Biochimie最新文献

{"title":"Sulfoquinovosyldiacylglycerol (SQDG) in chloroplast-poor tissues: What can lipidomics tell us?","authors":"Supakorn Potijun, Supaart Sirikantaramas, Hubert Schaller","doi":"10.1016/j.biochi.2026.10.011","DOIUrl":"10.1016/j.biochi.2026.10.011","url":null,"abstract":"<p><p>Sulfoquinovosyldiacylglycerol (SQDG) is an anionic sulfolipid of plastid membranes, classically associated with chloroplasts and thylakoids. Its detection by lipidomics in chloroplast-poor tissues raises a central problem: how can a reported SQDG signal be validated, and what evidence is required to determine its plastid context and biological meaning? In this critical narrative review, we reassess evidence beyond chloroplast-dominated tissues and evaluate both the strength of evidence for SQDG occurrence or function and the steps required to test lipidomics-derived hypotheses. The literature supports context-dependent rather than universal interpretations. Direct organelle-level lipid evidence from isolated non-green plastids remains limited; etioplast genetics supports an SQDG-related role in non-photosynthetic plastid membrane development; phosphate-deprived roots support phosphorus-economy remodeling; and sulfur-starvation studies establish regulated SQDG turnover and sulfur remobilization. By contrast, chromoplast and woody-tissue interpretations remain unresolved. These findings show that SQDG abundance alone is hypothesis-generating rather than diagnostic of function. We therefore propose a decision-tree framework that moves from chemical confirmation of the lipid signal to spatial localization, SQD1/SQD2-associated biosynthetic capacity, nutrient context, tissue-specific perturbation, and phenotype testing. This framework provides criteria for moving from lipidomic detection to supported biological interpretation in chloroplast-poor tissues.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149139376","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 and Metabolic Reprogramming by Docosahexaenoic Acid in Neuronal Cell Models of Alzheimer's Disease\".","authors":"Awdi Rana, Plourde Mélanie, Lo Van Amanda, Bernoud-Hubac Nathalie","doi":"10.1016/j.biochi.2026.10.005","DOIUrl":"https://doi.org/10.1016/j.biochi.2026.10.005","url":null,"abstract":"<p><p>Docosahexaenoic acid (DHA; 22:6n-3) is the most abundant omega-3 polyunsaturated fatty acid in the mammalian brain and an essential structural component of neuronal membranes. Several research studies indicate that DHA plays critical roles in maintaining membrane lipid composition, synaptic integrity, mitochondrial function, and metabolic homeostasis, processes that are disrupted in Alzheimer's disease (AD) and other neurodegenerative disorders. Because brain DHA availability depends largely on systemic metabolism and liver-brain communication, alterations in DHA homeostasis have been proposed as contributing factors to AD pathogenesis. In vitro neuronal culture models have been pivotal in investigating the molecular and biochemical mechanisms underlying DHA-mediated neuroprotection under disease-related conditions. This mini review summarizes how DHA treatment modulates cellular membrane organisation, synaptogenesis and cytoskeletal integrity, and its neuroprotective role in in vitro neuronal models of AD. Collectively, the literature supports DHA as a key modulator of the structure and metabolic mechanisms at the cellular level and supports the hypothesis that its greatest benefit may occur as a preventive or early-stage intervention. Although effective therapeutic interventions are still lacking, and more investigations integrating next-generation cellular models are still needed, these models provide crucial insights for developing targeted therapeutic applications in AD.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120062","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":"Extending the lifespan of human mesenchymal stromal cells: Approaches to immortalization and clinical prospects.","authors":"S Gokul Krishna, Nikshitha Kulal, Suresh Kannan, Uday Kumar Kolkundkar, Abhishek Kumar Singh, Samatha Bhat, Raviraja N Seetharam","doi":"10.1016/j.biochi.2026.10.009","DOIUrl":"10.1016/j.biochi.2026.10.009","url":null,"abstract":"<p><p>Mesenchymal stromal cells (MSCs) have a limited proliferative lifespan associated with replicative senescence, although the extent and onset of replicative senescence may vary among MSC sources. The immortalization of MSCs is being investigated as a strategy to extend proliferative capacity and facilitate scale-up. Moreover, immortalization may reduce the need for repeated isolation and expansion of primary MSCs, potentially facilitating the generation of sufficient cell numbers for research and manufacturing. Standardizing efficient methodologies remains important for consistent GMP manufacturing, product stability, and clinical translation. This review focuses on diverse strategies employed over the past 10 years to generate immortal MSCs, including induced pluripotent stem cell (iPSC)-derived sources and MSC-derived approaches. To determine whether the generated immortalized MSCs are functionally equivalent to primary MSCs, current trends and studies in the R&D phase are briefly discussed. Furthermore, this review highlights the underreported baseline stability assays and the need for comprehensive stability validation in the R&D phase. Additionally, the therapeutic potential of immortal MSCs is discussed, with an emphasis on their prospective applications in cell-based therapies and outlining future directions for their development.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120088","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":"Mesenchymal stem cells and their exosomes modulate sebocyte fate and lipid-associated proteomic-lipidomic remodeling.","authors":"Maryam Adelipour, Mohamed A Gab-Allah, Mingyu Kim, Sangsoo Lee, Kee K Kim, Ga Seul Lee, Jeong Hee Moon, David M Lubman, Jeongkwon Kim","doi":"10.1016/j.biochi.2026.10.003","DOIUrl":"10.1016/j.biochi.2026.10.003","url":null,"abstract":"<p><p>Sebocytes regulate skin lipid production and inflammatory homeostasis, yet how mesenchymal stem cells (MSCs) and MSCs-derived exosomes reshape sebocyte function remains unclear. This study compared the effects of indirect MSCs co-culture and MSCs-derived exosome treatment on MTS-associated metabolic activity, intracellular lipid droplet accumulation, proteomic remodeling, and lipidomic profiles in sebocytes. Human sebocytes were indirectly co-cultured with bone marrow-derived MSCs using transwell inserts or treated with MSCs-derived exosomes under proliferative or low-serum, lipid accumulation-promoting conditions. MTS-associated metabolic activity was assessed using the MTS assay, intracellular lipid droplet accumulation using Nile Red staining, proteomic remodeling using label-free LC-MS/MS, and lipidomic changes using untargeted LC-MS lipidomics. Indirect MSCs co-culture reduced MTS-associated metabolic activity, particularly under low-serum conditions, while markedly increasing intracellular lipid droplet accumulation. Proteomic analysis indicated that MSCs co-culture promoted cytoskeletal, adhesion-related, and lipid-handling remodeling. Lipidomics further revealed broad lipid-class reprogramming, characterized by increased phospholipid-associated features and reduced lysophospholipid-associated features. In contrast, MSCs-derived exosomes increased MTS-associated metabolic activity under low-serum conditions, while intracellular lipid droplet accumulation remained largely comparable to control levels. Exosome treatment induced more selective proteomic changes related to proteostasis, mitochondrial adaptation, and vesicular trafficking/signaling, with limited lipidomic alterations that did not remain significant after FDR correction. MSCs co-culture and MSCs-derived exosomes exert biologically distinct effects on sebocytes. Whole MSCs co-culture drives extensive lipid-associated remodeling, whereas isolated exosomes mainly increase MTS-associated metabolic activity and induce adaptive proteomic responses, suggesting that exosomes transmit only part of the broader MSCs paracrine influence on sebocyte biology.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120016","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":"Phytochemicals differentially modulate mitochondrial bioenergetics: roles of F₁F_O-ATPase, respiratory complexes, and mPTP opening.","authors":"Antonia Cugliari, Cristina Algieri, Patrycja Anna Glogowski, Micaela Fabbri, Fabiana Trombetti, Salvatore Nesci","doi":"10.1016/j.biochi.2026.10.001","DOIUrl":"10.1016/j.biochi.2026.10.001","url":null,"abstract":"<p><p>Phytochemicals can modulate mitochondrial function, but their specific actions on bioenergetic pathways are not fully defined. Here, isolated mitochondria were exposed to three phytocompounds, S-allyl cysteine (SAC), benzyl isothiocyanate (BITC), and epicatechin (EPC), and key mitochondrial parameters were assessed, including F₁F_O-ATPase activity, NADH- and succinate-driven respiration, and mitochondrial permeability transition pore (mPTP) opening. Mechanistic insights were obtained through kinetic analyses and by probing redox sensitivity using dithiothreitol-treated mitochondria. SAC increased F₁F_O-ATPase activity, displaying cooperative behaviour and multiple inhibitory/activating components consistent with uncompetitive and competitive interactions, while leaving respiration unchanged; it also reduced mPTP sensitivity, indicating desensitization of pore dynamics. In contrast, BITC produced mixed-type inhibition of F₁F_O-ATPase and significantly impaired respiration, with a stronger impact on Complex I-linked (NADH-driven) flux; BITC additionally delayed mPTP opening through a redox-dependent mechanism. EPC did not significantly alter F₁F_O-ATPase activity, respiration, or mPTP opening under the experimental conditions. Overall, these findings demonstrate compound-specific modulation of mitochondrial bioenergetics by phytochemicals, supporting their potential relevance for therapeutic strategies targeting oxidative stress and mitochondrial dysfunction.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120067","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":"Biochemical, structural, and functional characterization of the Nocardia asteroides dihydrofolate reductase: a primary target of anti-nocardiosis treatment.","authors":"Julie Couston, Sébastien Lainé, Jérôme Feuillard, Mickaël Blaise","doi":"10.1016/j.biochi.2026.10.002","DOIUrl":"10.1016/j.biochi.2026.10.002","url":null,"abstract":"<p><p>Nocardiosis is a human infectious disease caused by several species of Nocardia and primarily affecting the skin, lungs and central nervous system. The first-line treatment is based on cotrimoxazole, combining trimethoprim and sulfamethoxazole. These two drugs respectively target the dihydrofolate reductase (DHFR) and the dihydropteroate synthase (DHPS) involved in the essential folate synthesis pathway. The occurrence of drug resistance to these two drugs is however frequent. While the molecular mechanisms of trimethoprim resistance are well documented in other bacteria, they remain poorly explored and documented in Nocardia. This is partly because few biochemical, structural or genetic studies have been conducted on DHFR from this genus. In this study, we report the biochemical and structural characterization of DHFR from Nocardia asteroides (DHFR_Nad). We show that overexpression of DHFR_Nad in N. asteroides confers strong resistance to trimethoprim. We recombinantly expressed and purified active DHFR_Nad and determined its inhibition constant for trimethoprim. We solved the crystal structure of DHFR_Nad bound to trimethoprim at high- resolution. Further, biochemical studies of mutant DHFR variants pinpointed the role of important residues for trimethoprim binding and drug-resistance.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120041","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 dual stressor system negatively impacts In vivo luminescence from bioluminescent bacteria.","authors":"Rajeev Ranjan, Kumar Tarun Singh, Lazi Parween, Archna Pandey, Yeshvandra Verma, Valentina Kratasyuk","doi":"10.1016/j.biochi.2026.10.007","DOIUrl":"10.1016/j.biochi.2026.10.007","url":null,"abstract":"<p><p>Cellular health requires an intricate balance of prooxidants and antioxidants. Enzymatic and non-enzymatic molecules that maintain this balance succumb to oxidative insults beyond certain levels. Therefore, it becomes necessary to probe cellular health through the estimation of antioxidant enzymes/molecules, NADH/NAD⁺ and GSH/GSSG inside a viable cell. This approach demands skilled personnel, considerable time, expensive kits, and reagents. Therefore, there is a search for potent alternatives that can precisely estimate cellular health in real time. In the present study, we exposed bioluminescent bacteria (BB, OD₆₀₀: 0.1) to model prooxidants, viz. H₂O₂ and Hg (II) at different concentrations to study in vivo luminescence kinetics under nutrient-rich (cultivation media: Luria-Bertani broth, 2.5 %, and NaCl, 1.5 %) and nutrient-starved conditions (2.5 % NaCl). Further, we investigated the effect of a dual stressor system at low-dose (10 μL Hg (II) at 1.00 ppm in the presence of 10 μL of 10 ppm H₂O₂) on luminescence response from a cell suspension of BB (50 μL, OD₆₀₀: 0.1). The results showed that luminescence recovery in BB was delayed as the concentration of stressors increased. Moreover, a low-dose stimulatory effect (enhanced luminescence) was observed when Hg(II) at 0.142 ppm was exposed individually but in presence of H₂O₂ at 1.42 ppm were inhibitory.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120053","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":"Discovery of the TGCB microprotein translated from the lncRNA CHASERR.","authors":"Bernardo Bonilauri, Xiaochun Yang","doi":"10.1016/j.biochi.2026.10.008","DOIUrl":"10.1016/j.biochi.2026.10.008","url":null,"abstract":"<p><p>Long noncoding RNAs (lncRNAs) are key regulators of gene expression, and an increasing number have been found to contain small open reading frames (smORFs) that can be translated into functional microproteins. CHASERR is a conserved cis-regulatory lncRNA positioned upstream of CHD2, where it fine-tunes CHD2 dosage. Deletions spanning the CHASERR gene were recently identified in children with a syndromic, early-onset neurodevelopmental disorder, underscoring the clinical importance of this regulatory locus. Here, we report that CHASERR is not strictly noncoding but encodes a previously unannotated 41-amino-acid microprotein, which we name TGCB. Integrative analyses of bulk and single-cell transcriptomics, 47 public Ribo-seq datasets, including ribosome profiling datasets demonstrating initiation-associated P-site enrichment and canonical three-nucleotide translational periodicity, coding-potential predictors, and multispecies alignments support active translation and evolutionary constraint of the TGCB smORF. Public mass-spectrometry data provide reproducible peptide-spectrum matches corresponding to its N-terminal region, and TGCB-GFP overexpression supports nuclear and cytoplasmic localization. Structural prediction reveals a compact α-helical microdomain flanked by intrinsically disordered regions, characteristic of regulatory microproteins. Notably, all pathogenic deletions affecting the CHASERR-CHD2 region remove the entire TGCB coding sequence, raising the possibility that loss of this microprotein contributes to the associated neurodevelopmental phenotypes. These findings position CHASERR as a bifunctional transcript and uncover a conserved microprotein embedded within a clinically relevant regulatory locus.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120093","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":"Characterization of MdDOX-Co homologs revealed a novel gibberellin metabolic clade and a single-residue switch dictating the catalytic site.","authors":"Taiki Inoue, Yusaku Karasuno, Takatoshi Wakabayashi, Kazuma Okada, Sho Miyazaki, Ikuo Takahashi, Kazunori Okada, Tomohisa Kuzuyama, Masatoshi Nakajima","doi":"10.1016/j.biochi.2026.09.018","DOIUrl":"10.1016/j.biochi.2026.09.018","url":null,"abstract":"<p><p>The metabolism of gibberellin (GA) is generally mediated by GA 2-oxidase (GA2ox) through 2β-hydroxylation. These enzymes belong to the 2-oxoglutarate-dependent dioxygenase (2ODD, DOX) superfamily. However, MdDOX-Co, another 2ODD, was recently found to catalyze atypical GA 12α-hydroxylation. MdDOX-Co belongs to the DOXC41 clade, which is phylogenetically distant from the canonical GA2ox. The evolutionary and structural bases of this unique catalytic site remain unclear. In this study, we investigated the functional divergence of the DOXC41 clade. Through phylogenetic analyses, biochemical experiments with recombinant enzymes, and GC-MS detection, we discovered that MdDOX-Co homologs exhibit striking diversity in their GA hydroxylation sites, branching into two functional types: those possessing 12α-hydroxylation activity and those possessing 2-hydroxylation activity. We performed enzyme structure predictions, molecular docking, and molecular dynamics (MD) simulations to elucidate the mechanisms that dictate this functional diversity. These in silico approaches identified a key residue that distinguishes the two activities. Subsequent biochemical characterization using a synthesized variant demonstrated that a single-residue switch (T214P) shifted the catalytic activity of MdDOX-Co from 12α-hydroxylation to 2β-hydroxylation. Our findings provide new insights into the structural rationale of how a single amino acid dictates the hydroxylation sites of GA in this novel metabolic clade.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120043","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 riboflavin kinase domain is essential for FMNAT catalysis: A linker-dependent regulatory mechanism in Staphylococcus aureus FAD synthetase.","authors":"R Sahana, Anant Bakshi, Sandeep Kumar, Anusree Lohithakshan, Dandamudi Usharani, Chilkunda Nandini, Ravi Kumar","doi":"10.1016/j.biochi.2026.09.016","DOIUrl":"https://doi.org/10.1016/j.biochi.2026.09.016","url":null,"abstract":"<p><p>Flavin adenine dinucleotide (FAD) synthetase (FADS) from Staphylococcus aureus is a bifunctional enzyme comprising an N-terminal FMN adenylyltransferase (FMNAT) domain that catalyzes FAD synthesis and a C-terminal riboflavin kinase (RFK) domain responsible for riboflavin phosphorylation. While eukaryotic FMNAT and RFK homologs function as independently, the mechanistic basis for their fusion and interdependence in bacteria remains unclear. Here, we show that S. aureus FADS functions as an obligate structural assembly exhibiting pronounced functional asymmetry between its two domains. The isolated RFK domain retains substantial catalytic activity, with a k_cat of 14.5 min^-1, whereas the isolated FMNAT domain is catalytically inactive despite being properly folded. Perturbing the native inter-domain linker with flexible or rigid sequences severely compromises both domains, with FMNAT displaying a disproportionately greater functional loss. Biophysically, the isolated RFK domain exists predominantly as a dimer in solution, unlike the monomeric full-length enzyme, indicating that the native inter-domain linker and FMNAT domain influence the oligomeric state of RFK. Consistently, microscale thermophoresis shows a markedly reduced FMN affinity for the isolated FMNAT domain, and molecular dynamics simulations further indicate destabilization of the FMNAT active-site geometry without RFK. Together, these findings demonstrate that the RFK domain and native inter-domain linker act as essential structural elements stabilizing the FMNAT active site in a catalytically competent conformation, thereby enabling productive FAD synthesis and pointing to inter-domain coupling as a potentially important feature of bacterial FAD metabolism.</p>","PeriodicalId":93898,"journal":{"name":"Biochimie","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149120019","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}