Biochimica et biophysica acta. Proteins and proteomics最新文献

{"title":"Proteomic profiling of valproic acid-treated zebrafish embryos highlights dysregulation in energy and purine metabolism, and microtubule dynamics: Implications for autism spectrum disorder.","authors":"Saime Sürmen, Mustafa Gani Sürmen, Merih Beler, İsmail Ünal, Derya Cansız, Ebru Emekli-Alturfan","doi":"10.1016/j.bbapap.2026.141148","DOIUrl":"https://doi.org/10.1016/j.bbapap.2026.141148","url":null,"abstract":"<p><p>Valproate (VPA), a widely used anticonvulsant, is also employed to establish experimental autism spectrum disorder (ASD) models. This study aims to elucidate mechanisms underlying VPA's effects in ASD by analyzing proteomic profiles and oxidant-antioxidant dynamics in zebrafish embryos, uncovering the cellular pathways driving these changes. Zebrafish embryos were exposed to two concentrations of VPA (10 μM and 25 μM) for 72 h post-fertilization (hpf), and LC-MS/MS analyses were performed. Differentially expressed proteins (DEPs) were subjected to bioinformatic analysis to identify associated cellular pathways, and their biological significance was evaluated. Oxidant-antioxidant parameters and locomotor activities were determined. High-dose induced more pronounced proteomic changes, while most of the identified proteins in both groups, including key metabolic enzymes such as adenylate kinase 1 (Ak1), adenosine monophosphate deaminase 1 (Ampd1), pyruvate kinase (Pkmb) and creatine kinase (Ck), exhibited a dose-dependent decrease. Functional enrichment analyses revealed that these alterations were primarily associated with purine metabolism, energy metabolism, and microtubule dynamics. In addition, malondialdehyde, nitric oxide, and glutathione S-transferase, increased in a dose-dependent manner, whereas superoxide dismutase decreased. Decreased average speed, distance swam, and explored areas were found in both VPA treated groups, reflecting early sensorimotor dysfunction. Our findings demonstrate that VPA induces dose-dependent proteomic alterations in zebrafish embryos, with metabolic pathways and cytoskeletal dynamics being particularly affected. Extent of molecular disruptions appears to correlate with VPA concentration, suggesting potential implications for energy homeostasis and cellular structure. Understanding these effects could provide valuable insights into the developmental toxicity mechanisms of VPA and its broader biological significance.</p>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":" ","pages":"141148"},"PeriodicalIF":2.3,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147855864","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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 the interaction between the BH3-like domain of hepatitis B virus X protein and LC3B.","authors":"Hideki Kusunoki, Toshiyuki Tanaka, Takuo Mizukami, Kaori Wakamatsu, Takashi Nagata","doi":"10.1016/j.bbapap.2026.141149","DOIUrl":"https://doi.org/10.1016/j.bbapap.2026.141149","url":null,"abstract":"<p><p>Chronic infection with hepatitis B virus (HBV) remains a global health issue, leading to liver diseases such as chronic hepatitis B, cirrhosis, and hepatocellular carcinoma. The HBV X protein (HBx) promotes viral replication and disease progression by interacting with various host proteins. One of its functions involves binding to microtubule-associated protein 1 light chain 3B (LC3B), which mediates selective autophagy and facilitates the removal of the immune-related protein TNFRSF10B (tumor necrosis factor receptor superfamily 10B). However, even the mechanism by which HBx interacts with LC3B remained unclear. In this study, we focused on the HBx-LC3B interaction as a first step and identified a conserved LC3-interacting region motif (Trp120-X-X-Leu123) within the Bcl-2 homology 3 (BH3)-like domain of HBx that directly binds to LC3B. This interaction was characterized using isothermal titration calorimetry and nuclear magnetic resonance (NMR) spectroscopy. We present the first NMR structure of LC3B in complex with the HBx BH3-like peptide, revealing that it adopts an extended conformation upon binding and that Trp120 and Leu 123 are essential for LC3B recognition. Notably, the same portion forms an α-helix when binding to B-cell lymphoma 2 (Bcl-2) and B-cell lymphoma extra-large (Bcl-x_L), suggesting that HBx uses different conformations to interact with distinct targets. This structural plasticity may underlie the multifunctional roles of HBx.</p>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":" ","pages":"141149"},"PeriodicalIF":2.3,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147855817","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MS analysis of proteins concentrated on the surface of AFM chips from the blood plasma of healthy volunteers","authors":"Arina I. Gordeeva,&nbsp;Anastasia A. Valueva,&nbsp;Tatyana A. Materova,&nbsp;Elizaveta E. Rybakova,&nbsp;Maria O. Ershova,&nbsp;Nikita E. Vavilov,&nbsp;Victor G. Zgoda,&nbsp;Tatyana O. Pleshakova,&nbsp;Alexander I. Archakov","doi":"10.1016/j.bbapap.2026.141127","DOIUrl":"10.1016/j.bbapap.2026.141127","url":null,"abstract":"<div><div>Proteomic analysis of blood plasma plays a crucial role in biomedical research for biomarker discovery, development of diagnostic systems, and monitoring of treatment efficacy. In this study, we combine mass spectrometric analysis with surface-assisted protein concentration using specially prepared atomic force microscopy chips (AFM/MS) for plasma proteomic profiling. The chip surface is modified with a photocrosslinker that forms covalent bonds with protein functional groups during incubation in the analyzed solution. Using AFM chips followed by MS identification, the protein composition of 10²- and 10⁴-fold diluted blood plasma from a small cohort of conditionally healthy volunteers (<em>N</em> = 4) was analyzed, demonstrating interindividual variability in the number of adsorbed proteins below 8%. Analysis of the core proteome, defined as proteins consistently detected across all volunteers within each experimental condition, revealed dilution-dependent and partially non-overlapping protein sets, as well as marked differences between samples analyzed with and without the on-chip concentration step. Identified proteins were further characterized using literature-derived annotations. The AFM chip surface enabled concentration and detection of proteins spanning a broad reported plasma concentration range, from approximately ∼10⁻¹⁰ M to ∼10⁻⁶ M, indicating that plasma dilution and surface-assisted enrichment substantially influence proteome coverage. This approach provides a methodological basis for future comparative plasma proteomic studies of healthy individuals and patients for biomarker discovery and disease diagnostics.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141127"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146073968","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification of novel biomolecular characteristics and bioinformatic analyses of the anterior cingulate cortex in morphine-dependent mice via proteomic profiling","authors":"Jun-Xia Yang ,&nbsp;Song Yao ,&nbsp;Hong-Wei Cao ,&nbsp;Ping-Hao Li ,&nbsp;Shuo Yang ,&nbsp;Hai-Lei Ding","doi":"10.1016/j.bbapap.2026.141128","DOIUrl":"10.1016/j.bbapap.2026.141128","url":null,"abstract":"<div><div>Impaired function of the anterior cingulate cortex (ACC) is widely recognized as a critical factor in drug dependence. This study aimed to investigate protein alterations in the ACC of morphine-dependent mice using 4D label-free quantitative proteomics. Procrustes analysis and Pearson correlation analysis on the differentially expressed proteins (DEPs) and the phenotypes of morphine dependence identified 81 DEPs (<em>p</em>-value &lt;0.05). Advanced bioinformatics analysis of these DEPs suggested dysregulation of several biological pathways in the ACC of morphine-dependent mice, including mitochondrial energy metabolism, endoplasmic reticulum-to-nucleus signaling, inhibitory synapse assembly, and intracellular trafficking, secretion, and vesicle-mediated transport. These findings provide a basis for understanding the proteomic alterations and offer an integrated perspective on the biomolecular changes in the ACC associated with morphine dependence.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141128"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146131192","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Chemometric evaluation of key residues affecting the stability of cold shock proteins","authors":"Jack E. Buckley ,&nbsp;Nathaniel J. Zbacnik ,&nbsp;Charles S. Henry ,&nbsp;Mark Cornell Manning","doi":"10.1016/j.bbapap.2026.141126","DOIUrl":"10.1016/j.bbapap.2026.141126","url":null,"abstract":"<div><div>Reduced properties, also known as amino acid descriptors, quantify changes in physicochemical properties of amino acids upon mutation. Combined with PLS (partial least squares) modeling, the impact of various mutations on the conformational stability of cold shock proteins (CSPs) was examined. Consistent with the initial evaluation of these systems, electrostatic properties at a select number of central residues were found to govern the conformational stability of CSP mutants. In addition, the current studies found that packing efficiency within the β-sheet core and flexibility of the peptide backbone also contribute to the overall stability of these small proteins.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141126"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145994090","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Full-size recombinant ORF1p-L1 and RT domain of ORF2p-L1: Protein expression, purification and characterization","authors":"Vladislav Aksenov ,&nbsp;Maria G. Glazunova ,&nbsp;Igor P. Oscorbin ,&nbsp;Neonila V. Gorokhovets ,&nbsp;Maxim L. Filipenko ,&nbsp;Angelina V. Kurchatova ,&nbsp;Julia I. Svetlova ,&nbsp;Nikolay E. Kushlinskii ,&nbsp;Vasiliy N. Stepanenko ,&nbsp;Igor Ivanov","doi":"10.1016/j.bbapap.2026.141130","DOIUrl":"10.1016/j.bbapap.2026.141130","url":null,"abstract":"<div><div><em>Long interspersed nuclear elements-1 (LINEs-1)</em> are known to be active human retrotransposons containing two protein-coding genes, <em>ORF1</em> and <em>ORF2</em>, whose expression results in the production of two proteins—ORF1p-L1 and ORF2p-L1, respectively. Activation of <em>LINE-1</em> may occur during the early stages of lung, prostate, esophageal, colon or breast cancer progression, often without obvious pathological symptoms or any overt signs of disease. In this study, we developed a method for preparing the <em>LINE-1</em> proteins ORF1p-L1 and the reverse transcriptase (RT) domain of ORF2p-L1 and demonstrated their potential application as antigens in gastric cancer diagnostics. Both antigens were expressed as insoluble inclusion bodies in a bacterial expression system (<em>E. coli BL21 (DE3) pLysS)</em> using laboratory-scale fermentation. The preparation protocol involved solubilizing the inclusion bodies with a chaotropic agent, followed by multiple protein purification steps and subsequent renaturation of the proteins by dialysis under acidic conditions. At decreasing concentrations of the chaotropic agent, ORF1p-L1 and the RT domain of ORF2p-L1 were found to weakly bind to cation-exchange resins or to aggregate, whereas irreversible protein binding occurred under acidic conditions. The biological activity of the refolded ORF1p-L1 was confirmed by assessing its hybridization activity, while the reverse transcriptase activity of the RT domain of ORF2p-L1 was also successfully confirmed. Both refolded proteins reveal antigen-antibody response against antibodies in serum samples of patients with gastric cancer.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141130"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146137039","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cytotoxicity originates at the amorphous intermediate stage during amyloid-like oligomerization of serum albumin under mild denaturing conditions","authors":"Gulafsha ,&nbsp;Rinshu Singh ,&nbsp;Geeta Arya ,&nbsp;Surendra Nimesh ,&nbsp;Suhel Parvez ,&nbsp;Basir Ahmad","doi":"10.1016/j.bbapap.2025.141123","DOIUrl":"10.1016/j.bbapap.2025.141123","url":null,"abstract":"<div><div>Protein misfolding and aggregation into amyloid-like structures cause many pathological conditions and remain central to understanding protein homeostasis. Here, we report mechanistic insights into the aggregation of human serum albumin (HSA) under mild denaturing conditions. HSA adopts a partially unfolded intermediate state in mild denaturing conditions (1.8 M guanidine hydrochloride, pH 7.4) that is highly prone to aggregation. Kinetic analyses reveal a two-step pathway: an initial rapid formation of amorphous aggregates detected by light scattering, followed by their slower structural reorganization into β-sheet-rich spherical oligomers monitored by thioflavin T binding. Biophysical characterization using circular dichroism, dynamic light scattering (DLS), electron microscopy, tinctorial assays and mathematical modeling of the kinetics confirmed the role of amorphous aggregates as an intermediate state in oligomer formation. Both amorphous and spherical oligomeric species exhibited comparable cytotoxicity toward HEK 293 cells. These findings highlight a distinct aggregation route for HSA, expanding our understanding of how metastable intermediates facilitate toxic oligomer formation, and providing a model for dissecting early aggregation events in multidomain proteins.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141123"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145853726","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative proteomic profiling of advanced, injectable, and titanium-prepared platelet rich fibrins (PRF): Insights into functional divergence and clinical potential","authors":"Sri Vidhya Marimuthu ,&nbsp;Tamizhini Loganathan ,&nbsp;Muthukumar Santhanakrishnan ,&nbsp;C. George Priya Doss ,&nbsp;Magesh Ramasamy","doi":"10.1016/j.bbapap.2025.141121","DOIUrl":"10.1016/j.bbapap.2025.141121","url":null,"abstract":"<div><div>Platelet-rich fibrin (PRF) has emerged as a pivotal autologous biomaterial in regenerative medicine. Yet, comparative proteomic insights into its diverse formulations advanced PRF (A-PRF), injectable PRF (I-PRF), and titanium-prepared PRF (T-PRF) remain scarce. This study presents a comprehensive proteomic characterization of A-PRF, I-PRF, and T-PRF, employing imputed intensity data, principal component analysis (PCA), correlation matrices, and differential expression analysis. PCA identified distinct clustering patterns, reinforcing reproducible and formulation-specific proteomic signatures. Correlation and intensity distribution analyses demonstrated strong intra-group consistency, with A-PRF exhibiting the highest reproducibility, whereas T-PRF displayed greater variability. Differential expression analysis further delineated significant inter-group molecular variations, revealing unique proteomic compositions. Protein-protein interaction (PPI) network analysis identified key regulatory proteins such as fibrinogen alpha (FGA), fibrinogen beta (FGB), and fibronectin 1 (FN1), In contrast, enrichment analyses revealed biological processes related to coagulation, platelet activation, immune modulation, and extracellular matrix dynamics. Functional pathway mapping underscored divergent biological roles, A-PRF was enriched in coagulation-related pathways, while I-PRF linked to lipid metabolism and immune signaling. These findings validate the molecular distinctiveness of PRF variants and establish a proteomic framework for their precision-driven application in tissue engineering and regenerative therapy.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141121"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145793039","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Electrochemical enzyme biosensing reveals differential abundance of GPI-anchored metalloprotease across Leishmania (Viannia) braziliensis subpopulations","authors":"Fatemeh Farshchi ,&nbsp;Geovane Dias-Lopes ,&nbsp;Vitor Ennes-Vidal ,&nbsp;Luzia Monteiro de Castro Cortes ,&nbsp;Mohammad Hasanzadeh ,&nbsp;Franklin Souza-Silva ,&nbsp;Carlos Roberto Alves","doi":"10.1016/j.bbapap.2026.141129","DOIUrl":"10.1016/j.bbapap.2026.141129","url":null,"abstract":"<div><div><em>Leishmania (Viannia) braziliensis</em> Thor strain contains subpopulations Thor03, Thor10, and Thor22 with distinct biological and infection profiles in vitro and vivo. This study investigated GPI-anchored metalloproteases from the Thor strain and its subpopulations using phospholipase C treatment followed by Zn²⁺-charged affinity chromatography. An electrochemical biosensor based on screen-printed carbon electrodes and differential pulse voltammetry was used to detect metalloprotease activity and responsiveness to the ortho-phenanthroline inhibitor. Promastigotes and axenic amastigotes metalloproteases exhibit different binding profiles to the ortho-phenanthroline inhibitor which led to specific discrimination of these analytes. The highest sensitivity was observed in proteases from Thor10 promastigotes and Thor axenic amastigotes, with detection limits of 5 μM and 1 μM, respectively. The detectable concentration range for these analytes varied among subpopulations: for promastigotes, from 1000 μM down to 5 μM (with Thor10 showing the broadest range), and for axenic amastigotes, from 1000 μM down to 1 μM (with Thor and Thor10 exhibiting the greatest sensitivity). These differences suggest a variable abundance of metalloproteases among subpopulations. The findings underscore the biosensor's potential as a sensitive, specific tool for real-time analysis of <em>Leishmania</em> enzymes, offering a novel, systematic approach for studying enzyme function and virulence in parasite phenotypes.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141129"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146091752","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Purification of human sperm-specific PGK2 and assay development for drug screening for potential non-hormonal contraceptives","authors":"Samprikta Kundu ,&nbsp;Safia Baig ,&nbsp;Ariba Mahmood ,&nbsp;Aritra Ghosh ,&nbsp;Anam Khan ,&nbsp;Ritika Gupta ,&nbsp;Jayanta Sarkar ,&nbsp;Saman Habib ,&nbsp;Sanjay Batra ,&nbsp;Radha Rangarajan ,&nbsp;Niti Kumar ,&nbsp;Shashi Kumar Gupta","doi":"10.1016/j.bbapap.2026.141125","DOIUrl":"10.1016/j.bbapap.2026.141125","url":null,"abstract":"<div><div><ul><li><span>●</span><span><div>PGK2 is a sperm-specific glycolytic enzyme that catalyzes a reversible phosphotransferase reaction. It is critical for sperm motility and male fertility, making it a compelling protein target for non-hormonal contraception.</div></span></li><li><span>●</span><span><div>High-quality purification of human proteins and robust primary screening assays are vital for drug discovery.</div></span></li><li><span>●</span><span><div>We have established a method for the purification of recombinant human sperm-specific PGK2 through overexpression in the HEK293 cell line.</div></span></li><li><span>●</span><span><div>A luminescence-based, coupled biochemical assay was established to screen PGK2 inhibitors, which may provide an opportunity to explore non-hormonal, male-specific contraceptives.</div></span></li></ul></div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 3","pages":"Article 141125"},"PeriodicalIF":2.3,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145987916","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}