The EMBO JournalPub Date : 2026-04-07DOI: 10.1038/s44318-026-00742-y
Philipp Schenk,Shane M Devine,Simon A Cobbold,Niall D Geoghegan,Elizabeth L Kyran,Ching-Seng Ang,Jack A Alexandrovics,Dale J Calleja,Dylan H Multari,Vineet Vaibhav,Bernadine G C Lu,Theresa A Klemm,Laura F Dagley,Kym N Lowes,Nicholas A Williamson,Pieter J A Eichhorn,Ashley P Ng,Rebecca Feltham,David Komander
{"title":"Global analysis of cancer cell responses to USP9X inhibition.","authors":"Philipp Schenk,Shane M Devine,Simon A Cobbold,Niall D Geoghegan,Elizabeth L Kyran,Ching-Seng Ang,Jack A Alexandrovics,Dale J Calleja,Dylan H Multari,Vineet Vaibhav,Bernadine G C Lu,Theresa A Klemm,Laura F Dagley,Kym N Lowes,Nicholas A Williamson,Pieter J A Eichhorn,Ashley P Ng,Rebecca Feltham,David Komander","doi":"10.1038/s44318-026-00742-y","DOIUrl":"https://doi.org/10.1038/s44318-026-00742-y","url":null,"abstract":"The ubiquitin-specific protease (USP) USP9X is a human deubiquitinase (DUB) with a large number of described targets and cellular roles. In cancer, USP9X is found as an oncogene or as a tumour suppressor depending on context, and its utility as a target for cancer therapy remains unclear. We here describe WEHI-092, a piperazine-based USP9X-specific small-molecule inhibitor, which binds to a unique region in the USP9X Fingers-subdomain, distinct from known DUB-inhibitor binding sites. Using proteomics and ubiquitinomics, we show that USP9X targets distinct substrates compared to USP7, yet the substrate profile of USP9X varies significantly across cancer cell lines. We reveal a core set of 17 proteins commonly regulated by USP9X in most cell lines, which we consider as proximal biomarkers for USP9X inhibition. Consistent with proteomics, we show in unrelated cell lines that WEHI-092 treatment arrests the cell cycle in metaphase without inducing cell death. This explains growth suppression in long-term clonogenic assays in most cancer cell lines, and positions USP9X inhibitors as a new class of selective mitotic poisons.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"21 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147630371","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 : 2026-04-02DOI: 10.1038/s44318-026-00763-7
Guohui Xie,Xuan Du,Yifang Tan,Yuxing Zhou,Cheng Chi,Sixian Zhou,Colette L Picard,Songge Chai,Lei Wu,Danling Zhu,Jun Zhao,Yan Xue,Sisi Li,Steven E Jacobsen,Zhe Wu,Jiamu Du
{"title":"A spontaneous termination mechanism of RNA polymerase V shapes the DNA methylation landscape in plants.","authors":"Guohui Xie,Xuan Du,Yifang Tan,Yuxing Zhou,Cheng Chi,Sixian Zhou,Colette L Picard,Songge Chai,Lei Wu,Danling Zhu,Jun Zhao,Yan Xue,Sisi Li,Steven E Jacobsen,Zhe Wu,Jiamu Du","doi":"10.1038/s44318-026-00763-7","DOIUrl":"https://doi.org/10.1038/s44318-026-00763-7","url":null,"abstract":"DNA methylation plays critical roles in eukaryotic gene silencing, genome imprinting, viral defense, and suppression of transposable elements. In plants, RNA Polymerase V (Pol V)-generated non-coding RNA guides DNA methylation through the RNA-directed DNA methylation (RdDM) pathway; however, how these RNAs are selected is unknown. Here, we show that the 3'-ends of Pol V transcripts are enriched at A-rich template DNA (A-rich-DNAT). Arabidopsis RdDM regions possess AT-rich boundaries genome-wide, suggesting that Pol V likely terminates at A-rich-DNAT, which subsequently defines the DNA methylation landscape in plants. A-rich-DNAT successfully stops Pol V transcription in vitro. Structural snapshots of Pol V transcribing A-rich-DNAT show that accumulation of unstable rU:dA pairs in the RNA-DNA hybrid promotes transcription bubble collapse and spontaneous transcription termination. These findings identify an intrinsic Pol V termination signal that shapes genomic DNA methylation patterning in plants and reveals a common mechanism for spontaneous transcription termination.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"49 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147599524","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 : 2026-04-02DOI: 10.1038/s44318-026-00769-1
Angela Migur,Maximilian Feussner,Chunyu Liao,Omer S Alkhnbashi,Adrien Chauvier,Nils G Walter,Rolf Backofen,Zasha Weinberg,Chase L Beisel
{"title":"A leader-repeat hairpin blocks extraneous CRISPR RNA production in diverse CRISPR-Cas13 systems.","authors":"Angela Migur,Maximilian Feussner,Chunyu Liao,Omer S Alkhnbashi,Adrien Chauvier,Nils G Walter,Rolf Backofen,Zasha Weinberg,Chase L Beisel","doi":"10.1038/s44318-026-00769-1","DOIUrl":"https://doi.org/10.1038/s44318-026-00769-1","url":null,"abstract":"CRISPR RNAs (crRNAs) guide recognition and targeting of intracellular invaders as part of adaptive immunity by CRISPR-Cas systems. crRNAs are transcribed from CRISPR arrays of conserved repeats interlaced with invader-derived spacers. While crRNA production is essential for immunity, its optimization for defense remains poorly understood. Here, we show that, in diverse RNA-targeting type VI CRISPR-Cas systems, the leader RNA encoded upstream of the CRISPR array prevents formation of an invader-independent extraneous crRNA (ecrRNA) by blocking processing of the first repeat. Using the VI-B2 system from Porphyromonas gingivalis as a model, we demonstrate that the leader RNA and first repeat form a conserved inhibitory hairpin that precludes binding and processing by the system's Cas13b nuclease. Disrupting this hairpin enables ecrRNA production, which in turn can deplete invader-derived crRNAs and reduce Cas13b-mediated phage defense. Structure prediction indicates that these leader-repeat hairpins are widespread across diverse type VI subtypes, highlighting a conserved regulatory mechanism. Our findings reveal how a prevalent branch of CRISPR-Cas systems suppresses ecrRNA formation to promote RNA-guided immunity.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"19 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147599502","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 : 2026-03-31DOI: 10.1038/s44318-026-00760-w
Chia-Tsen Tsai,Venus Marie Gaela,Hsuan-Yu Hsia,Yu-Chen Huang,Yi-Ling Shen,Liuh-Yow Chen
{"title":"Orphan nuclear receptors recruit TRIM28 to promote telomeric H3K9me3 for the ALT pathway.","authors":"Chia-Tsen Tsai,Venus Marie Gaela,Hsuan-Yu Hsia,Yu-Chen Huang,Yi-Ling Shen,Liuh-Yow Chen","doi":"10.1038/s44318-026-00760-w","DOIUrl":"https://doi.org/10.1038/s44318-026-00760-w","url":null,"abstract":"Alternative lengthening of telomeres (ALT) is a telomere maintenance mechanism deployed in embryonic stem cells and cancer cells. High levels of the heterochromatin mark H3 lysine 9 trimethylation (H3K9me3) at telomeres are critical for ALT, but how this is achieved remains unclear. Telomeric association of orphan nuclear receptors (NRs)-such as COUP-TF1, COUP-TF2, TR2, and TR4-has been shown previously to facilitate ALT activation. Here, we show that orphan NRs regulate telomeric H3K9me3 through TRIM28, a corepressor of ZNF transcription factors, to promote ALT. We report that H3K9me3 is induced by telomeric association of orphan NRs in cultured human fibroblast and ALT cancer cell lines. Moreover, TRIM28 is required for the orphan-NR-induced H3K9 methylation and ALT phenotypes. Importantly, physical interaction of TRIM28 with orphan NRs induces telomeric localization of TRIM28. A TRIM28 variant defective in orphan-NR interaction fails to localize to telomeres and is unable to promote H3K9me3 and ALT phenotypes. These findings indicate that telomeric orphan NRs recruit TRIM28 for telomeric H3K9me3 and ALT activation, emphasizing the role of chromatin structure in ALT activation.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"18 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147583809","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 : 2026-03-31DOI: 10.1038/s44318-026-00767-3
Ruyi Shi,Mengquan Yang,Yusong Liu,Haishan Gao,Zhonghui Lin
{"title":"Mechanistic basis for selective Csm6-2 activation by cyclic penta-adenylate in a type III CRISPR-Cas system.","authors":"Ruyi Shi,Mengquan Yang,Yusong Liu,Haishan Gao,Zhonghui Lin","doi":"10.1038/s44318-026-00767-3","DOIUrl":"https://doi.org/10.1038/s44318-026-00767-3","url":null,"abstract":"Type III CRISPR systems generate cyclic oligoadenylate (cOA, 3 to 6 AMPs) messengers upon detecting viral RNA, activating downstream effectors to defend against viral infection. Although cOA-activated effectors have been extensively characterized, the effectors specific to cA5-one of the most abundant cOA species produced during phage infection-have remained unexplored. Here, we report that the CRISPR ribonuclease Csm6 (Csm6-2) from Actinomyces procaprae selectively employs cA5 as its activator. Csm6-2 utilizes its HEPN domain, rather than the CARF domain, to mediate self-limiting cleavage of cOA activators. Cryo-EM structural analyses reveal that Csm6-2 functions as a homotetramer, and disruption of tetramer formation significantly reduces its ribonuclease activity. Although cA6 and cA5 bind Csm6-2 with comparable affinity, only cA5 induces CARF domain closure, stabilizes the tetramer, and remodels the active site in the HEPN domain. In contrast, the sixth AMP of cA6 imposes significant steric hindrance on CARF domain movement, preventing its closure and subsequent allosteric activation. These findings expand our understanding of the cOA signaling diversity and specific cOA recognition mechanisms in type III CRISPR immunity.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"31 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147583816","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":"Structural insight into ligand binding and activation of the orphan GPCR Mas1.","authors":"Yumu Zhang,Qiuying Wang,Heng Liu,Hong Shan,Yimin Gu,Jiaqi Yang,Yuan Gao,Kai Wu,Dehua Yang,H Eric Xu","doi":"10.1038/s44318-026-00764-6","DOIUrl":"https://doi.org/10.1038/s44318-026-00764-6","url":null,"abstract":"The Mas1 receptor, an orphan class A G-protein-coupled receptor (GPCR), plays pivotal roles in cardiovascular and anti-inflammatory regulation. Despite its therapeutic relevance, the structural mechanisms underlying Mas1 ligand binding and activation remain poorly understood. Here, we report cryo-EM structures of Mas1 bound to two chemically distinct agonists-neuropeptide FF (NPFF) and synthetic small-molecule AR234958-captured in complex with inhibitory G proteins. These structures reveal a conserved orthosteric binding pocket accommodating both ligands through shared hydrophobic interactions. Unlike many other class A GPCRs that rely on direct W6.48 toggle switch engagement, Mas1 adopts a non-canonical activation strategy driven by a ligand-induced hydrophobic compression plane involving residues Y2486.55, L872.60, I842.57, and L2667.39 at the bottom of the ligand binding pocket. This mechanism transmits mechanical tension to promote TM6 displacement and G protein coupling. Functional mutagenesis validates this model, identifying two transmembrane helix 6 (TM6) residues, M2446.51 and F2376.44, as critical molecular switches. Comparative analyses of Mas1-related receptors, MRGPRX1-X4, reveal conserved features and mechanistic divergence within this subfamily. These findings provide a structural framework for understanding Mas1 pharmacology and rational design of selective therapeutics.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"18 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147578173","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":"CDKAL1 dysfunction impairs lysine codon translation in podocytes and accelerates chronic kidney disease.","authors":"Hiroko Nagata,Yu Nagayoshi,Takeshi Chujo,Hitomi Kaneko,Kayo Nishiguchi,Yutaka Kakizoe,Hiroko Ijima,Korin Sakakida,Takeshi Masuda,Sumio Ohtsuki,Fan-Yan Wei,Yukie Takahashi,Takaichi Fukuda,Hideaki Jinnouchi,Yuki Adachi,Ryosuke Yamamura,Koki Matsushita,Masataka Adachi,Hideki Yokoi,Kimitoshi Nakamura,Hitoshi Nakazato,Kazuhito Tomizawa","doi":"10.1038/s44318-026-00759-3","DOIUrl":"https://doi.org/10.1038/s44318-026-00759-3","url":null,"abstract":"Cdk5 regulatory subunit-associated protein 1-like 1 (Cdkal1) encodes a tRNA-modifying enzyme responsible for thiomethylation generating 2-methylthio-N6-threonylcarbamoyladenosine (ms2t6A) in the anticodon loop of tRNALysUUU. Genome-wide association studies have identified CDKAL1 variants as risk factors for type 2 diabetes mellitus (DM) and chronic kidney disease (CKD), but whether CKD arises independently of diabetes has remained elusive. Here, we demonstrate that CDKAL1 is required for kidney function and that its dysfunction directly promotes CKD progression independently of diabetes. Systemic and podocyte-specific Cdkal1 knockout in mice leads to CKD phenotypes in later adulthood or after increasing the burden on kidney. Cdkal1-knockout podocytes show reduced lysine-codon translation and decreased levels of lysine-rich proteins, including such that are important for podocyte functions, accompanied by impaired cell migration. These adverse effects on podocytes could be partially reversed by overexpressing CD2AP, a lysine-rich protein. These findings extend the concept of 'tRNA modopathy' to kidney disease and provide mechanistic insights into how defective tRNA modification contributes to kidney disease progression.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"16 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147535671","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":"FADD is recruited to activated STING oligomers to initiate caspase-mediated NF-κB activation in Drosophila melanogaster.","authors":"Kasper Grønbjerg Winther,Juliette Schneider,Gabrielle Haas,Anna Hvarregaard Christensen,Shreya Goyal,Weisheng Luo,Ziming Wei,Jiyong Liu,Katarzyna Kjøge,Jan J Enghild,Carine Meignin,Neal Silverman,Hua Cai,Jean-Luc Imler,Rune Hartmann","doi":"10.1038/s44318-026-00761-9","DOIUrl":"https://doi.org/10.1038/s44318-026-00761-9","url":null,"abstract":"STING is an evolutionarily conserved key regulator of innate immunity. In the model organism Drosophila melanogaster, STING activates the NF-κB-like transcription factor Relish, initially characterized for its role in the antibacterial IMD pathway. The versatile FADD/Caspase-8 axis is widely used in various immune signaling pathways throughout the animal kingdom, including the IMD pathway. Here, we show that it functions downstream of STING in Drosophila to mediate Relish activation by the Caspase-8 homolog DREDD. We present a detailed structural model illustrating how the adapter protein FADD interacts with two separate STING dimers in the activated oligomerized form of STING, thus providing a molecular explanation for the activation-dependent recruitment of FADD. We further show that FADD interacts with IMD in a structurally distinct but functionally related manner, highlighting how the STING and IMD pathways differentially utilize the adapter protein FADD. Our results illustrate how an ancestral module is incorporated into different innate immune pathways, providing insights into the evolution of host-pathogen interactions.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"17 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147535672","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 : 2026-03-26DOI: 10.1038/s44318-026-00699-y
Raine E S Thomson,Yosephine Gumulya,Anthony W Bengochea,Gabriel Foley,Julian Zaugg,Anna Aagaard,Connie M Ross,James Beckett,Mikael Bodén,Ulrik Jurva,Martin A Hayes,Shalini Andersson,Elizabeth M J Gillam
{"title":"Thermostable ancestors enabled evolutionary diversification of promiscuous chemical defence enzymes.","authors":"Raine E S Thomson,Yosephine Gumulya,Anthony W Bengochea,Gabriel Foley,Julian Zaugg,Anna Aagaard,Connie M Ross,James Beckett,Mikael Bodén,Ulrik Jurva,Martin A Hayes,Shalini Andersson,Elizabeth M J Gillam","doi":"10.1038/s44318-026-00699-y","DOIUrl":"https://doi.org/10.1038/s44318-026-00699-y","url":null,"abstract":"Enzymes are generally believed to evolve from promiscuous ancestors to more specialized descendants under some selection pressure related to their function. However, enzymes whose function depends on substrate promiscuity have not been studied. Here, we show that a group of highly diverse, xenobiotic-metabolizing enzymes, responsible for defense against a constantly changing battery of xenobiotic chemicals, evolved from highly thermostable ancestors. Thermostability declined in parallel with the accumulation of sequence diversity through evolution. The major lineages differed in their relative diversification, with the more stable lineage leading to greater extant sequence diversity. Thermostability was associated with a trend towards better sequestration of hydrophobic residues within the core of the protein and increased exposure of polar residues in solvent-accessible parts of the structure. Resurrected ancestral forms were active towards typical substrates and exhibited ligand-binding promiscuity comparable to, or greater than, their extant descendants. This work supports the hypothesis that robust ancestors facilitate evolutionary diversification and highlights features responsible for enhancing thermostability in a protein fold.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"29 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147518659","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":"Enhanced P-TEFb activity compromises dentate gyrus neurogenesis in mice.","authors":"Yin Fang,Tong Qiu,Ping Wang,Shujun Bai,Min Wang,Chao Yang,Yan Wang,Peixuan Zhang,He Wang,Shanling Liu,Xue Xiao,Qintong Li","doi":"10.1038/s44318-026-00752-w","DOIUrl":"https://doi.org/10.1038/s44318-026-00752-w","url":null,"abstract":"Enhanced P-TEFb activity is thought to promote cell proliferation by increasing the transcriptional output of RNA polymerase II. The 7SK snRNP complex, which contains LARP7 and HEXIM1, sequesters and inhibits most cellular P-TEFb to prevent premature transcription elongation. Paradoxically, instead of exerting overgrowth effects, biallelic inactivation of LARP7 is linked to Alazami syndrome, a human neurodevelopmental disorder characterized by growth restriction and cognitive impairment. Here, we report that conditional ablation of either Larp7 or Hexim1 in the murine brain reduces the size and impairs the function of the hippocampal dentate gyrus during the neonatal period. Functional analyses reveal that increased P-TEFb activity enhances self-renewal transcriptional programs in transit-amplifying neuronal progenitor cells to limit neurogenesis in developing dentate gyri. These results demonstrate that dysregulated subtissular stem cell dynamics can reconcile increased P-TEFb activity with reduced organ growth, and suggest a translational opportunity for repurposing P-TEFb inhibitors to treat medical conditions affecting dentate gyrus size and function.","PeriodicalId":501009,"journal":{"name":"The EMBO Journal","volume":"19 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-03-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147502520","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}
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
