Biochimica et biophysica acta. Proteins and proteomics最新文献

{"title":"Integrated computational and biological assays to identify and validate L. donovani homoserine dehydrogenase inhibitors","authors":"Shalu Verma ,&nbsp;Shaswat Sengar ,&nbsp;Abdul Basit Khan ,&nbsp;Anil Kumar Shakya ,&nbsp;J. Venkatesh Pratap","doi":"10.1016/j.bbapap.2025.141112","DOIUrl":"10.1016/j.bbapap.2025.141112","url":null,"abstract":"<div><div>The Neglected Tropical Disease (NTD) Leishmaniasis continues to pose a serious global health burden affecting millions globally. Visceral leishmaniasis, one of three clinical forms, can be fatal, if left untreated. Current treatment regimen relies mostly on re-purposed drugs and is limited by toxicity, high cost and the emergence of drug resistance, highlighting the need for safer, targeted therapies. In this study, we characterized <em>Leishmania donovani</em> homoserine dehydrogenase (<em>Ld</em>HSD), a crucial enzyme in the aspartate pathway. As no human homolog exists, it represents a promising target for selective therapeutic intervention. <em>Ld</em>HSD was purified to homogeneity, characterized biophysically and its activity biochemically assayed. Docking of the substrate (L-homoserine) and the cofactor (NADP⁺) to the <em>Ld</em>HSD homology model identified adjacent but discrete binding pockets. Structure-based virtual screening of the Maybridge Compound Library was subsequently performed and the top 10 substrate-site bound compounds were taken for experimental validation. Two of the three piperidine/piperazine scaffold compounds inhibited <em>Ld</em>HSD activity by ∼90 %. These findings highlight the therapeutic potential of targeting <em>Ld</em>HSD for the development of novel, selective anti-leishmanial agents and establish a strong foundation for future optimization of these identified inhibitors.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141112"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145511648","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":"Molecular insights into diosgenin's role in preventing protein aggregation in neurodegenerative diseases","authors":"Nagma Parveen ,&nbsp;Faizan Abul Qais ,&nbsp;Mohammad Faheem","doi":"10.1016/j.bbapap.2025.141116","DOIUrl":"10.1016/j.bbapap.2025.141116","url":null,"abstract":"<div><div>Neurodegenerative disorders (ND) such as Parkinson's and Alzheimer's progressively impair the nervous system, leading to cognitive deterioration and motor dysfunction. A primary factor in these diseases is the accumulation of misfolded protein aggregates, which interfere with cellular processes and ultimately result in neuronal death. Preventing the formation of these toxic aggregates has the potential to protect neurons and slow the advancement of disease. This study examined the impact of diosgenin on protein aggregation, utilizing human serum albumin (HSA) as model protein. Diosgenin reduced ThT fluorescence by 64.35 % and decreased turbidity by 62.61 %, indicating a notable suppression of protein aggregation. The % α-helix in HSA experienced a decline from 57.68 % to 8.82 %, but diosgenin treatment restored it to 43.89 %. Binding studies demonstrated that diosgenin interacts with HSA with −11.0 kcal/mol binding energy, facilitated by van der Waals, hydrophobic and hydrogen bonding interactions, and stability of HSA-diosgenin complex was also validated using molecular simulations. To further elucidate the aggregation inhibition mechanism by diosgenin, advanced molecular dynamics simulations were employed. Diosgenin increased the solvent accessibility of the HSA₂₈₂_–₂₉₂ oligomers, reduced β-sheet formation, and prevented H-bond interactions, key factors in aggregate formation. Molecular simulation of Aβ oligomers (Aβ₁₆_–₂₂) also showed the diosgenin prevents oligomerization and β-sheet formation. We show that diosgenin presents a promising alternative due to its ability to stabilize protein structures and inhibit protein aggregation, making it a potential therapeutic candidate for NDs. However, further experimental validation in animal models is necessary to confirm diosgenin's anti-aggregation effects, particularly of amyloid-forming proteins.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141116"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145572899","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":"AttnSeq-PPI: Enhancing protein-protein interaction network prediction using transfer learning-driven hybrid attention","authors":"Dipayan Sarkar,&nbsp;Chiranjib Sarkar","doi":"10.1016/j.bbapap.2025.141102","DOIUrl":"10.1016/j.bbapap.2025.141102","url":null,"abstract":"<div><div>Study of protein-protein interaction (PPI) network is fundamental to all cellular processes in living organisms. PPI study based on experimental techniques such as high-throughput assays, mass spectrometry is time-consuming and expensive. Computational techniques like molecular docking are restricted to availability of 3D protein structures and not suitable for large numbers of proteins. On the contrary Sequence-based PPI study is advantageous over the limitations of above techniques. Sequence-based PPI study has gained a broader scope with the help of deep learning techniques and large language model (LLM). In this study, we proposed AttnSeq-PPI, a deep learning framework based on two channels of hybrid attention mechanism. The protein sequences are embedded in high dimensional space using ProtT5 language model. In our model hybrid attention mechanism is designed by combining self-attention and cross-attention which enable the model to extract features from each protein with respect to the contextual features of both the proteins. The hybrid attention mechanism effectively captures long-range dependencies within protein sequences as well as interacting features of both proteins. The model was trained and evaluated based on 5-fold cross validation on intra-species and multi-species datasets. Additionally, four datasets of independent species and true PPI network datasets were used for validation. AttnSeq-PPI demonstrates superior generalization and outperforms existing models, achieving 99 % accuracy for both human and multi-species datasets. It can provide prediction of novel PPIs with fewer false negatives and higher precision. Additionally, we developed a web-based tool on AttnSeq-PPI accessible at <span><span>https://compbiosysnbu.in/attnseqppi/</span><svg><path></path></svg></span> to provide PPI prediction based on protein sequences.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141102"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145370181","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":"Phafin2 modulates the aggregation of NLRP3 on dispersed trans-Golgi network","authors":"Yurou Li,&nbsp;Kaiyong Zheng,&nbsp;Chunsheng Chen,&nbsp;Yi Wu,&nbsp;Shuai Li,&nbsp;Weihong Zhou,&nbsp;Xinqi Liu","doi":"10.1016/j.bbapap.2025.141101","DOIUrl":"10.1016/j.bbapap.2025.141101","url":null,"abstract":"<div><div>NLRP3 is one of the central players in innate immune signaling. Upon stimulation, NLRP3 could oligomerize and recruit ASC, NEK7, and caspase 1 (CASP1), then assemble into inflammasome, triggering downstream inflammation and pyroptosis. Recently, it was reported that both potassium efflux dependent and independent signaling, could lead to the formation of dispersed TGN (dTGN), where NLRP3 was initially recruited. Interestingly, the phosphatidylinositol-4-phosphate (PI4P) enriched on dTGN is indispensable for NLRP3 recruitment. In this study, we found that Phafin2, which can bind PI4P and PI3P via its PH and FYVE domains respectively, could modulate the NLRP3 aggregation on dTGN, thus regulating the cell pyroptosis. Phafin2 affects NLRP3 aggregation indirectly by influencing the constitution of dTGN. Our study unravels Phafin2 might act as a critical regulator of NLRP3-mediated pyroptosis, thus providing a new therapeutic target for human diseases associated with NLRP3-involved inflammation.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141101"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145298143","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":"Multifunctionality analysis of serine hydroxymethyltransferases from human and Escherichia coli","authors":"Mahiro Hayashi ,&nbsp;Kumiko Sakai-Kato ,&nbsp;Tetsuya Miyamoto","doi":"10.1016/j.bbapap.2025.141107","DOIUrl":"10.1016/j.bbapap.2025.141107","url":null,"abstract":"<div><div>Serine hydroxymethyltransferase (SHMT) catalyzes the conversion of <span>l</span>-serine and tetrahydrofolate (THF) to glycine and 5,10-methylenetetrahydrofolate, respectively. In a previous study, we found that human and <em>Escherichia coli</em> SHMTs possess THF-dependent <span>d</span>-serine dehydratase activity, which degrades <span>d</span>-serine to pyruvate and ammonia. Some activities including aldolase and racemase activities have also been reported for SHMTs. In the present study, we investigated the multifunctionality of <em>E. coli</em> SHMT and two human SHMTs. All three SHMTs displayed high aldolase activity toward <span>l</span>-<em>allo</em>-threonine and <span>l</span>-<em>threo</em>-phenylserine, and measurable activity toward <span>l</span>-threonine, but they did not act on <span>d</span>-<em>allo</em>-threonine and <span>d</span>-threonine. The catalytic efficiency (<em>k</em>_cat/<em>K</em>_m) for <span>l</span>-<em>allo</em>-threonine was higher than for <span>l</span>-<em>threo</em>-phenylserine. None of the SHMTs displayed racemase activity toward various amino acids, although slight alanine racemase activity was detected for <em>E. coli</em> SHMT. Likewise, none of the SHMTs showed lyase, aminotransferase, or aspartate decarboxylase activities, and none exhibited dehydratase activity toward other hydroxy amino acids except <span>d</span>-serine. SHMTs are multifunctional enzymes possessing canonical hydroxymethyltransferase, <span>d</span>-serine dehydratase, and low-specificity <span>l</span>-threonine aldolase activities.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141107"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145424731","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 new protein-coding potential in Leishmania braziliensis using a proteogenomics approach","authors":"Aditi Shenoy ,&nbsp;Soumi Chowdhury ,&nbsp;Shubhankar Pawar ,&nbsp;Nitin Tupperwar ,&nbsp;Harsh Pawar","doi":"10.1016/j.bbapap.2025.141108","DOIUrl":"10.1016/j.bbapap.2025.141108","url":null,"abstract":"<div><div>American tegumentary leishmaniasis (ATL) is primarily caused by <em>Leishmania</em> (<em>Viannia</em>) species such as <em>Leishmania braziliensis</em>, <em>Leishmania panamensis</em>, and <em>Leishmania guyanensis</em>, which show complex genomic organisation and stage-specific adaptations underlying their pathogenicity. Despite the availability of its reference genome, limitations in gene annotation persist due to the presence of hypothetical proteins, pseudogenes, and unrecognised coding regions. In this study, we used a proteogenomic approach integrating publicly available high-resolution mass spectrometry data with a custom six-frame translated genome database to refine the genome annotation of <em>L. braziliensis</em> strain MHOM/BR/75/M2904. Utilising stringent database-dependent searches with a 1 % false discovery rate, we identified many unique peptides, of which 1034 were genome search-specific peptides (GSSPs) mapping exclusively to unannotated genomic regions. These GSSPs facilitated the discovery of 56 novel protein-coding genes and the correction of 228 existing gene models, including N- and C-terminal extensions. Notably, several novel genes encode proteins with conserved domains such as membrane attack complex/perforin (MACPF), kinesin K39, and peptidase S9/S15, suggesting functional relevance in parasite biology. Our findings demonstrate the power of proteogenomics to uncover cryptic protein-coding regions and improve genome annotations beyond conventional predictions. This refined annotation enhances our understanding of <em>L.</em> <em>braziliensis</em> biology, providing a more accurate proteomic landscape that can inform studies on parasite virulence, host interaction, and potential therapeutic targets. The study underscores the importance of integrating proteomic evidence with genomic data to capture the full coding potential of kinetoplastid parasites, paving the way for improved diagnostics and interventions against leishmaniasis.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141108"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145424732","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":"Enhancement of the nucleotide incorporation activity of the terminal deoxynucleotidyl transferase by N-terminal truncation and DNA-binding protein modulation","authors":"Antos B. Sachanka,&nbsp;Stafaniya S. Douhaya,&nbsp;Veronika V. Shchur,&nbsp;Aliaksei V. Yantsevich","doi":"10.1016/j.bbapap.2025.141114","DOIUrl":"10.1016/j.bbapap.2025.141114","url":null,"abstract":"<div><div>Terminal deoxynucleotidyl transferase (TdT) is a unique DNA polymerase that catalyzes the template-independent addition of nucleotides to the 3′ terminus of single-stranded DNA. Its distinctive catalytic properties have been exploited in aptasensor design, nanomaterial synthesis, DNA mutagenesis, innovative data storage based on single-nucleotide DNA sequences, and enzymatic <em>de novo</em> DNA synthesis. However, the application of the enzyme is limited by its low expression yield, poor thermostability, and reduced nucleotide incorporation efficiency with substrates prone to forming secondary structures. To overcome these limitations, we engineered a bovine TdT variant truncated at the N-terminus by 148 residues (148_TrTdT), which demonstrates a twofold increase in expression yield, a 5 °C improvement in thermostability, and over 30 % enhancement in nucleotide incorporation efficiency and processivity compared to the wild-type enzyme. Moreover, we demonstrated that DNA-binding proteins enhance the nucleotide incorporation activity of native TdT (10-fold) and 148_TrTdT (2-fold) when substrates are prone to forming secondary structures. Collectively, the methodologies implemented in this study exhibit significant potential for enhancing the efficiency of enzymatic <em>de novo</em> DNA synthesis, thereby enabling the development of new bioengineering and biomedical applications.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141114"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145511594","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":"Structure prediction and engineering of de novo proteins","authors":"Lin Qi ,&nbsp;Mark Isalan","doi":"10.1016/j.bbapap.2025.141100","DOIUrl":"10.1016/j.bbapap.2025.141100","url":null,"abstract":"<div><div><em>De novo</em> proteins represent a challenging frontier at the intersection of evolutionary biology and synthetic biology. Broadly, the term encompasses two distinct categories: naturally evolved <em>de novo</em> proteins, which arise from previously non-coding DNA, and synthetically designed <em>de novo</em> proteins, which are created from scratch through computational and experimental methods. This review provides an overview of the definitions, history, functional significance, and investigation methods for both categories. By examining potential challenges in current <em>de novo</em> protein research, this review highlights the growing convergence between natural evolutionary processes and rational protein engineering, reflecting their importance in biological discovery and human innovations.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141100"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145079608","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":"Biophysical characterization of Hpa1 protein from Xanthomonas orzyae","authors":"Jaimini Patoliya ,&nbsp;Khushali Thaker ,&nbsp;Jahanvi Bajpai ,&nbsp;Dhaval Patel ,&nbsp;Nayan Jain ,&nbsp;Prasant Kumar ,&nbsp;Rushikesh Joshi","doi":"10.1016/j.bbapap.2025.141111","DOIUrl":"10.1016/j.bbapap.2025.141111","url":null,"abstract":"<div><div><em>Xanthomonas oryzae pv. oryzae</em> (Xoo), the causative agent of bacterial blight in rice, secretes a suite of effectors via the Type III Secretion System (T3SS), among which harpin proteins like Hpa1 are key modulators of plant immunity. Unlike other T3SS effectors, Hpa1 lacks enzymatic activity and instead acts as a biostimulant, promoting growth and defense responses. In this study, the <em>hpa1</em> gene was cloned from <em>Xoo</em> BXO1 strain and successfully expressed in <em>E. coli</em> Rosetta cells. The recombinant protein was purified using Ni-NTA chromatography, and SDS-PAGE, Western blotting, and MALDI-TOF analysis confirmed its molecular weight (∼16.5 kDa). Biophysical characterization revealed a predominance of α-helical content, with CD spectroscopy. Thermal and chemical unfolding of Hpa1 was evaluated using CD spectroscopy (with GuHCl) and ANS fluorescence (with GuHCl and urea), revealing moderate stability. pH-dependent stability assessed by fluorescence showed optimal structural retention at pH 5. TFE-induced structural modulation, studied by CD, demonstrated concentration-dependent α-helix enhancement. Thermal stability was assessed through four approaches: SDS-PAGE, CD at 222 nm, SYPRO Orange-based thermal shift assay, and HR-inducing activity in <em>Nicotiana benthamiana</em>. These results collectively confirmed that native Hpa1 conformation is not necessary for its function. These findings highlight its potential as a protein-based biostimulant for agricultural applications and its utility as a model for studying intrinsically disordered yet functionally stable proteins.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141111"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145480512","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":"Deciphering the structural attributes of PPAR-γ and SIRT1 to identify their dual activators using a combined molecular modeling approach","authors":"Swati Dogra ,&nbsp;Arijit Bhattacharya ,&nbsp;Gera Narendra,&nbsp;Shraddha Gautam,&nbsp;Om Silakari","doi":"10.1016/j.bbapap.2025.141104","DOIUrl":"10.1016/j.bbapap.2025.141104","url":null,"abstract":"<div><div>PPAR-γ and SIRT1 are the emerging targets that are vital in diabetes and diabetic complications. So, the development of dual activators for PPAR-γ and SIRT1 can be a good strategy in the treatment of diabetes and diabetic complications and in order to reduce the adverse effects that occur from the activation of these targets. The network analysis was applied to study the protein-protein interactions. Similarity-based virtual screening was done to screen Fisetin-based molecules, and docking analysis was performed for both targets. In addition, an ADME study and electrostatic complementarity analysis were conducted to study the role of binding energies between the ligands and the targets. The Molecular Dynamics (MD) simulation was performed to study the stable binding conformation. Different validation metrics from MD analysis, such as <em>RMSD, RMSF, R</em>_<em>g</em><em>,</em> PCA and free energy landscape (FEL), were analysed to evaluate the stability of the compounds with the target proteins. Moreover, the WaterSwap and MMPBSA analyses were also done to calculate the binding free energy of the compounds. The findings from this extensive evaluation depicted that the selected three molecules can be used as potent and safe dual activators of PPAR-γ and SIRT1 to combat diabetes and several diabetic complications.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1874 1","pages":"Article 141104"},"PeriodicalIF":2.3,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145318137","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}