicated that the 211 RR 212 residues of APV1 CP are crucial for their interaction with the CPm protein and likely play a key role in the symptom formation. Moreover, this study represents the first identification of APV1 CP as a pathogenic factor, offering new insights into the molecular mechanisms underlying APV1 pathogenicity.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://phytopatholres.biomedcentral.com/counter/pdf/10.1186/s42483-025-00354-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147880746","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Cylindrical inclusion protein of chilli veinal mottle virus promotes elevated viral titers of pod pepper vein yellows virus 辣椒脉斑驳病毒圆柱包涵蛋白促进豆荚椒脉黄病毒滴度升高

2区农林科学

Phytopathology Research Pub Date : 2025-07-22 DOI: 10.1186/s42483-025-00339-z

Shan Bu, Qionglian Wan, Lujia Wang, Shaoxiang Wang, Jian Wu, Yibao Ma, Xiaohan Mo, Fei Yan, Jiejun Peng

引用次数: 2

PMT family mannosyltransferase-mediated protein O-mannosylation is required for the development and pathogenicity of Colletotrichum graminicola PMT家族甘露糖基转移酶介导的蛋白o -甘露糖基化是禾草炭疽菌发育和致病性所必需的

2区农林科学

Phytopathology Research Pub Date : 2025-06-24 DOI: 10.1186/s42483-025-00326-4

Jie Mei, Na Ning, Yan Yang, Shaoqun Zhou, Wende Liu

{"title":"PMT family mannosyltransferase-mediated protein O-mannosylation is required for the development and pathogenicity of Colletotrichum graminicola","authors":"Jie Mei, Na Ning, Yan Yang, Shaoqun Zhou, Wende Liu","doi":"10.1186/s42483-025-00326-4","DOIUrl":"https://doi.org/10.1186/s42483-025-00326-4","url":null,"abstract":"Abstract Protein O-mannosylation in the endoplasmic reticulum (ER) plays a crucial regulatory role in the development and virulence of many phytopathogenic fungi. However, the corresponding biological function and underlying regulatory mechanism mediated by this process in Colletotrichum graminicola , causing the anthracnose disease of maize ( Zea mays ), is unclear. The protein O-mannosyltransferase (PMT) family-mediated protein O-mannosylation is absent in plants, which may provide good targets for developing safe antifungal agents. In the present study, we identified three PMT family mannosyltransferases: CgPMT1, CgPMT2, and CgPMT4 in C. graminicola. The subcellular localization analyses proved that these proteins were located in the ER as previously reported. qRT-PCR results showed that the expression levels of all the three genes were highest in the conidia compared with other developmental stages. Gene knockout analysis demonstrated that the PMT-mediated protein O-mannosylation was essential for the vegetative growth, conidiation, appressorium formation, and pathogenicity of C. graminicola . Immunoprecipitation-Mass Spectrometry (IP-MS) analysis showed that the potential interaction proteins of these CgPMTs were mainly enriched in the pathways of sphingolipid metabolism, autophagy, glycosylphosphatidylinositol (GPI)-anchor modification, and endocytosis. These findings enhanced our understanding of the functions of protein O-mannosylation and provide effective molecular targets for maize disease prevention and control.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://phytopatholres.biomedcentral.com/counter/pdf/10.1186/s42483-025-00326-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147334020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The powdery mildew effector Eae1 targets a SAMS enzyme within the ethylene biosynthesis pathway to disrupt plant immunity 白粉病效应物Eae1靶向乙烯生物合成途径中的SAMS酶来破坏植物免疫

2区农林科学

Phytopathology Research Pub Date : 2025-05-13 DOI: 10.1186/s42483-025-00334-4

Jiaxin Shan, Fan Su, Jinyao Yin, Yuhan Liu, Xuehuan Zhu, Minghao Zuo, Wenbo Liu, Chunhua Lin, Li Xiao, Weiguo Miao

{"title":"The powdery mildew effector Eae1 targets a SAMS enzyme within the ethylene biosynthesis pathway to disrupt plant immunity","authors":"Jiaxin Shan, Fan Su, Jinyao Yin, Yuhan Liu, Xuehuan Zhu, Minghao Zuo, Wenbo Liu, Chunhua Lin, Li Xiao, Weiguo Miao","doi":"10.1186/s42483-025-00334-4","DOIUrl":"https://doi.org/10.1186/s42483-025-00334-4","url":null,"abstract":"Abstract Phytopathogens secrete effector proteins that disrupt plant immunity. Phytohormones, such as ethylene, function as immune signals that regulate plant responses to phytopathogens. However, the mechanisms by which powdery mildew fungi utilize effectors to manipulate ethylene signaling remain poorly understood. This study reports that Eae1, an effector from the powdery mildew fungus Erysiphe quercicola , can reduce ethylene levels and attenuate the immune response in rubber trees ( Hevea brasiliensis ), thereby promoting fungus infection. Notably, Eae1 shares homologs with effectors from other powdery mildew fungi. Our findings indicate that the Eae1 transcription can be induced by enhanced ethylene signaling. Eae1 is translocated to plant chloroplasts, where it destabilizes Hevea brasiliensis S-adenosyl-L-methionine synthetase, a key enzyme in ethylene biosynthesis, leading to reduced ethylene production. The chloroplast-localized protein Toc159/AIG1 (AIG1) may facilitate this interaction. Overall, our study reveals a mechanism by which powdery mildew fungi disrupt ethylene-mediated resistance in host plants.","PeriodicalId":20098,"journal":{"name":"Phytopathology Research","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://phytopatholres.biomedcentral.com/counter/pdf/10.1186/s42483-025-00334-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147887808","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2