Journal of Biological Chemistry最新文献

{"title":"Nitric oxide attenuates PI4P accumulation at the ER membrane to inhibit encephalomyocarditis virus (EMCV) replication selectively in β-cells.","authors":"Alyssa L Gehant,Joshua D Stafford,Polly A Hansen,Katherine R Harty,Aaron Naatz,John A Corbett","doi":"10.1016/j.jbc.2025.110798","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110798","url":null,"abstract":"Viral infection, particularly by members of the picornavirus family, has been associated with autoimmune diabetes (T1D) onset. The encephalomyocarditis virus (EMCV) is a mouse-tropic member of the picornavirus family that stimulates innate immune activation, leading to the production of cytokines. In response to cytokines, β-cells express inducible nitric oxide synthase (iNOS) and produce low micromolar levels of the free radical, nitric oxide. We have previously shown that, due to its inhibitory action on mitochondrial oxidation and depletion of cellular ATP, nitric oxide selectively attenuates EMCV replication in and lysis of β-cells. In this study, we show that one mechanism by which nitric oxide inhibits EMCV replication is by attenuating the accumulation of phosphatidylinositol-4-phosphate (PI4P) at the endoplasmic reticulum (ER) membrane. As a result, viral replication complex formation is prohibited, and viral replication is effectively prevented. In agreement with previous studies, we show that these observations are selective for β-cells and due to a loss of cellular ATP.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"41 1","pages":"110798"},"PeriodicalIF":4.8,"publicationDate":"2025-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145254541","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Unraveling the pathway of Copper Delivery to Cytochrome c oxidases in the Free-Living Bacterium Caulobacter vibrioides.","authors":"Hala Kasmo,Jacquie Abolia Tepusa,Rubén Garcia-Dominguez,Chloe Piette,Marc Dieu,Damien Devos,Jean-Yves Matroule","doi":"10.1016/j.jbc.2025.110786","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110786","url":null,"abstract":"Copper (Cu) is an essential micronutrient that serves as a cofactor for many enzymes but becomes toxic when present in excess. In most bacteria, CopA-like P1B-type ATPases mediate Cu detoxification by exporting cytoplasmic Cu to the periplasm or extracellular environment. In this study, we show that Caulobacter vibrioides lacks a canonical CopA-like ATPase but encodes a single FixI/CcoI-type Cu-transporting ATPase, previously implicated in Cu delivery to the cbb3-type cytochrome c oxidase (Cox) in species such as Rhodobacter capsulatus. C. vibrioides harbors two terminal cytochrome c oxidases in its cytoplasmic membrane: an aa3-type and a cbb3-type Cox. We also demonstrate that the activity of cbb3-Cox requires the FixI-type Cu transporter and the periplasmic Cu chaperone PccA. In contrast, aa3-Cox activity depends on PccA and the inner membrane-bound protein CtaG. Since the mechanism of Cu acquisition for aa3-Cox remains largely unknown, we conducted a genetic screen and identified a novel outer membrane TonB-dependent receptor (TccA) that is specifically required for aa3-Cox function. We also showed that cbb3-Cox is upregulated under microaerobic conditions, possibly such as those encountered on solid media where O2 diffusion is limited. Under normoxic conditions, the expression and the activity of cbb3-Cox decrease, and aa3-Cox becomes the predominant terminal oxidase. These findings demonstrate that C. vibrioides differentially utilizes its Cox enzymes in response to O2 availability and relies on a distinct Cu trafficking pathway for their maturation, including an outer membrane component that has not been previously described in bacterial Cu homeostasis.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"22 1","pages":"110786"},"PeriodicalIF":4.8,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246833","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural Insights into Hormone Recognition and G-Protein Coupling of the Urotensin-II Receptor.","authors":"Tianyu Gao,Chongzhao You,Yinglong Cao,Xiaofang Xu,Qingning Yuan,Shiyi Shen,H Eric Xu,Jia Duan","doi":"10.1016/j.jbc.2025.110794","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110794","url":null,"abstract":"Urotensin-II (U-II) is a potent vasoconstrictor peptide that interacts with the human urotensin-II receptor (UTR), a class A G protein-coupled receptor (GPCR) that primarily couples with Gq proteins. In this study, we present the cryo-electron microscopy structure of the miniGq-coupled UTR bound to the potent UTR agonist P5U, providing insights into unique ligand recognition and activation mechanisms. Unlike typical linear peptides, the cyclic structure of P5U engages the receptor's transmembrane domains through key side chain interactions involving residues F6, W7, K8, and Y9, which are crucial for receptor activation. Comparative analysis with somatostatin receptors (SSTRs) reveals distinct ligand specificity, driven by variations in side chain composition. Notably, we identify F2746.51 as the toggle switch residue in UTR, in contrast to the classical W6.48 seen in other GPCRs. Our findings elucidate the structural basis for UTR's Gq coupling specificity, highlighting unique Gαq interactions. This study advances the understanding of U-II signaling and offers a foundation for developing selective UTR modulators, with potential therapeutic implications for cardiovascular diseases linked to dysregulated U-II activity.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"19 1","pages":"110794"},"PeriodicalIF":4.8,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246786","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Redox Partner Adrenodoxin Induces Substrate Binding to Steroidogenic Cytochrome P450 11B2 and 11A1 by Promoting A Conformational Change.","authors":"Cara L Loomis,Michelle Redhair,Sang-Choul Im,Emily E Scott","doi":"10.1016/j.jbc.2025.110792","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110792","url":null,"abstract":"In humans, cytochrome P450 (CYP) 11A1 and 11B2 play crucial roles in the steroidogenic pathway. CYP11A1 is involved in the first step in the steroidogenic pathway, converting cholesterol to pregnenolone, whereas CYP11B2 completes the final step in aldosterone synthesis. Each is a drug target for a distinct disease, and detailed information about enzyme kinetics and function could inform drug development. Both enzymes require the common redox partner adrenodoxin. Adrenodoxin allosterically modulates CYP11B2 function separate from its role in electron transfer. Herein, stopped-flow investigations establish that adrenodoxin is also an allosteric modulator of CYP11A1 substrate binding. For both enzymes, a kinetic modeling approach was used to elucidate the substrate binding mechanisms in the absence and presence of adrenodoxin. This analysis determined that substrate binding to both enzymes is best described by a complex, 4-state mechanism. Substrate 11-deoxycorticosterone binds CYP11B2 primarily through a branched induced fit mechanism, and the presence of adrenodoxin shifts the mechanism to a 4-state closed model containing both induced fit and conformational selection steps. CYP11A1 primarily binds its substrate 20R,22R-dihydroxycholesterol through a 4-state closed mechanism, while increasing adrenodoxin results in enhancement of the conformational selection step. Overall, this demonstrates the complexity of both P450 substrate binding and its fine-tuning by interactions with redox partners.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"22 1","pages":"110792"},"PeriodicalIF":4.8,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246787","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"SH2-mediated steric occlusion of the C2 domain regulates autoinhibition of SHIP1 inositol 5-phosphatase.","authors":"Emma E Drew, Hunter G Nyvall, Matthew A H Parson, Reed K Talus, John E Burke, Scott D Hansen","doi":"10.1016/j.jbc.2025.110788","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110788","url":null,"abstract":"<p><p>The Src homology 2 (SH2) domain containing inositol polyphosphate 5-phosphatase 1 (SHIP1) is an immune cell specific enzyme that regulates phosphatidylinositol-(3,4,5)-trisphosphate signaling at the plasma membrane following receptor activation. SHIP1 plays an important role in processes such as directed cell migration, endocytosis, and cortical membrane oscillations. Alterations in SHIP1 expression have been shown to perturb myeloid cell chemotaxis and differentiation. In the brain, SHIP1 regulate microglial cell behaviors, which has been linked to Alzheimer's disease. Understanding the structural and functional relationships of SHIP1 is critical for developing ways to modulate SHIP1 membrane localization and lipid phosphatase activity during immune cell signaling. Recently, we discovered that the N-terminal SH2 domain of SHIP1 suppresses lipid phosphatase activity. SHIP1 autoinhibition can be relieved through interactions with receptor-derived phosphotyrosine (pY) peptides presented on membranes or in solution. Using hydrogen-deuterium exchange mass spectrometry (HDX-MS) we identified intramolecular contacts between the N-terminal SH2 domain and CBL1 motif of the C2 domain that limit SHIP1 membrane localization and activity. Single molecule measurements of purified SHIP1 on supported lipid bilayers and in neutrophil-like cells support a model in which the SH2 domain blocks membrane binding of the central catalytic module. Mutations that disrupt autoinhibition enhance the membrane binding frequency and increase the catalytic efficiency of SHIP1. Although dimerization of SHIP1 enhances membrane localization and the apparent phosphatase activity, it is not required for SHIP1 autoinhibition. Overall, our results provide new insight concerning SHIP1's structural organization, membrane binding dynamics, and the mechanism of autoinhibition.</p>","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":" ","pages":"110788"},"PeriodicalIF":4.0,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145251125","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Variation in type IV pilus stability modulates DNA-uptake and biofilm formation.","authors":"Yafan Yu,Rabab Mahdi,Ahmad Al-Hilfy Leon,Nam Vo,Reese Lofgren,Jean Luc Mutabazi,Kurt H Piepenbrink","doi":"10.1016/j.jbc.2025.110787","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110787","url":null,"abstract":"Type IV pili are helical filaments composed of protein subunits which are produced by numerous taxa of bacteria, including Acinetobacter. Type IV pili are extended out from the cell by extension enzyme complexes, which extract subunits from the membrane and insert them into the base of the filament, but can also be retracted by reverse rotation catalyzed by a retraction enzyme. Type IV pili have diverse functions, including twitching motility and DNA-uptake, which require retraction, and host adhesion and bacterial aggregation, which do not. Acinetobacter bacteria, including International Clone I (IC-I) and International Clone II (IC-II) strains, show variable phenotypes in assays of type IV pilus-dependent functions. Here, we show this variation is the result of differentiation of type IV pilus subtypes in Acinetobacter, which we defined based on the sequence of the major subunit, PilA. These subtypes show variable efficiency in pilus retraction between pilus subtypes, and from that, a differential balance between retraction-dependent and retraction-independent functions. In both naturally-occurring pilA variants from the IC-I and IC-II groups and isogenic strains complemented with IC-I or IC-II pilA, the IC-I pilus subtype promotes greater twitching motility and DNA-uptake while the IC-II pilus subtype promotes biofilm formation while showing reduced capacity for DNA-uptake and twitching motility, similar to a retraction-deficient mutant and consistent with the hypothesis that pilus retraction of the IC-II pilus is naturally deficient. This defect in retraction was sufficient to increase the level of piliation on the cell surface when we compared the yields of T4P sheared from the cell surface from IC-I pilA and IC-II pilA complements in an isogenic background. Complementation with IC-II pilA results in greater levels of surface PilA per cell than equivalent complementation with an IC-I pilA gene. Additionally, direct comparisons of pilus stability between type IV pili isolated from IC-I pilA and IC-II pilA complements show greater thermostability for the IC-II pili, supporting the hypothesis that pilus stability can impede retraction and increase piliation.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"82 1","pages":"110787"},"PeriodicalIF":4.8,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246785","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The non-conserved integrin cytoplasmic region determines integrin subtype-specific characteristics by modulating talin1 binding kinetics.","authors":"Naoyuki Kondo,Kenji Fukui,Yuji Kamioka,Yoshihiro Ueda,Yoshiki Ikeda,Taiju Matsushita,Ryo Yazaki,Tatsuo Kinashi","doi":"10.1016/j.jbc.2025.110793","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110793","url":null,"abstract":"Talin governs integrin adhesion by binding to the cytoplasmic tail (CT) of integrin β subunits, but the effects of integrin subtype-specific variations on talin interactions remain unclear. Here, we identify a non-conserved region within the integrin-CT, termed the WN linker, that modulates talin1 binding kinetics and integrin adhesiveness. Single-molecule imaging in live lymphocytes revealed that talin1 bound more strongly to β2 than β7 integrin, with higher off-rates in β7 in vivo. This difference was due to the unique NND sequence in the β2 WN linker compared with KQDS in the β7 WN linker. Structural and biochemical analyses showed that NND established a tighter interaction with talin, whereas KQDS bent, narrowing the interaction area and weakening the interaction. Substituting the NND sequence in β2 with KQDS impaired inside-out signaling- and ligand binding-induced conformational activation of LFA1. Multiple sequence alignment and single-molecule binding analyses revealed that the NND sequence is highly conserved only in mammalian β2 integrins, and that the second asparagine in NND, a residue absent in non-mammalian β2 integrins and other integrins, plays a key role in talin1 binding. Parallel observations in β3 integrins reinforced the pivotal role of the WN linker in modulating integrin-talin affinity. These observations highlight the WN linker as a novel regulator of integrin-talin binding strength and adhesiveness diversity.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"61 1","pages":"110793"},"PeriodicalIF":4.8,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246789","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Sirtuin 6 is a histone delactylase.","authors":"Garrison A Nickel, Nicholas J Pederson, Faheem, Zhenyu Yang, Jack Bulf, Katharine L Diehl","doi":"10.1016/j.jbc.2025.110795","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110795","url":null,"abstract":"<p><p>Histone lactylation (Kla) is a post translational modification (PTM) that is derived from metabolic lactate. Histone Kla has been extensively studied in the field of inflammation resolution and macrophage polarization but has also been implicated in diverse cellular processes including differentiation, various wound repair phenotypes, and oncogenesis in several cancer models. While mechanistic connections between histone Kla and transcriptional changes have been studied in very limited contexts, general mechanistic details describing how regulation of gene expression by histone Kla occurs are scarce. It is hypothesized that histone Kla may be installed either through nonenzymatic means or by acetyltransferases like p300, and it is known that Class I HDACs and Sirtuins 1-3 can remove histone Kla. Here, we identified histone delactylase activity of the deacylase enzyme Sirtuin 6 (Sirt6), a member of the Class III HDAC family known to have roles in regulating metabolic homeostasis. We characterized the ability of Sirt6 to delactylate histones in vitro and in a mammalian cell culture model. We identified H3K9 and H3K18, canonical histone sites of Sirt6-catalyzed deacetylase activity, as sites of its delactylase activity. We also demonstrated that Sirt6 and the Class I HDACs exhibit some degree of non-overlapping delactylase activity, suggesting that they represent different cellular axes of regulating gene expression via controlling levels of histone Kla.</p>","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":" ","pages":"110795"},"PeriodicalIF":4.0,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145251137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In vivo analysis of Drosophila chondroitin sulfate biosynthetic genes.","authors":"Tomomi Izumikawa,Ayano Moriya,Eriko Nakato,Kako Yamamoto,Raiki Sano,Takuya Akiyama,Akiko Kinoshita-Toyoda,Hidenao Toyoda,Hiroshi Nakato","doi":"10.1016/j.jbc.2025.110783","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110783","url":null,"abstract":"Chondroitin sulfate (CS) is an evolutionarily conserved class of glycosaminoglycans and is found in most animal species. Previous studies of CS-deficient Drosophila models, Chondroitin sulfate synthase (Chsy) and Chondroitin polymerizing factor (Chpf) mutants, demonstrated the importance of CS in structural integrity of the basement membrane and organ shape maintenance. However, biosynthetic mechanisms of Drosophila CS remain to be elucidated. To investigate the CS biosynthesis in Drosophila, we generated mutants for two additional biosynthetic enzyme genes, CS N-acetylgalactosaminyltransferase (Csgalnact) and CS 4-O sulfotransferase (C4st), using CRISPR/Cas9 mutagenesis. Csgalnact null mutants show moderate changes in CS biosynthesis, including reduced CS in the larval brain and altered CS chain length. We found that this gene is dispensable for normal viability and morphogenesis. On the other hand, C4st mutants show more severe defects, including a high level of lethality and a folded wing phenotype. The C4st mutation not only eliminates CS sulfation but increases production of unsulfated chondroitin, suggesting the existence of a compensatory feedback mechanism. Both Csgalnact and C4st mutants show impaired adult negative geotaxis behavior, consistent with CSPGs' roles in the neuromuscular systems. Our study revealed unique and poorly understood features of invertebrate CS biosynthesis and provides novel in vivo toolsets to investigate CSPG functions in development.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"15 1","pages":"110783"},"PeriodicalIF":4.8,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cyanophycinase is required for heterotrophy in cyanobacteria.","authors":"Éva Kiss,Martin Moos,Jan Mareš,Stanislav Opekar,Lenka Tomanová,Paulina Duhita Anindita,Martin Lukeš,Petra Urajová,Roman Sobotka","doi":"10.1016/j.jbc.2025.110791","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110791","url":null,"abstract":"Cyanophycin is a biopolymer of arginine and aspartate, and it is found in various prokaryotes. Two key enzymes of cyanophycin metabolism are cyanophycin synthase (CphA) producing cyanophycin, and cyanophycinase (CphB) catalysing the first step of cyanophycin degradation. CphB is a well conserved enzyme found in the majority of cyanobacteria, and ubiquitous amongst those that are known to perform heterotrophy besides their primary photosynthetic lifestyle. Unlike in diazotrophs, where CphB is connected to the mobilization of fixed nitrogen, the importance of this enzyme remains elusive in non-diazotrophs, such as the model cyanobacterium Synechocystis sp. PCC 6803. The Synechocystis ΔcphB deletion strain does not accumulate cyanophycin and shows no photoautotrophic growth defect. However, we show here that ΔcphB is not able to proliferate heterotrophically, although the CphA-less strain exhibits no obvious defect under heterotrophic conditions. Metabolomics profiling revealed that ΔcphB failed to upregulate the biosynthesis of arginine and displayed missregulated carbon and nucleoside metabolisms. These suggest that CphB is needed for the activation of the arginine pathway, which appeared to be crucial for balancing the nitrogen and carbon ratio during the acclimation to heterotrophy. On the other hand, the interaction of CphB with the Arg biosynthetic enzyme, acetylornithine aminotransferase, stimulated the hydrolysis of cyanophycin in an in vitro assay. These data, together with the metabolic profiles of ΔcphB, imply that the catabolism of cyanophycin and the biosynthesis of Arg are mutually co-regulated metabolic pathways.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"213 1","pages":"110791"},"PeriodicalIF":4.8,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246759","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}