Pub Date : 2024-09-18DOI: 10.1080/07391102.2024.2404145
Aftab Alam,Mohammed H Alqarni,Bader S Alotaibi,Farhan R Khan,Md Shamsher Alam,Faris F Aba Alkhayl,Ali A Alhafi,Turki M Almutairi,Zeyad M Alharbi,Faez Falah Alshehri
Tuberculosis (TB) is a global health challenge; therefore, there is an urgent requirement to develop a novel and more effective anti-TB therapeutic. This study targeted the isocitrate lyase (ICL) protein due to its pivotal role in the pathogenicity of Mycobacterium tuberculosis (Mtb). Virtual screening of 8752 bioactive compounds used an ML-based QSAR model and molecular docking. ADMET testing was performed on the top three hits to identify the compound most closely mimicking a drug molecule. The top hits, 648 and 2785758, showed high binding affinity towards ICL with -7.3 and -7 kcal/mol, comparable to the control. These molecules also showed strong binding with the residue Asp108, which plays a vital role in ICL activity. Molecular dynamics simulations showed stability for 648 and 2785758, comparable to the control compound used in this study. It was found that 648 bound to the protein maintained the RMSD constant and consistent at 0.3 nm for a complete 100 ns simulation. 2785758 showed a comparable RMSD trend to the control. Both 648 and 2785758 showed high RMSF for critical residue Asp108. Further, PCA and FEL confirmed the formation of a stable complex. MM/GBSA estimations of binding free energy indicated that compounds 648 had an elevated level of stability (ΔGTOTAL = -28.11 kcal/mol) and 2785758 (ΔGTOTAL = -21.05 kcal/mol). This study suggests that compounds 648 and 2785758 can potentially affect the activity of ICL, leading to its inactivation and ultimately preventing the progression of tuberculosis.Communicated by Ramaswamy H. Sarma.
{"title":"Cheminformatics-enhanced discovery of therapeutic agents targeting isocitrate lyase in Mycobacterium tuberculosis infections.","authors":"Aftab Alam,Mohammed H Alqarni,Bader S Alotaibi,Farhan R Khan,Md Shamsher Alam,Faris F Aba Alkhayl,Ali A Alhafi,Turki M Almutairi,Zeyad M Alharbi,Faez Falah Alshehri","doi":"10.1080/07391102.2024.2404145","DOIUrl":"https://doi.org/10.1080/07391102.2024.2404145","url":null,"abstract":"Tuberculosis (TB) is a global health challenge; therefore, there is an urgent requirement to develop a novel and more effective anti-TB therapeutic. This study targeted the isocitrate lyase (ICL) protein due to its pivotal role in the pathogenicity of Mycobacterium tuberculosis (Mtb). Virtual screening of 8752 bioactive compounds used an ML-based QSAR model and molecular docking. ADMET testing was performed on the top three hits to identify the compound most closely mimicking a drug molecule. The top hits, 648 and 2785758, showed high binding affinity towards ICL with -7.3 and -7 kcal/mol, comparable to the control. These molecules also showed strong binding with the residue Asp108, which plays a vital role in ICL activity. Molecular dynamics simulations showed stability for 648 and 2785758, comparable to the control compound used in this study. It was found that 648 bound to the protein maintained the RMSD constant and consistent at 0.3 nm for a complete 100 ns simulation. 2785758 showed a comparable RMSD trend to the control. Both 648 and 2785758 showed high RMSF for critical residue Asp108. Further, PCA and FEL confirmed the formation of a stable complex. MM/GBSA estimations of binding free energy indicated that compounds 648 had an elevated level of stability (ΔGTOTAL = -28.11 kcal/mol) and 2785758 (ΔGTOTAL = -21.05 kcal/mol). This study suggests that compounds 648 and 2785758 can potentially affect the activity of ICL, leading to its inactivation and ultimately preventing the progression of tuberculosis.Communicated by Ramaswamy H. Sarma.","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"28 1","pages":"1-18"},"PeriodicalIF":0.0,"publicationDate":"2024-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142267551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-13DOI: 10.1080/07391102.2024.2402692
K Aiswarya,T Vishwam,T Vamshi Prasad,C Thirmal,K C James Raju
The complex dielectric permittivity of L-Proline in water and ethanol solutions with molar concentrations ranging from 0.025 M to 0.15 M was measured by open-ended coaxial probe technique. The measurements were carried out across a frequency span of 0.02 < ν/GHz < 20 and temperatures varying from 298.15 K to 323.15 K. The densities (ρ) and refractive index (nD) of the L-proline in aqueous and ethanol solutions were also determined to provide insights into the solute-solvent interactions in the system. The Havriliak-Negami equation was employed to compute the dielectric relaxation time of the mixtures. The relaxation time of L-Proline in an ethanol medium was found to be higher than that of L-Proline in an aqueous medium due to the greater degree of self-association of ethanol molecules. Additionally, the relaxation time of the mixtures lengthened with rising molar concentration, which is attributed to the presence of hydrogen bonds among L-Proline and aqueous/ethanol molecules. The strength of the hydrogen bond interaction of L-Proline in both mediums was calculated using single-point energy calculations employing IEFPCM/PCM solvation models through DFT/B3LYP and MP2 approaches with a 6-311 G ++ (d, p) basis set. The results were correlated with the hydrogen bond strength, Gibbs' free energy of activation parameter, and dipole-dipole interactions.Communicated by Ramaswamy H. Sarma.
采用开口同轴探针技术测量了 L-脯氨酸在摩尔浓度为 0.025 M 至 0.15 M 的水和乙醇溶液中的复介电常数。测量的频率跨度为 0.02 < ν/GHz < 20，温度范围为 298.15 K 至 323.15 K。此外，还测定了 L-脯氨酸在水溶液和乙醇溶液中的密度 (ρ)和折射率 (nD)，以便深入了解体系中溶质与溶剂之间的相互作用。计算混合物的介电弛豫时间时采用了 Havriliak-Negami 方程。结果发现，由于乙醇分子的自结合程度较高，L-脯氨酸在乙醇介质中的弛豫时间高于 L-脯氨酸在水介质中的弛豫时间。此外，混合物的弛豫时间随着摩尔浓度的增加而延长，这是因为 L-脯氨酸和水/乙醇分子之间存在氢键。通过 DFT/B3LYP 和 MP2 方法，采用 6-311 G ++ (d, p) 基集，利用 IEFPCM/PCM 溶解模型进行单点能量计算，计算了两种介质中 L-脯氨酸氢键相互作用的强度。计算结果与氢键强度、吉布斯活化自由能参数和偶极-偶极相互作用相关。
{"title":"Molecular interaction studies of L-proline in water and ethanol at different temperatures using dielectric relaxation, refractive index and DFT methods.","authors":"K Aiswarya,T Vishwam,T Vamshi Prasad,C Thirmal,K C James Raju","doi":"10.1080/07391102.2024.2402692","DOIUrl":"https://doi.org/10.1080/07391102.2024.2402692","url":null,"abstract":"The complex dielectric permittivity of L-Proline in water and ethanol solutions with molar concentrations ranging from 0.025 M to 0.15 M was measured by open-ended coaxial probe technique. The measurements were carried out across a frequency span of 0.02 < ν/GHz < 20 and temperatures varying from 298.15 K to 323.15 K. The densities (ρ) and refractive index (nD) of the L-proline in aqueous and ethanol solutions were also determined to provide insights into the solute-solvent interactions in the system. The Havriliak-Negami equation was employed to compute the dielectric relaxation time of the mixtures. The relaxation time of L-Proline in an ethanol medium was found to be higher than that of L-Proline in an aqueous medium due to the greater degree of self-association of ethanol molecules. Additionally, the relaxation time of the mixtures lengthened with rising molar concentration, which is attributed to the presence of hydrogen bonds among L-Proline and aqueous/ethanol molecules. The strength of the hydrogen bond interaction of L-Proline in both mediums was calculated using single-point energy calculations employing IEFPCM/PCM solvation models through DFT/B3LYP and MP2 approaches with a 6-311 G ++ (d, p) basis set. The results were correlated with the hydrogen bond strength, Gibbs' free energy of activation parameter, and dipole-dipole interactions.Communicated by Ramaswamy H. Sarma.","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"21 1","pages":"1-13"},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142269652","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has quickly become a global health pandemic. Among the viral proteins, RNA-dependent RNA polymerase (RdRp) is responsible for viral genome replication and has emerged as a promising target against SARS-CoV-2 infection. Dietary bioactive compounds represent an important source of evolutionarily optimized molecules with antiviral properties against SARS-CoV-2 RdRp. We investigated the inhibitory potential effects of different phytochemicals against SARS-CoV-2 RdRp, including andrographolide, kaempferol, resveratrol, and silibinin. Unlike the other investigated compounds, kaempferol exhibited a significant dose-dependent in vitro inhibition of SARS-CoV-2 RdRp activity. To assess the binding interactions and stability of the SARS-CoV-2 RdRp-kaempferol complex, we performed in silico techniques, including molecular docking, quantum chemical calculation, and molecular dynamics simulations. We found strong binding affinities and stability between kaempferol and SARS-CoV-2 RdRp variants (Wuhan and Omicron). These findings provide valuable insights into the antiviral properties of kaempferol as a stable inhibitor of SARS-CoV-2 RdRp.Communicated by Ramaswamy H. Sarma.
{"title":"Kaempferol as a novel inhibitor of SARS-CoV-2 RNA-dependent RNA polymerase.","authors":"Alessandro Medoro,Francesca Benedetti,Mariano Intrieri,Tassadaq Hussain Jafar,Sawan Ali,Truong Tan Trung,Daniela Passarella,Saba Ismail,Davide Zella,Giovanni Scapagnini,Sergio Davinelli","doi":"10.1080/07391102.2024.2402695","DOIUrl":"https://doi.org/10.1080/07391102.2024.2402695","url":null,"abstract":"Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has quickly become a global health pandemic. Among the viral proteins, RNA-dependent RNA polymerase (RdRp) is responsible for viral genome replication and has emerged as a promising target against SARS-CoV-2 infection. Dietary bioactive compounds represent an important source of evolutionarily optimized molecules with antiviral properties against SARS-CoV-2 RdRp. We investigated the inhibitory potential effects of different phytochemicals against SARS-CoV-2 RdRp, including andrographolide, kaempferol, resveratrol, and silibinin. Unlike the other investigated compounds, kaempferol exhibited a significant dose-dependent in vitro inhibition of SARS-CoV-2 RdRp activity. To assess the binding interactions and stability of the SARS-CoV-2 RdRp-kaempferol complex, we performed in silico techniques, including molecular docking, quantum chemical calculation, and molecular dynamics simulations. We found strong binding affinities and stability between kaempferol and SARS-CoV-2 RdRp variants (Wuhan and Omicron). These findings provide valuable insights into the antiviral properties of kaempferol as a stable inhibitor of SARS-CoV-2 RdRp.Communicated by Ramaswamy H. Sarma.","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"181 1","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142217345","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-08-28DOI: 10.1080/07391102.2024.2384693
Published in Journal of Biomolecular Structure and Dynamics (Vol. 42, No. sup1, 2024)
发表于《生物分子结构与动力学杂志》（第 42 卷，第 sup1 期，2024 年）
{"title":"Book of Abstracts. The 1st Next Generation Conversations: Albany at Ruston 2024 (The 21st Albany Conversation)","authors":"","doi":"10.1080/07391102.2024.2384693","DOIUrl":"https://doi.org/10.1080/07391102.2024.2384693","url":null,"abstract":"Published in Journal of Biomolecular Structure and Dynamics (Vol. 42, No. sup1, 2024)","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"34 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142217289","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-18DOI: 10.1080/07391102.2024.2332507
Ali A. Rabaan, Wadha A. Alfouzan, Mohammed Garout, Muhammad A. Halwani, Nouf Alotaibi, Mubarak Alfaresi, Nawal A. Al Kaabi, Zainab H. Almansour, Ahmed S. Bueid, Amjad A. Yousuf, Hamza M. A. Eid, Mohammed Alissa
In response to the escalating threat of drug-resistant fungi to human health, there is an urgent need for innovative strategies. Our focus is on addressing this challenge by exploring a previously ...
为应对耐药真菌对人类健康不断升级的威胁，迫切需要创新的策略。我们的重点是通过探索一种以前...
{"title":"Antifungal drug discovery for targeting Candida albicans morphogenesis through structural dynamics study","authors":"Ali A. Rabaan, Wadha A. Alfouzan, Mohammed Garout, Muhammad A. Halwani, Nouf Alotaibi, Mubarak Alfaresi, Nawal A. Al Kaabi, Zainab H. Almansour, Ahmed S. Bueid, Amjad A. Yousuf, Hamza M. A. Eid, Mohammed Alissa","doi":"10.1080/07391102.2024.2332507","DOIUrl":"https://doi.org/10.1080/07391102.2024.2332507","url":null,"abstract":"In response to the escalating threat of drug-resistant fungi to human health, there is an urgent need for innovative strategies. Our focus is on addressing this challenge by exploring a previously ...","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"37 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140615046","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-11DOI: 10.1080/07391102.2024.2325107
Swati Gupta, Debnath Pal
We compare the WebGeSTer and INtrinsic transcription TERmination hairPIN (INTERPIN) databases used for intrinsic transcription termination (ITT) site prediction in bacteria. The former deploys inve...
{"title":"Detection of intrinsic transcription termination sites in bacteria: consensus from hairpin detection approaches","authors":"Swati Gupta, Debnath Pal","doi":"10.1080/07391102.2024.2325107","DOIUrl":"https://doi.org/10.1080/07391102.2024.2325107","url":null,"abstract":"We compare the WebGeSTer and INtrinsic transcription TERmination hairPIN (INTERPIN) databases used for intrinsic transcription termination (ITT) site prediction in bacteria. The former deploys inve...","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"36 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140588877","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-09DOI: 10.1080/07391102.2024.2330710
Balajee Ramachandran, Ahmed Nadeem, Aruchamy Mohanprasanth, Muthupandian Saravanan
Globally the SARS-CoV-2 viral infection demands for the new drugs, the TMPRSS2 target plays a vital role in facilitating the virus entry. The aim of the present study is to identify the potential p...
{"title":"Prediction of deleterious non-synonymous SNPs of TMPRSS2 protein combined with Molecular Dynamics Simulations and free energy analysis to identify the potential peptide substrates against SARS-CoV-2","authors":"Balajee Ramachandran, Ahmed Nadeem, Aruchamy Mohanprasanth, Muthupandian Saravanan","doi":"10.1080/07391102.2024.2330710","DOIUrl":"https://doi.org/10.1080/07391102.2024.2330710","url":null,"abstract":"Globally the SARS-CoV-2 viral infection demands for the new drugs, the TMPRSS2 target plays a vital role in facilitating the virus entry. The aim of the present study is to identify the potential p...","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"197 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140588974","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-08DOI: 10.1080/07391102.2024.2330714
Miroslava Nedyalkova, Ralitsa Robeva, Julia Romanova, Kirila Yovcheva, Marco Lattuada, Vasil Simeonov
Glucagon-like peptide-1 (GLP-1) is an intestinal hormone that exerts its pleiotropic effects through a specific GLP-1 receptor (GLP-1R). The hormone–receptor complex might regulate glucose-dependen...
{"title":"In silico screening of potential agonists of a glucagon-like peptide-1 receptor among female sex hormone derivatives","authors":"Miroslava Nedyalkova, Ralitsa Robeva, Julia Romanova, Kirila Yovcheva, Marco Lattuada, Vasil Simeonov","doi":"10.1080/07391102.2024.2330714","DOIUrl":"https://doi.org/10.1080/07391102.2024.2330714","url":null,"abstract":"Glucagon-like peptide-1 (GLP-1) is an intestinal hormone that exerts its pleiotropic effects through a specific GLP-1 receptor (GLP-1R). The hormone–receptor complex might regulate glucose-dependen...","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"52 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140588955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-05DOI: 10.1080/07391102.2024.2317981
T. Sankar Ganesan, N. Elangovan, Munusamy Thirumavalavan, Shanthi Seenan, S. Sowrirajan, S. Chandrasekar, Natarajan Arumugam, Abdulrahman I. Almansour, Sakkarapalayam M. Mahalingam, Datta Darshan V M, Subbarao Kanchi, Venketesh Sivaramakrishnan
The N, N’-(1,2-phenylene) bis (1- (4- chlorophenyl) methanimine) (CS4) was synthesized and characterized by infrared (IR), absorption (UV-vis) and NMR (1H and 13C) spectral analyses. The structural...
{"title":"Synthesis, topology, molecular docking and dynamics studies of o-phenylenediamine derivative","authors":"T. Sankar Ganesan, N. Elangovan, Munusamy Thirumavalavan, Shanthi Seenan, S. Sowrirajan, S. Chandrasekar, Natarajan Arumugam, Abdulrahman I. Almansour, Sakkarapalayam M. Mahalingam, Datta Darshan V M, Subbarao Kanchi, Venketesh Sivaramakrishnan","doi":"10.1080/07391102.2024.2317981","DOIUrl":"https://doi.org/10.1080/07391102.2024.2317981","url":null,"abstract":"The N, N’-(1,2-phenylene) bis (1- (4- chlorophenyl) methanimine) (CS4) was synthesized and characterized by infrared (IR), absorption (UV-vis) and NMR (1H and 13C) spectral analyses. The structural...","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"51 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140588963","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-03-20DOI: 10.1080/07391102.2024.2329291
Olalekan Onisuru, Ikechukwu Achilonu
Research has spotlighted glutathione transferase (GST) as a promising target for antimalarial drug development due to its pivotal role in cellular processes, including metabolizing toxins and manag...
{"title":"Describing the ligandin properties of Plasmodium falciparum and vivax glutathione transferase towards bromosulfophthalein from empirical and computational modelling viewpoints","authors":"Olalekan Onisuru, Ikechukwu Achilonu","doi":"10.1080/07391102.2024.2329291","DOIUrl":"https://doi.org/10.1080/07391102.2024.2329291","url":null,"abstract":"Research has spotlighted glutathione transferase (GST) as a promising target for antimalarial drug development due to its pivotal role in cellular processes, including metabolizing toxins and manag...","PeriodicalId":15085,"journal":{"name":"Journal of Biomolecular Structure and Dynamics","volume":"16 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140172209","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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