The FEBS journal最新文献

{"title":"The tryptophan prenyltransferase ComQ from Bacillus subtilis 168 can prenylate daptomycin at Trp1.","authors":"Yanli Xu, Maximilian J L J Fürst, Oscar P Kuipers","doi":"10.1111/febs.70578","DOIUrl":"https://doi.org/10.1111/febs.70578","url":null,"abstract":"<p><p>Prenylation is a common natural modification that enhances peptide bioactivity. Identifying prenyltransferases with broad substrate specificity is vital for enabling the modification of diverse compounds. In Bacillus subtilis 168, the tryptophan at Position 3 from the C terminus of the ComX₁₆₈ pheromone is farnesylated by ComQ₁₆₈, producing an inducer of natural competence. While ComQ₁₆₈'s native substrate, ComX, is a linear peptide, many bioactive cyclic peptides like daptomycin and polymyxin also contain long lipid tails, similar to farnesylated ComX. This study investigates whether ComQ₁₆₈ can be used as a synthetic biology tool to farnesylate cyclic antimicrobial peptides. ComQ₁₆₈ was cloned from B. subtilis 168, expressed in E. coli, and purified in soluble fusion form. Its ability to farnesylate ComX, which was generated by a ribosomally synthesized and post-translationally modified peptide (RiPPs) approach, confirmed its activity and proper folding. Remarkably, TF-ComQ₁₆₈ also catalyzed farnesylation of daptomycin in vitro, most likely at the N-terminal tryptophan residue. To explore substrate recognition, AlphaFold modeling was used to predict the binding pocket of ComQ₁₆₈ with both ComX and daptomycin, highlighting a C-terminal region potentially important for substrate interaction. These insights offer a promising starting point for engineering ComQ₁₆₈ variants with expanded substrate scopes. In summary, this work demonstrates for the first time that ComQ₁₆₈, previously known to modify linear peptides, can also farnesylate cyclic peptides-establishing its potential as a versatile tool in the biosynthetic engineering of bioactive compounds.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2026-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147825144","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":"Exploring the role of phase separation in TDP-43 pathogenesis with ArtiTDP43.","authors":"Eric Chevet","doi":"10.1111/febs.70577","DOIUrl":"https://doi.org/10.1111/febs.70577","url":null,"abstract":"<p><p>TDP-43 is a nuclear RNA-binding protein implicated in neurodegenerative diseases such as ALS and FTLD, where it becomes mislocalized to the cytoplasm and forms pathological aggregates. These aggregates are thought to arise through liquid-liquid phase separation, a process by which proteins form dynamic, membrane-less condensates that can mature into solid structures. To better understand this process, the authors developed ArtiTDP43, a chemically controllable system that enables reversible formation of TDP-43 condensates in cells. Using this tool, they showed that TDP-43 forms different structures depending on its concentration: small liquid-like puncta, intermediate condensates associated with stress granules, and large solid aggregates resembling disease pathology. These transitions are reversible at early stages but become irreversible as aggregates solidify. The study by Combe et al. demonstrates that increasing cytoplasmic TDP-43 concentration drives a liquid-to-solid transition, while oxidative stress accelerates this process and promotes pathological features such as phosphorylation and p62 recruitment. Importantly, formation of cytoplasmic aggregates leads to depletion of nuclear TDP-43 and increased cell death, indicating toxicity. Overall, the findings establish a mechanistic link between phase separation, aggregation, and cytotoxicity in TDP-43 proteinopathies. ArtiTDP43 provides a powerful tool to study early disease mechanisms and explore therapeutic strategies aimed at preventing pathological aggregation or maintaining normal TDP-43 dynamics.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2026-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147825148","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":"Toward understanding the catalytic mechanism for two classes of bacterial phospholipid N-methyltransferases.","authors":"Irina Shevyreva, Lena Sophie Fritsch, Leander Mika Koch, Anton Effing, Meriyem Aktas, Franz Narberhaus","doi":"10.1111/febs.70571","DOIUrl":"https://doi.org/10.1111/febs.70571","url":null,"abstract":"<p><p>Phosphatidylcholine (PC), the predominant phospholipid in eukaryotic membranes, also plays a crucial role in certain bacterial species, often mediating interactions with eukaryotic hosts. In bacteria, a major pathway for PC biosynthesis involves the three-step methylation of phosphatidylethanolamine, catalyzed by phospholipid N-methyltransferases (Pmts). While the binding site for the methyl donor S-adenosyl-l-methionine is well characterized in Pmt enzymes, the detailed mechanism of methyl group transfer remains poorly understood. In this study, we combined computational and biochemical approaches to identify the amino acid residues critical for the catalytic activity of two distinct Pmt classes: the Rhodobacter (R)-type enzyme from Rubellimicrobium thermophilum (RtPmtA) and the Sinorhizobium (S)-type enzyme from Agrobacterium tumefaciens (AtPmtA). Despite low sequence identity, both enzyme types share similar reaction mechanisms, with tyrosine residues playing key roles in methyl group transfer. In RtPmtA, two highly conserved tyrosines located within the substrate-binding pocket on the N-terminal αA-helix are critical for enzymatic function. In contrast, AtPmtA depends on a single tyrosine buried in the protein core for catalysis. These findings reveal distinct active site architectures and suggest that R-type and S-type enzymes have evolved class-specific structural strategies for tyrosine activation. This divergence highlights the evolutionary flexibility of Pmt enzymes, despite their shared catalytic function.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2026-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147825194","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":"Unraveling in vitro phase separation and aggregation properties of the structured region of FMRP and the impact of Fragile X syndrome-linked mutations.","authors":"Flavia Catalano, Alessandra Bigi, Francesca Troilo, Federica Gabriele, Gianluca Pistoia, Italia A Asteriti, Francesco Angelucci, Giorgio Giardina, Fabrizio Chiti, Carlo Travaglini-Allocatelli, Adele Di Matteo","doi":"10.1111/febs.70564","DOIUrl":"https://doi.org/10.1111/febs.70564","url":null,"abstract":"<p><p>Fragile X messenger ribonucleoprotein 1 (FMRP) is a multidomain RNA-binding protein highly expressed in neurons. It comprises a structured N-terminal region (NTR) containing five RNA/protein interaction domains and a large intrinsically disordered C-terminal region. A limited number of fragile X syndrome (FXS)-associated point mutations have been identified in the NTR, leading to the expression of mutated protein variants. Here, we show that the destabilizing effects of these mutations on the NTR region are less severe than those previously observed in the isolated domains, suggesting the presence of inter-domain interactions that stabilize the overall NTR architecture. Moreover, we demonstrate that the NTR structured region has an intrinsic propensity to undergo liquid-liquid phase separation (LLPS) and amyloid fibril formation in vitro, depending on protein concentration, and we characterize how three FXS-associated mutations (R138Q, G266E, and I304N) affect these processes. We show that the mutations either destabilize the entire NTR (G266E/I304N), markedly affect the kinetics of LLPS and suppress the droplet liquid nature (R138Q/G266E), or promote solid or gel-like non-amyloid aggregation (G266E), thus providing mechanistic insights into how they may alter protein function, contributing to the pathogenic mechanism. These findings suggest that the interplay between protein stability, LLPS, and fibrillization is finely regulated and may be critical for understanding FMRP function and its dysfunction in disease.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2026-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147825183","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":"Investigating the molecular mechanisms underlying the anti-CRISPR function of AcrIIA13b protein.","authors":"So Yeon Lee, Hyun Ho Park","doi":"10.1111/febs.70304","DOIUrl":"10.1111/febs.70304","url":null,"abstract":"<p><p>The CRISPR-Cas systems of adaptive immunity in bacteria and archaea provide resistance against phages and other mobile genetic elements. Counteractive anti-CRISPR (Acr) proteins in phages and archaeal viruses impede these CRISPR-Cas systems. Although CRISPR-Cas systems have revolutionized genome editing, potential off-target events remain a safety concern. Hence, a thorough comprehension of the structural and molecular basis of diverse Acrs is imperative to unravel the fundamental mechanisms governing CRISPR-Cas regulation. Here, we present the structure of AcrIIA13b from Staphylococcus haemolyticus and analyze its structural and functional features to reveal the molecular basis underlying the inhibition of Cas9 by AcrIIA13b. Our structural analysis shows that AcrIIA13b eliminates the cleavage activity of Staphylococcus aureus Cas9 (SauCas9) by blocking the PAM-binding region of Cas9 so that Cas9 cannot recognize the target DNA. In addition, we demonstrate that the 15 amino acid residues at the N terminus of AcrIIA13b, which were revealed to be important for its dimerization, are critical for its inhibitory activity against Cas9. Our findings shed light on the molecular basis of AcrIIA13b-mediated CRISPR-Cas inhibition and provide valuable insights into the arms race between bacteria and phages.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":"2560-2578"},"PeriodicalIF":4.2,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13147308/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145369425","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enzymatic synthesis of bioactive quinolones and (thio)coumarins by fungal type III polyketide synthases.","authors":"Nika Sokolova, Angelina Osipyan, Lili Zhang, Matthew R Groves, Sandy Schmidt, Kristina Haslinger","doi":"10.1111/febs.70376","DOIUrl":"10.1111/febs.70376","url":null,"abstract":"<p><p>Quinolones are privileged scaffolds for drug discovery that are relatively rare in nature. Here, we characterise two promiscuous fungal polyketide synthases AthePKS and FerePKS, which we had previously found to produce 2-quinolones in vitro. We challenged the enzymes with several substituted anthranilic acid derivatives, revealing their ability to produce precursors of pharmaceutically relevant quinolones. We also discovered that AthePKS and FerePKS accept other 2-substituted benzoic acids, leading to the formation of coumarin and thiocoumarin scaffolds. We applied AthePKS in an artificial enzymatic cascade towards an antimicrobial 4-methoxy-1-methyl-2-quinolone and demonstrated its in vivo feasibility by successfully expressing the pathway in Escherichia coli. Lastly, we determined the crystal structure of AthePKS, suggesting hotspots for enhancing its catalytic efficiency by enzyme engineering. Our results provide a framework for further engineering of enzymatic routes towards privileged heteroaromatic scaffolds and derivatives thereof.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":"2673-2691"},"PeriodicalIF":4.2,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13147306/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145844486","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Liver-specific BAG3 knockout delays chemically induced hepatocellular carcinoma development.","authors":"Verena Damiani, Erika Pizzinato, Federica Di Marco, Alessia Lamolinara, Francesco Del Pizzo, Aurora Navicella, Beatrice Dufrusine, Paola Lanuti, Enrico Dainese, Rossano Lattanzio, Manuela Iezzi, Michael Hahne, Damiana Pieragostino, Vincenzo De Laurenzi","doi":"10.1111/febs.70381","DOIUrl":"10.1111/febs.70381","url":null,"abstract":"<p><p>Bcl-2-associated athanogene 3 (BAG3) is a multifunctional protein involved in several cellular processes, including protein folding, degradation, apoptosis regulation, and cytoskeleton dynamics. Its dysregulation has been associated with several pathological conditions, including cancer. Hepatocellular carcinoma (HCC), a leading cause of cancer-related deaths worldwide, represents a complex molecular landscape involving multiple pathways. Pro- and antitumorigenic roles have been suggested for BAG3 in HCC. To elucidate the function of BAG3 in HCC, we established a hepatocyte-specific BAG3 knockout mouse model (BAG3albKO). Histological analysis revealed delayed hepatocarcinogenesis in BAG3albKO mice induced by diethylnitrosamine (DEN) treatment, suggesting a potential role for BAG3 deficiency in modulating liver lesion development. Moreover, BAG3 deletion attenuated cell migration and epithelial-to-mesenchymal transition in HCC-derived murine cell lines, indicating an impact on tumor aggressiveness. Proteomic analysis of DEN-induced acute liver injury revealed alterations in key pathways in BAG3albKO mice livers, including inhibition of autophagy and increased liver necrosis. Collectively, these findings emphasize the complex role of BAG3 in HCC pathogenesis and indicate its participation in tumor onset and progression.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":"2753-2771"},"PeriodicalIF":4.2,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145936829","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 hidden property of the iron-sulfur protein in the mononuclear iron-bound state: species-dependent structural ordering induced by magnetic fields.","authors":"Shigeki Arai, Shogo Soga, Mitsuhiro Hirai, Ryoma Kobayashi, Hirokazu Masai, Koji Kimura, Kiminori Maeda, Hiroki Nagashima","doi":"10.1111/febs.70377","DOIUrl":"10.1111/febs.70377","url":null,"abstract":"<p><p>The iron-sulfur (Fe-S) cluster assembly homolog 1 (ISCA1) is a ubiquitous protein conserved in various organisms. Previous work has shown that a pigeon ISCA1 (clISCA1) forms columnar oligomers in the 2Fe-2S cluster-bound state, the length of which has been known to change in response to magnetic fields. However, whether this unique property is conserved in ISCA1 proteins of other species, particularly humans (hsISCA1), is unclear. Moreover, a recent study revealed that clISCA1 binds to not only Fe-S clusters but also mononuclear iron atoms, which may impart some magnetic properties to clISCA1. In this study, the electron spin resonance revealed that hsISCA1 also binds to mononuclear iron atoms. Moreover, the magnetic responses of Fe-S cluster-unbound ISCA1s (Fe-ISCA1s), which bind only mononuclear iron atoms, were inspected by small-angle X-ray scattering analyses for pigeon (Fe-clISCA1) and human (Fe-hsISCA1). The results indicated that Fe-hsISCA1 formed columnar oligomers under geomagnetic conditions, whereas Fe-clISCA1 formed dumbbell-like oligomers. When a magnetic field (180 mT) was applied, the Fe-hsISCA1 oligomer was shortened within 1 min and gradually elongated again after 10 min. This result indicates that mononuclear iron atoms contribute to the magnetically induced structural ordering of ISCA1, whereas the contribution of the Fe-S clusters to the columnarization of ISCA1 varies among species. Although the physiological role of the magnetic properties of ISCA1 is not yet elucidated, this study demonstrated that the magnetic field responsiveness of ISCA1 is conserved in humans. The magnetic field responsiveness may be a hidden fundamental property of ISCA1 that is maintained even if the Fe-S cluster is released.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":"2692-2707"},"PeriodicalIF":4.2,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145859088","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":"SARS-CoV-2 nucleocapsid protein variants have differential RNA chaperone activity.","authors":"Sabrina Babl, Julia M Seidel, Fabian Kugler, Elisabeth Silberhorn, Anna Ludwig, Jonas Abel, Sophia Winklbauer, Niklas Schaub, Silvia Materna-Reichelt, Kamran Honarnejad, Nataša Stojanović Gužvić, Gernot Längst","doi":"10.1111/febs.70329","DOIUrl":"10.1111/febs.70329","url":null,"abstract":"<p><p>The single-stranded RNA genome of the SARS-CoV-2 virus is characterized by a complex secondary structure formed by patches of intramolecular RNA double-strands. Here, we show that the nucleocapsid (N) protein is not only the specific viral RNA packaging protein, but also acts as an RNA chaperone, facilitating RNA folding. RNA chaperones are classified by their non-specific RNA binding and the presence of intrinsically disordered regions (IDRs). N possesses three IDRs, separated by the structured RNA-binding domain (RBD) and the C-terminal domain (CTD). Our study identifies the amino acids 46-364 (RBD-IDR2-CTD) as crucial for chaperone activity, with flanking IDRs either enhancing or repressing this function, revealing the essential role of IDRs for the chaperone mechanism. Furthermore, a comparison between the Wuhan and Omicron BA.5 variant N shows reduced chaperone activity of the Omicron N protein. However, mimicking the cellular phosphorylation state of Omicron N restored its chaperone activity to the levels of the Wuhan variant. Our results identify N-phosphorylation as a regulatory mechanism of chaperone activity, emphasizing an intricate regulatory role of post-translational modifications in the dynamics of viral RNA secondary structure establishment. The regulation of RNA chaperoning could serve as a potential therapeutic target for future treatment of RNA viruses.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":"2579-2598"},"PeriodicalIF":4.2,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13147315/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145566871","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cryo-EM structure of N-glycosylated Pomacea canaliculata hemocyanin provides insights into its role in the immune response of gastropods.","authors":"Tabata Romina Brola, Ignacio Rafael Chiumiento, Santiago Ituarte, Guillermo Ignacio Benítez, Marcos Gragera, Jose-Maria Carazo, Horacio Heras, Lisandro Horacio Otero, Marcos Sebastián Dreon","doi":"10.1111/febs.70378","DOIUrl":"10.1111/febs.70378","url":null,"abstract":"<p><p>Hemocyanins are multifunctional soluble proteins found in most mollusks and some arthropods that may turn into a phenoloxidase-like enzyme (PO) associated with innate immune functions. To expand the structural understanding of gastropod hemocyanins and their physiological implications, here we report the single-particle cryogenic electron microscopy (cryo-EM) structure of Pomacea canaliculata snail hemocyanin (PcH) at 4.4 Å resolution along with its intrinsic and proteolytically induced PO activity. PcH shows a Megathura crenulata (giant keyhole limpet) hemocyanin (KLH)-type structure with a cylindrical shape, comprising 20 protomers assembled as di-pentamers of antiparallel asymmetric dimers, organized in a D5 symmetry. Each protomer comprises eight paralogous functional units (FUs) sharing conserved structural features typical of hemocyanins. The achieved map resolution allowed delineation of interaction networks among adjacent subunits across quaternary structure tiers-dimer, pentamer of dimers (decamer), and di-pentamer of dimers (di-decamer). Additionally, we identified six N-glycosylation sites per protomer, totaling 120 glycan trees in the overall structure. Kinetic analysis of intrinsic PO activity using catechol as substrate revealed a Michaelis constant (K_M) of 45.3 mm and a catalytic rate constant (k_cat) of 2.87 min^-1. This specific activity was enhanced by limited proteolysis using digestive and bacterial proteases. Potential protease cleavage sites were identified in silico, mapped onto the PcH model, and their accessibility assessed. Combined with molecular dynamics simulations, these findings suggest a structural basis for the PO induction mechanism. This study expands our knowledge of KLH-type hemocyanins and provides clues into their PO activation, which is triggered by endogenous and/or pathogen-associated proteases. This further underscores the role of molluscan hemocyanins in the innate immune system.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":"2708-2731"},"PeriodicalIF":4.2,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145844540","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}