Biochimica et biophysica acta. Proteins and proteomics最新文献

{"title":"Exploratory chromosome 14-focused transcriptomic profiling of PSEN1-associated familial Alzheimer's disease across brain regions.","authors":"Jangampalli Adi Pradeepkiran, Manne Munikumar, More Pallavi, Debi Prasad Pradhan, Jagadeesh Maddineni, Mounish Kosanam, Sreekar Srichurnam, Thejomayi Malempati, Aasritha Thota, S B Sainath","doi":"10.1016/j.bbapap.2026.141192","DOIUrl":"https://doi.org/10.1016/j.bbapap.2026.141192","url":null,"abstract":"<p><p>Familial Alzheimer's disease (FAD) is an inherited form of early-onset Alzheimer's disease associated with pathogenic variants in presenilin 1 (PSEN1). To explore chromosome 14-associated transcriptional patterns in FAD across anatomically distinct brain regions, publicly available RNA sequencing (RNA-Seq) datasets from frontal cortex, temporal cortex, and whole-brain samples were analyzed. Because one FAD sample and one control sample were available for each brain region, expression differences were evaluated descriptively using observed log₂ fold-change values rather than conventional inferential differential-expression statistics. Functional annotation and protein-protein interaction analyses were subsequently used to provide biological context for the observed expression patterns. Distinct regional expression patterns were observed within the chromosome 14-focused dataset. Higher expression was observed for representative genes including FITM1, IFI27, AHSA1, and NFKBIA in the frontal cortex, and DHRS4L2, ESR2, GPR65, EFCAB11, and HOMEZ in the temporal cortex. The observed expression patterns were associated with inflammatory, cellular stress, metabolic, receptor-mediated, proteostatic, and neuronal signaling-related functions. Network analysis was used to contextualize these expression patterns rather than to infer causal regulatory relationships. Five representative proteins-NFKBIA, ESR2, GPR65, AHSA1, and IFI27-were further examined structural information to provide structural context for selected transcriptomic observations. Given the absence of biological replication and the chromosome 14-focused design, these findings should be considered descriptive and hypothesis-generating. Independent replicated cohorts and complementary transcriptomic, proteomic, and functional studies are required to determine the reproducibility and biological relevance of the observed patterns.</p>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":" ","pages":"141192"},"PeriodicalIF":2.2,"publicationDate":"2026-10-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149223258","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":"Rational attenuation of elapid long-chain neurotoxin by targeted residue substitution and disulfide architecture simplification: implications for receptor interaction and immune recognition.","authors":"Víctor Carpanta, Iván Arenas, Herlinda Clement, Estuardo López-Vera, Gerardo Corzo","doi":"10.1016/j.bbapap.2026.141191","DOIUrl":"10.1016/j.bbapap.2026.141191","url":null,"abstract":"<p><p>Elapid long-chain neurotoxins (LNTxs) exert their toxicity through high-affinity binding to nicotinic acetylcholine receptors (nAChRs). Specific residues mediate this process, including basic (Lys23, Arg33, Arg36, Lys49), structural (Cys26, Cys30), and aromatic (Phe29) amino acids. To investigate the functional and immunogenic implications of modifying these residues, we designed two recombinant variants of a consensus LNTx. The first variant, rLcNTx V1, contains charge-reversal mutations at four key basic positions, while the second, rLcNTx V2, lacks the segment corresponding to the fifth disulfide bond. We expressed both variants in Escherichia coli Origami cells. rLcNTx V1 was recovered in a soluble form, but rLcNTx V2 was present only in inclusion bodies. We assessed the binding affinity of both proteins to muscle and neuronal nicotinic acetylcholine receptors (nAChRs) and observed no channel blockade for either variant, as expected. While this lack of activity in rLcNTx V2 points to the structural importance of the fifth disulfide region, it also suggests that its deletion disrupts the structure of the tip of loop II. Immunizing rabbits with these proteins elicited antibodies capable of recognizing α-bungarotoxin and various elapid venoms, but they failed to neutralize venom toxicity in vivo. These results emphasize that preserving the native electrostatic and conformational integrity of the basic core is essential for maintaining neutralizing epitopes in LNTxs.</p>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":" ","pages":"141191"},"PeriodicalIF":2.2,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149190838","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}