The EMBO JournalPub Date : 2026-03-11DOI: 10.1038/s44318-026-00732-0
Neha Uttekar,Annette Artz,Vallari Ghanekar,Pragya Kaul,Jessica Heinrichs,Rebekka I Stegmeyer,Gizem Gülevin Takir,Astrid F Nottebaum,Dietmar Vestweber
{"title":"Plakoglobin transmits tension across VE-cadherin for vascular leak formation and leukocyte diapedesis.","authors":"Neha Uttekar,Annette Artz,Vallari Ghanekar,Pragya Kaul,Jessica Heinrichs,Rebekka I Stegmeyer,Gizem Gülevin Takir,Astrid F Nottebaum,Dietmar Vestweber","doi":"10.1038/s44318-026-00732-0","DOIUrl":"https://doi.org/10.1038/s44318-026-00732-0","url":null,"abstract":"VE-cadherin controls endothelial junction integrity, and thereby inflammation-induced vascular permeability and leukocyte extravasation. The adhesive function of VE-cadherin is influenced by its binding to β-catenin, which is linked by α-catenin to actin. Plakoglobin can replace β-catenin in such complexes, and both types of complexes co-exist in endothelial cells. Here, we have investigated whether β-catenin and plakoglobin differ in their relevance for controlling endothelial junctions. Based on gene silencing in vitro and conditional endothelium-specific gene inactivation in mice in vivo, we found that both leukocyte diapedesis through endothelium and induction of vascular permeability by inflammatory mediators depend on plakoglobin, but not β-catenin. Mechanistically, we demonstrated that plakoglobin is crucial for the generation of tension across VE-cadherin by transmigrating leukocytes and by inflammatory mediators, whereas β-catenin was dispensable in this context. Transgenic mice expressing a VE-cadherin tension sensor revealed that plakoglobin is essential in vivo for histamine-induced tension across VE-cadherin. Thus, plakoglobin, but not β-catenin, is needed for leukocyte diapedesis, the induction of vascular permeability, and the stimulation of mechanical tension across VE-cadherin.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"76 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147393903","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"m6A reader Ythdf proteins control retrotransposon B2 repeat expression and safeguard early embryo development.","authors":"Ruibao Su,Di Gao,Zongchang Du,Tie-Gang Meng,Chao Li,Lei-Ning Chen,Xiaoting Lin,Changchang Cao,Li-Hua Fan,Yanbin Dong,Sheng Li,Shi-Ming Luo,Shuai Jiang,Zhong Guo,Yulu Tian,Qing-Yuan Sun,Xiang-Hong Ou","doi":"10.1038/s44318-026-00728-w","DOIUrl":"https://doi.org/10.1038/s44318-026-00728-w","url":null,"abstract":"N6-methyladenosine (m6A) and its binding proteins are critical regulators of gene expression and development in mammals. Despite its extent and importance, the regulatory mechanisms of m6A-binding reader proteins Ythdf1, Ythdf2, and Ythdf3 during the early stages of mammalian development remain incompletely understood. Here, we show that Ythdf2 and Ythdf3, but not Ythdf1, are required for early embryo development in mice. Mechanically, we demonstrate that all three Ythdf proteins mediate the decay of their target transcripts by binding to similar m6A sites, including maternal mRNAs, mid-preimplantation-activated transcripts, and retrotransposon RNAs. Among these, retrotransposon B2 RNAs emerge as one of the primary targets of Ythdf proteins throughout early embryo development, and deficiency in Ythdf1-3 leads to the accumulation of SINE/B2 RNAs, which, in turn, attenuates RNA polymerase II (Pol II) transcription through trans-regulatory mechanisms. In parallel, Ythdf1-3 deficiency represses Pol III-driven B2 transcription, thereby modulating RNA polymerase II activity at genomic regions adjacent to B2 loci via cis-regulatory effects. Together, the coordinated regulatory axis of Ythdf-SINE/B2-gene expression governs a broad transcriptional network that is crucial for embryogenesis.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"43 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147393905","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The EMBO JournalPub Date : 2026-03-05DOI: 10.1038/s44318-026-00724-0
Matthew J Morris,Yvonne Y Yeap,Jonathon R Edwards,Chi Chen,Annalisa Paolino,Sebastian G B Furness,S Sean Millard,Julia K Pagan,Laura R Fenlon,Dominic C H Ng
{"title":"Microcephaly-associated protein WDR62 supports purine metabolism by interacting with co-chaperone BAG2.","authors":"Matthew J Morris,Yvonne Y Yeap,Jonathon R Edwards,Chi Chen,Annalisa Paolino,Sebastian G B Furness,S Sean Millard,Julia K Pagan,Laura R Fenlon,Dominic C H Ng","doi":"10.1038/s44318-026-00724-0","DOIUrl":"https://doi.org/10.1038/s44318-026-00724-0","url":null,"abstract":"Inherited mutations in the spindle pole-associated scaffold protein WDR62 cause autosomal recessive primary microcephaly. Previous research has characterised the roles of WDR62 in the regulation of spindle dynamics, cell division, and brain development. Here, we identify a new function of this protein in regulating purine metabolism. WDR62 interacts directly with BAG2, a co-chaperone of HSP70/90. Under stress conditions, WDR62 and BAG2 re-localise to cytoplasmic granules enriched for enzymes involved in purine synthesis (PFAS) and salvage (HPRT). In WDR62-deficient cells, purine synthesis is impaired, while purine deprivation leads to cytotoxicity and nucleoside accumulation. Furthermore, in these cells elevated BAG2 levels are linked to HPRT destabilisation, which can be reversed by BAG2 knockdown. Notably, microcephaly-associated WDR62 mutations disrupt interaction with BAG2 and fail to restore HPRT levels. In utero depletion of WDR62 or HPRT in the mouse neocortex causes premature delamination and migration of neural precursor cells. Interestingly, HPRT loss enhances self-renewal and proliferation of these precursors, contrasting with the reduced proliferation and precocious differentiation observed upon WDR62 loss. Our study identifies regulatory functions of WDR62 in purine metabolism that may contribute to primary microcephaly.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147359221","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The EMBO JournalPub Date : 2026-03-05DOI: 10.1038/s44318-026-00719-x
Christa Schleper,Thiago Rodrigues-Oliveira
{"title":"Asgard archaea: have we found our microbial ancestors?","authors":"Christa Schleper,Thiago Rodrigues-Oliveira","doi":"10.1038/s44318-026-00719-x","DOIUrl":"https://doi.org/10.1038/s44318-026-00719-x","url":null,"abstract":"The discovery of Asgard archaea about a decade ago has greatly reshaped our understanding of archaeal evolution and the origin of eukaryotes. Asgards are currently thought to be the closest prokaryotic relatives of eukaryotes and to represent the archaeal host lineage that participated in the endosymbiotic event leading to the first eukaryotic cell. The presence of numerous eukaryotic signature proteins in Asgard genomes supports this view and provides important insights into the deep evolutionary roots of eukaryotic cellular complexity. However, the close relationship between archaea and eukaryotes had been observed for decades, based on features that are shared in different molecular processes. This review discusses the discovery of Asgard archaea in the broader context of archaeal molecular and cellular biology and highlights how earlier findings foreshadowed their emergence. Primarily targeted at newcomers to the field, the review provides an overview of evolutionary innovations across the Archaea domain and discusses molecular and cellular features of cultivated Asgard strains in light of previous archaeal research.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"67 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147359219","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A bacterial gene acquired by parasitoid wasps contributes to venom secretion against host defence.","authors":"Zhiguo Liu,Mei Tao,Zixuan Xu,Junwei Zhang,Yang Li,Zhi Dong,Qichao Zhang,Lan Pang,Yifeng Sheng,Yueqi Lu,Ting Feng,Wenqi Shi,Longtao Yu,Antonis Rokas,Jiani Chen,Xing-Xing Shen,Jianhua Huang","doi":"10.1038/s44318-026-00702-6","DOIUrl":"https://doi.org/10.1038/s44318-026-00702-6","url":null,"abstract":"Horizontal gene transfer (HGT) is an important source of gene innovation in prokaryotic and eukaryotic organisms. Several genes acquired by hosts of parasitoid wasps via HGT have been reported to protect hosts from parasitoid wasps. In contrast, little is known about whether HGT-acquired genes in parasitoid wasps are involved in attacking their hosts. Here, we report a prokaryote-type CDP-diacylglycerol synthase (PTCDS) gene that was horizontally transferred into the last common ancestor of two parasitoid wasps, Leptopilina heterotoma and L. syphax, from the bacterial family Rickettsiaceae. We experimentally demonstrated that PTCDS is linked to ensure the appropriate storage amount of venom in the venom reservoir of parasitoid wasps. PTCDS knockdown downregulated the expression of certain vesicle-mediated transport genes, thereby reducing the secretion of venom into venom reservoir without altering its composition. This resulted in a significant increase in the proportion of encapsulated wasp eggs in parasitized hosts, ultimately leading to host immune-mediated killing. We conclude that parasitoid wasps use the foreign gene PTCDS to influence venom amounts against host defence, providing new insight into the arms race between parasitoid wasps and hosts.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"4 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146070019","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The EMBO JournalPub Date : 2026-01-28DOI: 10.1038/s44318-025-00680-1
Monica Gobran,Peter Lenart
{"title":"Mitotic entry: Bora takes Polo to Aurora, and gives them a hug.","authors":"Monica Gobran,Peter Lenart","doi":"10.1038/s44318-025-00680-1","DOIUrl":"https://doi.org/10.1038/s44318-025-00680-1","url":null,"abstract":"","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"296 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146070020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The EMBO JournalPub Date : 2026-01-28DOI: 10.1038/s44318-025-00679-8
Anaïs Pillan,Philippine Ormancey,Celia Ben Choug,Stephen Orlicky,Nicolas Tavernier,Lucie Van Hove,Batool Ossareh-Nazari,Nicolas Joly,Frank Sicheri,Thierry Lorca,Lionel Pintard
{"title":"Molecular basis for the activation of Aurora A and Plk1 kinases during mitotic entry.","authors":"Anaïs Pillan,Philippine Ormancey,Celia Ben Choug,Stephen Orlicky,Nicolas Tavernier,Lucie Van Hove,Batool Ossareh-Nazari,Nicolas Joly,Frank Sicheri,Thierry Lorca,Lionel Pintard","doi":"10.1038/s44318-025-00679-8","DOIUrl":"https://doi.org/10.1038/s44318-025-00679-8","url":null,"abstract":"The evolutionarily conserved, intrinsically disordered protein Bora is critical for initiating the activation of mitotic kinases. Once phosphorylated at Ser112 by Cyclin A-Cdk1 kinase, phospho-Bora activates unphosphorylated Aurora A kinase (AURKA), directing it towards Polo-like kinase 1 (Plk1), thus promoting Cyclin B-Cdk1 activation and mitotic entry. Here, by combining structural modeling and in vitro assays, we provide evidence that Bora wraps around the N-terminal lobe of AURKA to position its phospho-Ser112 near AURKA's T-loop, mimicking T-loop phosphorylation. Additionally, Bora transiently interacts with the αC helix of the Plk1 kinase domain through a conserved motif, guiding AURKA activity towards the Plk1 T-loop, which is otherwise impervious to phosphorylation by AURKA. We highlight the importance of this motif for Bora function in vitro and during mitotic entry in Xenopus laevis egg extracts. Our results reveal critical molecular details of mitotic kinase activation, which could lead to the development of pathway-specific inhibitors.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"71 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146070021","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The EMBO JournalPub Date : 2026-01-28DOI: 10.1038/s44318-025-00681-0
Arianna Esposito-Verza,Duccio Conti,Paulo D Rodrigues Pedroso,Lina Oberste-Lehn,Carolin Koerner,Sabine Wohlgemuth,Artem Mansurkhodzhaev,Ingrid R Vetter,Marion E Pesenti,Andrea Musacchio
{"title":"Molecular requirements for PLK1 activation by T-loop phosphorylation.","authors":"Arianna Esposito-Verza,Duccio Conti,Paulo D Rodrigues Pedroso,Lina Oberste-Lehn,Carolin Koerner,Sabine Wohlgemuth,Artem Mansurkhodzhaev,Ingrid R Vetter,Marion E Pesenti,Andrea Musacchio","doi":"10.1038/s44318-025-00681-0","DOIUrl":"https://doi.org/10.1038/s44318-025-00681-0","url":null,"abstract":"Activation of PLK1, a master mitotic kinase, requires phosphorylation of its activation segment on Thr210, within a basic consensus sequence for Aurora kinases. Aurora B-dependent phosphorylation of Thr210 has been reported, but other evidence identified a strict requirement for the Aurora A partner Bora for Thr210 phosphorylation. Here, we investigate the elusive mechanistic basis for this requirement. We show that Aurora A:Bora phosphorylates Thr210 of PLK1 in vitro. On the contrary, T210 was not phosphorylated by isolated Aurora A, additional Aurora A:activator complexes, or Aurora B:INCENP, even when used at high kinase/substrate ratios. A transient interaction of Bora and PLK1, identified by structural modeling and probed mutationally, is uniquely required for Thr210 phosphorylation. Dependency on Bora for Thr210 phosphorylation is eliminated after mutating Lys208, in the Aurora consensus, into arginine. This conservative mutation turns PLK1 into a substrate of nearly all tested active Aurora kinases, including Aurora B. Collectively, these results shine a new light on the specificity of the PLK1 activation mechanism.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"143 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146070022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The lysosomal LAMTOR-Rag complex functions as a checkpoint for antiviral interferon production.","authors":"Zeming Feng,Lulu Wang,Shujun Chen,Sihan Cao,Miao Lei,Xiuzhen Yang,Kaixiong Ma,Shi Yu,Huina Hu,Kaixuan Zheng,Xin Xu,Qi Zheng,Shaobo Wang,Wenxiang Hu,Chun-Yan Lim","doi":"10.1038/s44318-026-00695-2","DOIUrl":"https://doi.org/10.1038/s44318-026-00695-2","url":null,"abstract":"Lysosomes are emerging as important signaling hubs for antiviral defense, yet how they enable type I interferon (IFN-β) production is unclear. Here, we identify an evolutionarily repurposed lysosomal pathway, centered on the LAMTOR-Rag GTPase complex, that governs IFN-β production through dual transcriptional and post-transcriptional regulation. Genetic ablation of LAMTOR or Rag GTPases in macrophages abolishes IFN-β responses despite intact pattern recognition receptor (PRR) signaling, uncovering a lysosome-specific checkpoint essential for antiviral immunity. Mechanistically, Rag GTPase activity controls IRF expression to prime IFN transcription, while upon PRR stimulation, the tumor suppressor FLCN recruits p38 MAPK to lysosomes, where Rag-dependent p38 phosphorylation stabilizes Ifnb1 mRNA. Nutrient availability dynamically modulates Rag nucleotide states and thereby its activation, linking IFN production to metabolic capacity. Notably, this checkpoint operates independently of mTORC1, illustrating how an ancient nutrient-sensing module has been co-opted for immune regulation. Disruption of the LAMTOR-Rag-FLCN-p38 axis impairs IFN induction in vitro and antiviral responses in vivo, underscoring its physiological significance. Our findings support the role of the lysosome as a central signaling hub integrating metabolic and immune cues, suggesting future directions for potential therapeutic strategies against viral infections.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"10 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146021697","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The EMBO JournalPub Date : 2026-01-20DOI: 10.1038/s44318-025-00687-8
Junchao Shi,Xudong Zhang,Chen Cai,Shichao Liu,Jiancheng Yu,Emma R James,Lihua Liu,Benjamin R Emery,Megan R McMurray Bires,Elizabeth Torres-Arce,Hukam C Rawal,Joemy Ramsay,Jason Kunisaki,Changcheng Zhou,David S Milstone,Mary Elizabeth Patti,Xiaoxu Yang,Tim G Jenkins,Aaron Quinlan,Bradley R Cairns,Paul Schimmel,James M Hotaling,Kenneth I Aston,Tong Zhou,Qi Chen
{"title":"Conserved shifts in sperm small non-coding RNA profiles during mouse and human aging.","authors":"Junchao Shi,Xudong Zhang,Chen Cai,Shichao Liu,Jiancheng Yu,Emma R James,Lihua Liu,Benjamin R Emery,Megan R McMurray Bires,Elizabeth Torres-Arce,Hukam C Rawal,Joemy Ramsay,Jason Kunisaki,Changcheng Zhou,David S Milstone,Mary Elizabeth Patti,Xiaoxu Yang,Tim G Jenkins,Aaron Quinlan,Bradley R Cairns,Paul Schimmel,James M Hotaling,Kenneth I Aston,Tong Zhou,Qi Chen","doi":"10.1038/s44318-025-00687-8","DOIUrl":"https://doi.org/10.1038/s44318-025-00687-8","url":null,"abstract":"Sperm aging impacts male fertility and offspring health, highlighting the need for reliable aging biomarkers to guide reproductive decisions. However, the molecular determinants of sperm fitness during aging remain ill-defined. Here, we profiled sperm small non-coding RNAs (sncRNAs) using PANDORA-seq, which overcomes RNA modification-induced detection bias to capture previously undetectable sncRNA species associated with mouse and human spermatozoa throughout the lifespan. We identified an \"aging cliff\" in mouse sperm RNA profiles-a sharp age-specific transition marked by significant shifts in genomic and mitochondrial tRNA-derived small RNAs (tsRNAs) and rRNA-derived small RNAs (rsRNAs). Notably, rsRNAs in mouse sperm heads exhibited a transformative length shift, with longer rsRNAs increasing and shorter ones decreasing with age, suggesting altered biogenesis or processing with age. Remarkably, this sperm head-specific shift in rsRNA length was consistently observed in two independent human aging cohorts. Moreover, transfecting a combination of tsRNAs and rsRNAs resembling the RNA species in aged sperm was able to induce transcriptomic changes in mouse embryonic stem cells, impacting metabolism and neurodegeneration pathways, mirroring the phenotypes observed in offspring fathered by aged sperm. These findings provide novel insights into longitudinal dynamics of sncRNAs during sperm aging, highlighting an rsRNA length shift conserved in mice and humans.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"123 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146005510","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}