Biochimie最新文献

{"title":"A clot to uncover: SARS-CoV-2 nucleocapsid can outcompete the FOXP3 forkhead domain for DNA binding in vitro.","authors":"Keiran McInnes, Sylvia Fanucchi","doi":"10.1016/j.biochi.2025.08.006","DOIUrl":"10.1016/j.biochi.2025.08.006","url":null,"abstract":"<p><p>During COVID-19, systemic coagulopathy can lead to strokes and embolisms and may also contribute to long COVID. This coagulopathy is the result of overactivated platelets in circulation that lead to inappropriate clot formation. FOXP3 is a transcription factor involved in platelet development. Loss of FOXP3 function leads to abnormal platelets resembling those seen during COVID-19. Thus, FOXP3 may be dysregulated in COVID-19. The SARS-CoV-2 nucleocapsid (NC) is a multifunctional protein typically associated with viral genome packaging and virion assembly. However, it is also capable of binding DNA and may alter host gene expression. Here, potential interactions between the DNA-binding forkhead domain (FHD) of FOXP3 and the SARS-CoV-2 NC were investigated. Identification of a novel interaction between FOXP3 and SARS-CoV-2 NC may provide new clues to the pathophysiology of COVID-19. To address this aim, both proteins were overexpressed in T7 E. coli, purified via immobilised metal affinity chromatography, and monitored for interactions in the absence and presence of DNA using pull-down assays, electrophoretic mobility shift assays, and fluorescence anisotropy. A direct interaction was identified between the two proteins in the absence of DNA in vitro. Additionally, both proteins were found to bind DNA simultaneously under limiting conditions, but competed for binding under saturating conditions, where excess NC led to dissociation of FHD from the FHD-NC-DNA complex. This result implicates NC in FOXP3 dysfunction, potentially contributing to the coagulopathy and other symptoms observed during COVID-19. This work may inform future therapeutic strategies for severe COVID-19.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-08-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144812781","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":"Phenolic acids inhibit local and systemic effects induced by Bothrops brazili venom.","authors":"Sarah de Sousa Ferreira, Diana Pontes da Silva, Manoela Torres-Rêgo, Allanny Alves Furtado, Eduardo Augusto da Silva Diniz, Karla Patrícia de Oliveira Luna, Arnóbio Antônio da Silva-Júnior, Renata Mendonça Araújo, Marcela Abbott Galvão Ururahy, Davi Serradella Vieira, Matheus de Freitas Fernandes-Pedrosa","doi":"10.1016/j.biochi.2025.08.003","DOIUrl":"10.1016/j.biochi.2025.08.003","url":null,"abstract":"<p><p>Bothropic envenomation induces local damage, such as edema, necrosis, and hemorrhage, as well as systemic effects, including cardiovascular, renal and coagulation disturbances. While serum therapy remains, the primary treatment used for snakebites and efficiently neutralizes systemic damage, it inadequately addresses local tissue injury. Aiming to understand the pathophysiological mechanism of Bothrops brazili envenomation and explore novel complementary treatments, this study evaluated the local and systemic injuries caused by B. brazili venom and their mitigation by chlorogenic and rosmarinic acids. The venom exhibited high proteolytic and phospholipase activities, caused inflammation with edema formation, increased myeloperoxidase and cytokine dosage (IL-1β and IL-6). These effects were attenuated by phenolic acids. Molecular docking analysis assessed the interaction of these acids with B. brazili venom toxins, specifically catalytic PLA₂ (BbTX-III) and non-catalytic Lys49-PLA₂ (MTX-II). Chlorogenic and rosmarinic acids showed superior binding energies with MTX-II (-135.5683 ± 45.8415 kcal/mol and -166.8876 ± 17.7874 kcal/mol, respectively) compared to BbTX-III (-120.0387 ± 7.4546 kcal/mol and -114.3389 ± 15.4885 kcal/mol, respectively). Furthermore, these acids reduced myotoxicity, hemorrhage, hemostatic disturbances, and kidney and liver injuries, as well as leukogram and platelet alterations induced by B. brazili venom. The chlorogenic and rosmarinic acids demonstrated antiophidic potential by inhibiting both the local and systemic effects of envenomation. These findings suggest that their potential use as complementary therapies against envenomation caused by B. brazili.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144805429","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":"Divergent clinical, inflammatory, and histopathological responses induced by Amazonian Tityus venoms: insights and limitations of current antivenom therapy.","authors":"Karina Furlani Zoccal, Karla de Castro Figueiredo Bordon, Mouzarllem Barros Reis, Paloma Beatriz Rosa Nunes de Souza Chini, Jonas Gama Martins, Beatriz Acquaroni Zuanazzi, Gisele Adriano Wiezel, Ana Carolina Campos Dos Santos, Rudi Emerson de Lima Procópio, Eliane Candiani Arantes","doi":"10.1016/j.biochi.2025.08.004","DOIUrl":"10.1016/j.biochi.2025.08.004","url":null,"abstract":"<p><p>Scorpion stings are considered a neglected condition and represent a serious health problem in many tropical countries, especially for children and the elderly. In Brazil, the yellow scorpion (Tityus serrulatus) is widely found and responsible for the majority of severe envenoming cases; however, other medically relevant species endemic to the Brazilian Amazon region, such as Tityus silvestris, Tityus metuendus and Tityus obscurus, remain underexplored. In the present study, we characterized the clinical, inflammatory and histopathological responses induced by venoms from these Amazonian species in a murine model (Balb/c mice), using T. serrulatus as a reference. Envenomation with T. silvestris resulted in pronounced systemic manifestations, including elevated clinical scores, hyperglycemia, leukocytosis, cytokine release (IL-6, IL-1β, IL-10), and tissue injury in the lungs and kidneys, comparable to the pathophysiological manifestations from T. serrulatus venom. In contrast, T. metuendus and T. obscurus induced milder inflammatory profiles. It is noteworthy that cross-reactivity assays revealed limited immunoreactivity and reduced in vivo neutralization of T. metuendus and T. obscurus venoms by the commercially available T. serrulatus-based antivenom. These findings reveal critical limitations in relying on a single-species antivenom for treating scorpion envenomation across diverse regions and underscore the need for region-specific therapeutic strategies tailored to the distinct venom profiles and pathogenicity of Amazonian Tityus species.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144805428","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":"TSPO, reactive oxygen species and oxidative stress in physiological and pathological situations: a complex relationship.","authors":"Didier Morin, Jean-Jacques Lacapère","doi":"10.1016/j.biochi.2025.08.002","DOIUrl":"10.1016/j.biochi.2025.08.002","url":null,"abstract":"<p><p>Since its discovery in 1977 in the external membrane of mitochondria, the precise role of TSPO, previously named PBR for peripheral type benzodiazepine receptor, remains an enigma because of its interactions with various exogenous and endogenous ligands such as cholesterol, porphyrins and its implication in different cellular processes. Moreover, its presence in organisms ranging from bacteria to humans and its wide distribution in the body, including central nervous system, asked the question of its conserved function. Its involvement in many diseases often connected to inflammation led to the development of many positrons emission tomography tracers, but also questioned its link to the production of reactive oxygen species (ROS) well described in the inflammation processes. This critical review presents the various systems involving TSPO that produce ROS, such as for instance the respiratory chain or the NADPH oxidases. The protein partners that have been described to interact with TSPO in such processes are also presented. Finally, the relationships of TSPO with diseases implicating ROS are overviewed.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-08-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144786120","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":"Codon usage and antibiotic resistance: A hidden evolutionary mechanism.","authors":"Ujwal Dahal, Anu Bansal","doi":"10.1016/j.biochi.2025.07.027","DOIUrl":"10.1016/j.biochi.2025.07.027","url":null,"abstract":"<p><p>Antibiotic resistance represents a global health crisis, and emerging evidence suggests that codon usage, traditionally considered a silent aspect of genetic coding, plays a pivotal role in the evolution of resistance. Traditional resistance mechanisms, such as efflux pumps, enzymatic inactivation, and target modification, have been extensively studied. Still, recent findings highlight the role of codon optimization in enhancing the synthesis of resistance determinants in pathogens, including Acinetobacter baumannii, Neisseria gonorrhoeae, and Klebsiella pneumoniae. Comparative genomic analyses employing metrics such as Codon Adaptation Index (CAI), Effective Number of Codons (ENC), and Relative Synonymous Codon Usage (RSCU), alongside advanced bioinformatic and machine learning approaches, have identified subtle yet significant shifts in codon usage patterns between resistant and susceptible strains. Additionally, experimental studies using in vitro assays, in vivo models, and synthetic biology approaches prove that translational control through codon modulation contributes to adaptive responses under antibiotic pressure. Understanding these associations offers potential avenues for developing novel diagnostic biomarkers and therapeutic strategies. Therefore, this review underscores the necessity of an interdisciplinary approach to decipher the complex interplay between codon usage and antibiotic resistance, ultimately informing future efforts to mitigate the impact of multidrug-resistant pathogens.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144769448","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":"In-silico prioritization of pathogenic Interleukin-37b variants and a fusion platform for high-yield soluble production.","authors":"Sana Tahir, Jannat Rahim, Saima Sadaf","doi":"10.1016/j.biochi.2025.07.026","DOIUrl":"10.1016/j.biochi.2025.07.026","url":null,"abstract":"<p><p>Human interleukin-37 isoform 1 (IL-37b) is a key anti-inflammatory cytokine with significant therapeutic potential for inflammatory and immune-mediated disorders. However, its clinical translation is limited by poor understanding of disease-associated genetic variants and lack of an expression system for soluble production. While addressing both challenges, this study presents (a) a prioritized catalog of high-confidence, pathogenic IL-37b variants, and (b) a fusion-based expression platform for its soluble production, providing essential resources for future functional validations. Screening of over 3000 IL-37b variants using various computational tools and multi-algorithm consensus approach identified 25 potentially pathogenic non-synonymous single nucleotide variants (nsSNVs). Amongst these, 16 variants (e.g., D64 V/N, L72R, L111Q, V113F, C122R, F154S, I155 N, Y157C, E168G, G174A, I111T) were predicted to significantly destabilize IL-37b's structure and impair its interaction with the IL-18 receptor. Further, guided by complementary in-silico predictions, an aspartate-rich lunasin peptide yielded the highest soluble expression, constituting ∼40 % of total E. coli cellular proteins. The fusion expression system achieved ∼80 % solubility (compared to <10 % for wild-type IL-37b) and a yield of 167 mg/L following Ni²⁺-affinity purification under optimized conditions (25 °C, lactose autoinduction). The findings underscore the significance of complementary computational workflows in establishing an end-to-end pipeline for variant-to-solution analysis of IL-37b - a dual foundation linking in silico discovery to therapeutic development.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-07-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144765884","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":"Venomics and insect prey specificity of the Central American scorpion Centruroides limbatus (Pocock, 1898) and its comparison with close species Centruroides bicolor (Pocock, 1898).","authors":"Cecilia Díaz, Jennifer Rivera, Arturo Chang-Castillo, Fabián Bonilla, Natalia Ortiz, Adriana Alfaro-Chinchilla, Mahmood Sasa","doi":"10.1016/j.biochi.2025.07.025","DOIUrl":"10.1016/j.biochi.2025.07.025","url":null,"abstract":"<p><p>Centruroides limbatus and Centruroides bicolor are phylogenetically related species with different geographical distributions. The scarce envenomation cases in Costa Rica suggest they are probably 'mammal harmless', but their venom's effect on other animals has been poorly characterized. We aimed to describe the protein venom composition of C. limbatus and C. bicolor, in the context of their trophic habits and prey specificity. We applied a proteomics shotgun approach to analyze the composition of venom peptides of C. limbatus and compare them with those expressed by C. bicolor. We also tested the venom's lethal effect on insects and their ability to induce paralysis. Among the recovered NaTxs, there were C. bicolor Cbi1, C. suffusus CssIX, C. noxius Cn11, C. gracilis Cg2, and C. vittatus β-toxins. Regarding KTxs, we identified ergtoxins, limbatotoxins, and hongotoxins, all peptides commonly found in Centruroides venoms, as well as C. noxius cobatoxin-1 and C. margaritatus Cm39. Regarding lethality, as demonstrated with other buthid venoms, crickets were very sensitive, whereas mealworms were the most resistant. The current study shows that these scorpion species display similar venom compositions, including previously identified peptides from other Centruroides with and without medical importance, and as expected, they show only minor specificity differences.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-07-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144719217","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":"Mechanisms of outer membrane vesicles in bacterial drug resistance: Insights and implications.","authors":"Xianyu Zhang, Wenbo Ding, Jianyu Yang, Linran Gao, Qianying Wang, Jingjing Wang, Yu Luo, Xin Yuan, Baoyu Sun, Jifei Yang, Yujiao Zhou, Liyuan Sun","doi":"10.1016/j.biochi.2025.07.024","DOIUrl":"https://doi.org/10.1016/j.biochi.2025.07.024","url":null,"abstract":"<p><p>The emergence of antibiotic resistance has rendered the treatment of bacterial infections exceedingly challenging, with diseases caused by resistant strains often resulting in significant morbidity and mortality. Consequently, it is crucial to investigate the mechanisms underlying antibiotic resistance. Outer membrane vesicles (OMVs) are nanoscale spheres characterized by a double membrane structure, released by Gram-negative bacteria (GNB). While the mechanisms governing OMV biogenesis remain under investigation, three models have been proposed. These vesicles have been implicated in enhancing bacterial survival during antibiotic treatment and contributing to the onset and development of drug resistance through various pathways. OMVs function as a secretion system, delivering cargo that mediates intercellular communication to neighboring cells, and their closed structure facilitates this molecular delivery. Vesicles released into the extracellular compartment can protect bacteria from antibiotic treatment by promoting horizontal gene transfer, inactivating or binding antibiotics, influencing biofilm formation, and mediating bacterial gene mutations, among other mechanisms. Many studies have demonstrated that OMVs play a critical role during antibiotic exposure. An in-depth understanding of the mechanisms of OMVs in the development of bacterial drug resistance could help develop more effective therapeutic strategies to prevent persistent bacterial infections. This review focuses on summarising the latest evidence on the involvement of OMVs in the development of drug resistance, to provide ideas for future studies.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144719206","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":"In vitro and in vivo antibacterial activity of TsAP-2 from Tityus stigmurus scorpion venom in multidrug-resistant strains and its NMR three-dimensional structure.","authors":"Alessandra Daniele-Silva, Janainna Xavier Fernandes, Adriana Marina E Silva Parente, Bruno Amorim-Carmo, Suedson de Carvalho Silva Rodrigues, Lucas Hilário Nogueira de Sousa, Elizabeth C G Dos Santos, Thaís G de Carvalho, Raimundo F Araújo Júnior, Raudiney Frankilin Vasconcelos Mendes, Rafael Matos Ximenes, Arnóbio A da Silva-Júnior, Luiz Alberto Lira Soares, Renata Mendonça Araújo, Matheus F Fernandes-Pedrosa","doi":"10.1016/j.biochi.2025.07.023","DOIUrl":"10.1016/j.biochi.2025.07.023","url":null,"abstract":"<p><p>Microbial infections are a public health problem that combined with the emergence of resistant microorganisms have boosted the search for new antibiotic agents. In this approach, the antibacterial and antibiofilm effects in vitro of TsAP-2 (peptide from the Tityus stigmurus scorpion venom) were evaluated. In addition, its antimicrobial action in the skin wound model infected with Staphylococcus aureus and Galleria mellonella larvae infected with a multidrug-resistant strain and the effect of the combination with conventional antibiotics in vitro were investigated. TsAP-2 demonstrated broad-spectrum antibacterial activity in vitro, with antibiofilm action against standard and multidrug-resistant strains during early biofilm formation. Furthermore, TsAP-2 exhibited additive and synergistic effects when combined with conventional antibiotics. TsAP-2 revealed antibacterial and healing activity in vivo, reducing wound area and necrosis, while promoting an increase in neovascularization and epithelialization. TsAP-2 decreased the number of resistant bacteria in infected larvae, increasing their survival rate. The structural conformation of the peptide was assessed using circular dichroism and its three-dimensional structure was determined through NMR spectroscopy. In zwitterionic vesicles, TsAP-2 revealed a random conformation and a predominant helical structure in the presence of anionic vesicles. The three-dimensional structure of TsAP-2 obtained by NMR analysis indicates a helical segment from the 7th to the 15th residue, with flexibility in the N and C-terminal peptide domains. Taken together, this approach indicates the ability of TsAP-2 to change its conformation when interacting with biomimetic medium, highlights its extensive pharmacological potential, being an attractive candidate for the exploration of new anti-infective drugs.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144719205","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 extreme C-terminal region of the phage BFK20 gp41 helicase has a role in DNA binding, protein-ATP interactions and ATPase activity.","authors":"Nora Halgasova, Lucia Bocanova, Jacob A Bauer, Barbora Niku, Kristina Papayova, Gabriela Bukovska","doi":"10.1016/j.biochi.2025.07.022","DOIUrl":"10.1016/j.biochi.2025.07.022","url":null,"abstract":"<p><p>Replication protein gp41 from bacteriophage BFK20 is a 537 residue SF2 family helicase. The N-terminal two-thirds of the gp41 sequence is homologous to XPB/Ssl2-like helicases, but no clear homology to any known and characterized protein could be found for the C-terminal one-third. We prepared and studied the following gp41 mutant recombinant proteins: deletion mutant gp41L481, missing the last 56 C-terminal amino acids (482-537), and five point mutants, each substituting a single amino acid from this region with alanine (K516A, R518A, D520A, D521A and E522A). We tested the ATPase activities, DNA binding abilities, thermal stabilities and protein-ATP interactions of each isolated protein and compared them with wild-type-like protein gp41HN. The ATPase activity and DNA binding ability of gp41L481 were significantly lower than gp41HN. The K516A and R518A mutations resulted in an almost total loss of ATPase activity, while the D521A mutation produced a lesser loss. The K516A mutation also significantly reduced the DNA binding ability of the mutant protein. All point mutants were less stable than the wild-type protein to a greater or lesser extent, and ATP had a significant stabilizing effect on most tested proteins. We conclude that the amino-acids at the extreme C-terminus of gp41 are important for its ATPase activity, DNA binding ability and protein-ATP interactions. BFK20 gp41 is an example of a phage helicase whose accessory domain significantly affects its properties and it provides additional evidence for the importance of accessory domains for helicase function.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144710282","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}