{"title":"ALS-associated RNA-binding proteins promote UNC13A transcription through REST downregulation.","authors":"Yasuaki Watanabe,Naoki Suzuki,Tadashi Nakagawa,Masaki Hosogane,Tetsuya Akiyama,Naotoshi Kageyama,Yukino Funayama,Hitoshi Warita,Satoru Morimoto,Hideyuki Okano,Masashi Aoki,Keiko Nakayama","doi":"10.1038/s44318-025-00506-0","DOIUrl":"https://doi.org/10.1038/s44318-025-00506-0","url":null,"abstract":"Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by selective loss of motor neurons. Although multiple pathophysiological mechanisms have been identified, no comprehensive understanding of these heterogeneous processes has been achieved. The ALS-associated RNA-binding protein (RBP) TDP-43 has previously been shown to stabilize UNC13A mRNA by preventing cryptic exon inclusion. Here, we show that the ALS-associated RBPs MATR3, FUS, and hnRNPA1 regulate UNC13A expression by targeting the transcriptional repressor REST. These RBPs bind to and downregulate REST mRNA to promote UNC13A transcription. Loss of any of these RBPs in cultured cells or in iPSC-derived motor neurons carrying the ALS-causing FUS P525L mutation leads to REST overexpression, and the same is observed in motor neurons of individuals with familial or sporadic ALS. The functional convergence of four RBPs on the regulation of UNC13A expression underscores the important role of this process for synaptic integrity, and its association with ALS pathogenesis could be relevant for the development of new therapeutic agents.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"20 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144701181","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":"Deletion of EP3 prostaglandin receptor in murine macrophages aggravates diet-induced obesity by suppressing SPARC.","authors":"Wenlong Shang,Yinxiu Li,Lu Wang,Jiao Liu,Huiwen Ren,Qian Liu,Shumin Guo,Yuhong Wang,Yubo Ma,Tianyi You,Yujun Shen,Yu Zhou,Danyang Tian,Ying Yu","doi":"10.1038/s44318-025-00508-y","DOIUrl":"https://doi.org/10.1038/s44318-025-00508-y","url":null,"abstract":"Macrophages are primary immune cells involved in obesity-triggered chronic low-grade inflammation in adipose tissues. Prostaglandin E2 (PGE2), mainly generated from macrophages, can regulate adipose tissue remodeling, yet the underlying mechanisms are not fully understood. Here, we observed that PGE2 receptor subtype 3 (EP3) was remarkably downregulated in adipose tissue macrophages from high-fat diet (HFD)-fed mice and patients with obesity. Notably, macrophage-specific deletion of EP3 exacerbated HFD-induced fat expansion, whereas EP3α isoform overexpression in macrophages alleviated obesity phenotypes. Further, EP3 deficiency suppressed secretion of anti-adipogenic matricellular protein SPARC from macrophages. SPARC deletion in macrophages abrogated the protection of EP3-overexpression against diet-induced obesity. Mechanistically, EP3 activation promoted SPARC expression by suppressing DNA methylation in macrophages through a PKA-Sp1-Dnmt1/3a signaling cascade. Finally, EP3 agonist treatment ameliorated HFD-induced obesity in mice. Thus, EP3 inhibits adipogenesis through promoting release of SPARC from macrophages, suggesting a novel therapeutic target for diet-induced obesity.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"107 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144693473","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":"Human fetal kidney organoids model early human nephrogenesis and Notch-driven cell fate.","authors":"Michael Namestnikov,Osnat Cohen-Zontag,Dorit Omer,Yehudit Gnatek,Sanja Goldberg,Thomas Vincent,Swati Singh,Yair Shiber,Tal Rafaeli Yehudai,Hadas Volkov,Dani Folkman Genet,Achia Urbach,Sylvie Polak-Charcon,Igor Grinberg,Naomi Pode-Shakked,Boaz Weisz,Zvi Vaknin,Benjamin S Freedman,Benjamin Dekel","doi":"10.1038/s44318-025-00504-2","DOIUrl":"https://doi.org/10.1038/s44318-025-00504-2","url":null,"abstract":"Pluripotent stem cell (PSC)-derived kidney organoids are used to model human renal development and disease; however, accessible models of human fetal development to benchmark PSC-derived organoids remain underdeveloped. Here, we establish a chemically defined, serum-free protocol for prolonged culture of human fetal kidney-derived organoids (hFKOs) in vitro. hFKOs self-organize into polarized renal epithelium, reinitiate from NCAM1+ progenitors, and recapitulate nephrogenic and ureteric bud lineages. Bulk transcriptomics, single-cell RNA sequencing, pseudotime analysis, and immunostaining revealed diverse renal tissue cell populations, with a preserved epithelial progenitor pool and tubular differentiation axis. hFKOs were enriched for Notch signaling genes, enabling single-cell analysis of pharmacological Notch inhibition. This revealed a maturation block with increased nephron progenitors and a shift toward distal over early proximal tubule fates. We also identified a novel prominin-1-expressing cell state that evades Notch inhibition to generate both proximal and distal tubules. Overall, hFKOs provide a faithful model to gain insights into human kidney development, advancing the fields of stem cell biology and regenerative medicine.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"14 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144677866","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 : 2025-07-21DOI: 10.1038/s44318-025-00505-1
Gianluca Figlia,Sandra Müller,Fabiola Garcia-Cortizo,Marilena Neff,Glynis Klinke,Gernot Poschet,Aurelio A Teleman
{"title":"mTORC1 senses glutamine and other amino acids through GCN2.","authors":"Gianluca Figlia,Sandra Müller,Fabiola Garcia-Cortizo,Marilena Neff,Glynis Klinke,Gernot Poschet,Aurelio A Teleman","doi":"10.1038/s44318-025-00505-1","DOIUrl":"https://doi.org/10.1038/s44318-025-00505-1","url":null,"abstract":"mTORC1 promotes cell growth when nutrients such as amino acids are available. While dedicated sensors relaying availability of leucine, arginine and methionine to mTORC1 have been identified, it is still unclear how mTORC1 senses glutamine, one of its most potent inducers. Here, we find that glutamine is entirely sensed through the protein kinase GCN2, whose initial activation is not triggered by depletion of glutamine itself, but by the concomitant depletion of asparagine. In turn, GCN2 leads to a succession of events that additively inhibit mTORC1: within 1 h, GCN2 inhibits mTORC1 through the Rag GTPases, independently of its function as an eIF2α kinase. Later, GCN2-mediated induction of ATF4 upregulates Ddit4 followed by Sestrin2, which together cause additional mTORC1 inhibition. Additionally, we find that depletion of virtually any other amino acid also inhibits mTORC1 through GCN2. GCN2 and the dedicated amino acid sensors thus represent two independent systems that enable mTORC1 to perceive a wide spectrum of amino acids.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"38 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144677868","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":"Anillin directly crosslinks microtubules with actin filaments.","authors":"Ilina Bareja,Ondřej Kučera,Irene Istúriz Petitjean,Beatriz Eugenia Orozco Monroy,Jan Sabo,Marcus Braun,Zdenek Lansky,Gijsje H Koenderink,Marileen Dogterom","doi":"10.1038/s44318-025-00492-3","DOIUrl":"https://doi.org/10.1038/s44318-025-00492-3","url":null,"abstract":"Complex morphogenetic processes such as cell division require a tight coordination of the activities of microtubules and actin filaments. There is evidence that anillin, conventionally known as an actin-binding and -bundling protein, regulates microtubule/actin crosstalk during cell division. However, it is unknown whether anillin binds directly to microtubules and whether it is sufficient to establish crosslinking between microtubules and actin filaments. Here we address both questions by developing an in vitro system for observing anillin-mediated interactions with actin filaments and dynamic microtubules via total internal-reflection fluorescence microscopy. We find that anillin can interact directly with microtubules and promote microtubule bundling. We confirm that anillin binds and bundles actin filaments, and find that it has a strong preference for actin bundles over individual filaments. Moreover, we show that anillin can directly crosslink microtubules and actin filaments, cause sliding of actin filaments on the microtubule lattice, and transport actin filaments by the growing microtubule tip. Our findings indicate that anillin can potentially serve as a direct regulator of microtubule/actin crosstalk, e.g., during cell division.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"115 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144677867","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 : 2025-07-18DOI: 10.1038/s44318-025-00510-4
Krzysztof Wierbiłowicz,Chun-Song Yang,Ahmed Almaghasilah,Patryk A Wesołowski,Philipp Pracht,Natalia M Dworak,Jack Masur,Sven Wijngaarden,Dmitri V Filippov,David J Wales,Joshua B Kelley,Aakrosh Ratan,Bryce M Paschal
{"title":"Parp7 generates an ADP-ribosyl degron that controls negative feedback of androgen signaling.","authors":"Krzysztof Wierbiłowicz,Chun-Song Yang,Ahmed Almaghasilah,Patryk A Wesołowski,Philipp Pracht,Natalia M Dworak,Jack Masur,Sven Wijngaarden,Dmitri V Filippov,David J Wales,Joshua B Kelley,Aakrosh Ratan,Bryce M Paschal","doi":"10.1038/s44318-025-00510-4","DOIUrl":"https://doi.org/10.1038/s44318-025-00510-4","url":null,"abstract":"The androgen receptor (AR) transduces the effects of circulating and tumor-derived androgens to the nucleus through ligand-induced changes in protein conformation, localization, and chromatin engagement. Defining how these events are integrated with signal transduction is critical to understand how AR drives prostate cancer and unveil pathway features that are potentially amenable to therapeutic intervention. We describe a novel post-transcriptional mechanism that controls AR levels on chromatin and gene output based on highly selective, inducible degradation. We find that the mono-ADP-ribosyltransferase PARP7 generates an ADP-ribosyl degron in the DNA-binding domain of AR, which is recognized by the ADP-ribose reader domain in the ubiquitin E3 ligase DTX2 and degraded by the proteasome. Mathematical modeling of the pathway suggested that PARP7 ADP-ribosylates chromatin-bound AR, a prediction that was validated in cells using an AR DNA-binding mutant. Non-conventional ubiquitin conjugation to ADP-ribosyl-cysteine and degradation by the proteasome forms the basis of a negative feedback loop that regulates modules of AR target genes. Our data expand the repertoire of mono-ADP-ribosyltransferases to include gene regulation via highly selective protein degradation.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"10 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144664194","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 : 2025-07-17DOI: 10.1038/s44318-025-00497-y
Preman J Singh,Bhavna Verma,Adam Wells,Cláudia C Mendes,Dali Dunn,Ying-Ni Chen,Jade Oh,Lewis Blincowe,S Mark Wainwright,Roman Fischer,Shih-Jung Fan,Adrian L Harris,Deborah C I Goberdhan,Clive Wilson
{"title":"Amyloid-β disrupts APP-regulated protein aggregation and dissociation from recycling endosomal membranes.","authors":"Preman J Singh,Bhavna Verma,Adam Wells,Cláudia C Mendes,Dali Dunn,Ying-Ni Chen,Jade Oh,Lewis Blincowe,S Mark Wainwright,Roman Fischer,Shih-Jung Fan,Adrian L Harris,Deborah C I Goberdhan,Clive Wilson","doi":"10.1038/s44318-025-00497-y","DOIUrl":"https://doi.org/10.1038/s44318-025-00497-y","url":null,"abstract":"Secretory proteins aggregate into non-soluble dense-core granules in recycling endosome-like compartments prior to regulated release. By contrast, aberrantly processed, secreted amyloid-β (Aβ) peptides derived from amyloid precursor protein (APP) form pathological extracellular amyloidogenic aggregations in late-stage Alzheimer's disease (AD). By examining living Drosophila prostate-like secondary cells, we show that both APP and Aβ peptides affect normal biogenesis of dense-core granules. These cells generate dense-core granules and secreted nanovesicles called Rab11-exosomes via evolutionarily conserved mechanisms within highly enlarged secretory compartments with recycling endosomal identity. The fly APP homologue, APP-like (APPL), associates with these vesicles and the compartmental limiting membrane, from where its extracellular domain modulates protein aggregation. Proteolytic release of this domain permits mini-aggregates to coalesce into a large central dense-core granule. Mutant Aβ expression disrupts this process and compartment motility, and increases aberrant lysosomal targeting, mirroring previously unexplained early-stage pathological events in AD. It also promotes cell-to-cell propagation of these endolysosomal defects, again phenocopying changes observed in AD. Our data therefore demonstrate physiological roles for APP in membrane-dependent protein aggregation, involving molecular mechanisms, which when disrupted by Aβ peptides, trigger Alzheimer's disease-relevant pathologies.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"24 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144652900","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 : 2025-07-16DOI: 10.1038/s44318-025-00507-z
Malvina Pizzuto,Mercedes Monteleone,Sabrina Sofia Burgener,Jakub Began,Melan Kurera,Jing Rong Chia,Emmanuelle Frampton,Joanna Crawford,Monalisa Oliveira,Kirsten M Kenney,Jared R Coombs,Masahiro Yamamoto,Si Ming Man,Petr Broz,Pablo Pelegrin,Kate Schroder
{"title":"Cardiolipin inhibits the non-canonical inflammasome by preventing LPS binding to caspase-4/11.","authors":"Malvina Pizzuto,Mercedes Monteleone,Sabrina Sofia Burgener,Jakub Began,Melan Kurera,Jing Rong Chia,Emmanuelle Frampton,Joanna Crawford,Monalisa Oliveira,Kirsten M Kenney,Jared R Coombs,Masahiro Yamamoto,Si Ming Man,Petr Broz,Pablo Pelegrin,Kate Schroder","doi":"10.1038/s44318-025-00507-z","DOIUrl":"https://doi.org/10.1038/s44318-025-00507-z","url":null,"abstract":"Caspase-4 and caspase-11 (CASP4/11) sense bacterial lipopolysaccharide (LPS). Currently available inhibitors of CASP4/11 also block the activity of caspase-1 (CASP1), which restricts their usefulness in the study of CASP4/11 functions, as well as their clinical potential for the treatment of LPS-linked diseases through CASP4/11 inhibition. Here, we identify mitochondrial cardiolipin as a selective inhibitor of CASP4/11-dependent cell death and inflammatory cytokine secretion, without affecting CASP1 function. Cardiolipin targets the CARD domain of CASP4/11, impeding its interaction with LPS to restrain CASP4/11 activation, thereby suppressing LPS-induced systemic inflammation in vivo. By identifying cardiolipin as a selective inhibitor of CASP4/11, we provide an urgently needed tool for studying caspase-4/11 and noncanonical inflammasome functions in inflammatory pathways and LPS-induced pathogenesis.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"3 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144645894","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":"Proteomic aging signatures across mouse organs and life stages.","authors":"Enzo Scifo,Sarah Morsy,Ting Liu,Kan Xie,Kristina Schaaf,Daniele Bano,Dan Ehninger","doi":"10.1038/s44318-025-00509-x","DOIUrl":"https://doi.org/10.1038/s44318-025-00509-x","url":null,"abstract":"Aging is associated with the accumulation of molecular damage, functional decline, increasing disease prevalence, and ultimately mortality. Although our system-wide understanding of aging has significantly progressed at the genomic and transcriptomic levels, the availability of large-scale proteomic datasets remains limited. To address this gap, we have conducted an unbiased quantitative proteomic analysis in male C57BL/6J mice, examining eight key organs (brain, heart, lung, liver, kidney, spleen, skeletal muscle, and testis) across six life stages (3, 5, 8, 14, 20, and 26-month-old animals). Our results reveal age-associated organ-specific as well as systemic proteomic alterations, with the earliest and most extensive changes observed in the kidney and spleen, followed by liver and lung, while the proteomic profiles of brain, heart, testis, and skeletal muscle remain more stable. Isolation of the non-blood-associated proteome allowed us to identify organ-specific aging processes, including oxidative phosphorylation in the kidney and lipid metabolism in the liver, alongside shared aging signatures. Trajectory and network analyses further reveal key protein hubs linked to age-related proteomic shifts. These results provide a system-level resource of protein changes during aging in mice, and identify potential molecular regulators of age-related decline.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"37 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144640238","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":"FTO promotes weight gain via altering Kif1a splicing and axonal vesicle trafficking in AgRP neurons.","authors":"Daisuke Kohno,Reika Kawabata-Iwakawa,Sotaro Ichinose,Shigetomo Suyama,Kazuto Ohashi,Winda Ariyani,Tetsushi Sadakata,Hiromi Yokota-Hashimoto,Ryosuke Kobayashi,Takuro Horii,Vina Yanti Susanti,Ayumu Konno,Haruka Tsuneoka,Chiharu Yoshikawa,Sho Matsui,Akihiro Harada,Toshihiko Yada,Izuho Hatada,Hirokazu Hirai,Masahiko Nishiyama,Tsutomu Sasaki,Tadahiro Kitamura","doi":"10.1038/s44318-025-00503-3","DOIUrl":"https://doi.org/10.1038/s44318-025-00503-3","url":null,"abstract":"N6-methyladenosine (m6A) is an abundant chemical RNA modification involved in the regulation of many biological processes. The m6A demethylase FTO (fat mass and obesity-associated protein) is known to affect body weight, but its systemic context and underlying mechanisms remain unclear. Here, we found that mice lacking or overexpressing Fto in agouti-related peptide-expressing (AgRP) neurons in the hypothalamus exhibited decreased and increased body weight, respectively. FTO demethylated m6A on mRNAs for proteins associated with membrane trafficking and alternative splicing in AgRP neurons. Downstream, FTO-modulated alternative splicing of the axonal motor protein Kif1a affected its hinge region, which is relevant to the structure and function of KIF1A. Notably, Kif1a knockdown in AgRP neurons suppressed the weight gain of mice overexpressing Fto. In addition, FTO increased the trafficking and secretion of dense-core vesicles containing neuropeptides NPY and AgRP from AgRP neurons. Collectively, these results reveal a novel regulatory FTO-KIF1A axis in the brain affecting appetite-stimulating AgRP neurons and systemic energy homeostasis, via FTO regulation of the epitranscriptome of AgRP neurons.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"19 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144594402","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}
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