ACS Infectious Diseases最新文献

{"title":"Activity of Thiourea-Linked Diamidines against Multidrug-Resistant Staphylococcus aureus","authors":"Yi Jin,&nbsp;Sandra Story,&nbsp;Jordan Chamberlin,&nbsp;Dev P. Arya","doi":"10.1021/acsinfecdis.6c00572","DOIUrl":"https://doi.org/10.1021/acsinfecdis.6c00572","url":null,"abstract":"<p><em>Staphylococcus aureus</em> isa leadingcause of antibiotic-resistant infections worldwide. Therefore, thereis a constant need to develop new growth inhibitors. Pentamidine analogs(PAs) composed of thiourea-linked amidines were evaluated for activityagainst methicillin-resistant <em>S. aureus</em> (MRSA) and other Gram-positive bacteria. <em>S. aureus</em>, MRSA, <em>Staphylococcus epidermidis</em>, <em>Streptococcus pyogenes</em>, <em>Mycobacterium</em>, and <em>Bacillus</em> were highly susceptible with minimal inhibitory concentration (MIC)values ranging from 1.56 to 6.25 μM, whereas <em>Enterococcus</em> species and <em>Clostridioides difficile</em> were not as susceptible with MICs of 50to ≥100 μM. For <em>S. aureus</em>, MRSA and VISA strains, PAs showed ∼4-fold lower MICs whencompared to pentamidine (PNT). The concentration of PAs needed tolyse 50% of red blood cells (HC₅₀) was ∼16–32-foldhigher than their corresponding MICs. For PNT, a lower HC₅₀/MIC range of 1.25–5 was observed. Approximately 60% of MRSAwas cleared from infected <em>Caenorhabditis elegans</em> by the PAs. PAs also provided 100% protection in a septicemia modelof infected mice. Morphological changes induced by these compoundsindicate disruption of cell membrane integrity, where &gt;80% of treatedbacterial cells took up propidium iodide in a permeation assay. Importantly,there was a lack of resistance observed with the PAs, compared tothe fairly rapid and stable resistance occurrence for drugs commonlyused to treat <em>S. aureus</em> infection.These results reflect the potential of such compounds as potentialnew tools to optimize and combat the menace of drug-resistant <em>S. aureus</em>.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2874–2891"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729539","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Divergent MBL-Fold Metallo-Hydrolase (Kmh-1) from Klebsiella pneumoniae Confers Aztreonam Degradation and Expands the β-Lactamase Landscape","authors":"Jyoti Barman,&nbsp;Partho Biswas,&nbsp;Partha Roy,&nbsp;Saugata Hazra","doi":"10.1021/acsinfecdis.5c01093","DOIUrl":"10.1021/acsinfecdis.5c01093","url":null,"abstract":"<p>The widespread use and misuse of β-lactam antibioticsexertselective pressure on bacteria, driving the continuous emergence ofnovel metallo-β-lactamases (MBLs). Characterizing newly evolvedMBLs is critical for elucidating the molecular basis of their antimicrobialresistance (AMR) and may contribute to designing novel inhibitors.In this study, we have done the functional characterization of anMBL-fold metallo-hydrolase from <em>Klebsiella pneumoniae</em> (designated Kmh-1), which shares low sequence similarity with B1MBLs. Unlike B1 enzymes, where zinc binding motifs are strictly conserved(H116–H118–H196 and D120–C221–H263), Kmh-1retains only Asp120 and His263, marking its clear divergence. Phylogeneticanalysis further establishes its divergence from the existing B1 MBLs.Kmh-1 has activity toward diverse β-lactams, and zinc is requiredfor enzymatic activity. This study also finds aztreonam hydrolyzingactivity in this enzyme. Kmh-1–aztreonam interaction is validatedthrough circular dichroism (CD) and fluorescence spectroscopy. AlphaFoldstructure prediction and docking studies confirm that Kmh-1 can accommodateaztreonam in the active site and disclose the probable aztreonam bindingresidues. Our results demonstrate a plausible explanation of effectiveaztreonam binding in Kmh-1, which is similar to that of clinicallyrelevant NDM-1. IC₅₀ values against different inhibitorsare determined for Kmh-1, and the IC₅₀ value against bicyclicboronate is observed in the nM range. Together, these findings establishKmh-1 as an MBL-fold metallo-hydrolase endowed with aztreonam bindingand hydrolysis, expanding the landscape of resistance and providinga framework for inhibitor design.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2614–2626"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147968502","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rational Substitution-Driven Enhancement of Anti-Mycobacterium tuberculosis Activity in a Quinoline–Isonicotinic Acid Hydrazide Hybrid","authors":"Govinda Raju Vadankula,&nbsp;Anushka Agarwal,&nbsp;Yandrapally Sriram,&nbsp;Shalini Saxena,&nbsp;Rashmita Biswas,&nbsp;Hepsibha Chirra,&nbsp;Pavitra S. Thacker,&nbsp;Mohammed Arifuddin,&nbsp;Vijay Nema,&nbsp;Alvala Mallika,&nbsp;Sharmistha Banerjee","doi":"10.1021/acsinfecdis.6c00376","DOIUrl":"10.1021/acsinfecdis.6c00376","url":null,"abstract":"<p>The obstinatproblem of drug resistancein tuberculosis (TB) requiressustained efforts in the search for new drug molecules. Building onour previously developed synthetic hybrid compound, UH-NIP-16, whichdemonstrated anti-<em>Mycobacterium tuberculosis</em> (<em>M.tb</em>) activity, we synthesized and evaluated 15new derivatives to improve its potency. Among these, two lead compounds,UN-7 and UN-14, bearing hydrogen and methyl substitutions at the sixthposition, respectively, along with a 2-phenoxy moiety, exhibited a∼5-fold reduction in MIC₅₀ values across laboratory,clinical, and multidrug-resistant <em>M.tb</em> strains relativeto UH-NIP-16. Both compounds displayed a bacteriostatic mechanismof action and exhibited predominantly additive or indifferent interactionprofiles in combinatorial antitubercular studies. Importantly, UN-7and UN-14 showed minimal cytotoxicity toward mammalian cells and effectivelyreduced intracellular bacterial burden in an <em>in vitro</em> infection model. A coupled enzymatic assay revealed that UN-7 andUN-14 inhibited mycobacterial shikimate kinase (Mt-SK) activity byapproximately 65%, a target not inhibited by the parent compound UH-NIP-16. <em>In silico</em> ADMET analyses indicated several favorable drug-likenessproperties despite predicted liabilities, including Ames mutagenicityand low aqueous solubility. Collectively, these findings identifyUN-7 and UN-14 as structure–activity relationship (SAR)-guidedderivatives of the UH-NIP-16 scaffold with improved antimycobacterialactivity and promising potential for further antitubercular lead development.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2799–2814"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148409695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Platanosides, a Promising Class of Plant-Derived Antibiotics, Are Effective against a Suite of Clinically Derived MDR and Drug-Sensitive Staph and Strep spp.","authors":"Cody F. Dickinson,&nbsp;Menny M. Benjamin,&nbsp;Ahmed Alford,&nbsp;Hope L. Moreno,&nbsp;Geehan Suleyman,&nbsp;Maryssa Trupiano,&nbsp;Britney Aldrich,&nbsp;Frederick A. Valeriote,&nbsp;Nicolas Arosemena,&nbsp;Lucas Bialousow,&nbsp;Ron Benjamin,&nbsp;Zhi Zhong,&nbsp;Marcus A. Tius,&nbsp;Yeun-Mun Choo,&nbsp;John J. Lemasters,&nbsp;Mark T. Hamann","doi":"10.1021/acsinfecdis.6c00028","DOIUrl":"10.1021/acsinfecdis.6c00028","url":null,"abstract":"<p>Systemicmultidrug-resistant bacterial infections have become aglobal public health priority due to the diminished efficacy of standardantibiotic regimens and can lead to sepsis, which is among the leadingcauses of death (11 million/year) and years of lost life worldwide.We report an effective and well-defined antibiotic equimolar mixtureof the platanosides 1–4 that is as effective as its constituentparts and is active against multidrug-resistant <em>Staphylococcus</em> and <em>Streptococcus</em> spp. The platanosides can beeasily and inexpensively manufactured in good purity from sycamoretree (<em>Platanus</em> spp.) leaves, making them a viableoption as a drug to control multidrug-resistant infections in low-and middle-income countries. The platanosides 1–4 exhibitedactivity against clinically derived <em>Staphylococcus aureus</em> (methicillin-resistant, vancomycin-resistant,and vancomycin-intermediate) with minimal inhibitory concentrationvalues of 0.5–16 μg/mL. The minimal inhibitory concentrationvalues against clinically derived <em>Streptococcus</em> spp.were 2, 1, 0.06, and 1 μg/mL against <em>Streptococcus mitis</em>, <em>Streptococcus paramsanginis</em>, <em>Streptococcus gordonii</em>, and <em>Streptococcus pneumoniae</em>, respectively. Time-killstudies of the platanosides are reported. The proposed molecular targetsand unique polypharmacology of the platanosides 1–4 are alsodiscussed.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2642–2649"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148467826","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anti-RBD Single-Chain Variable Fragments Library (scFv Library) Generation toward the Development of a Diagnostic Platform for SARS-CoV-2","authors":"Mohd Shoeb Alam,&nbsp;Saurabh Sharma,&nbsp;Romisa Razvi,&nbsp;Harsh Bhakhri,&nbsp;Kulsum Fatima,&nbsp;Ekta Sachdeva,&nbsp;Manish Tripathi,&nbsp;Kalpana Luthra,&nbsp;Sumit Rathore","doi":"10.1021/acsinfecdis.6c00269","DOIUrl":"10.1021/acsinfecdis.6c00269","url":null,"abstract":"<p>Thecontinued emergence of SARS-CoV-2 variants worldwide underscoresthe need for effective measures to combat the current and future outbreaks.The receptor-binding domain (RBD) of the spike glycoprotein playsa critical role in viral entry and represents a highly immunogenictarget. In this study, we generated a mouse-derived single-chain variablefragment (scFv) phage display library against the RBD of the SARS-CoV-2spike protein. Peptide ELISA-based epitope mapping demonstrated thatselected monoclonal scFv phages exhibited broad epitope recognitionand reactivity across multiple recently reported variants. In a SARS-CoV-2pseudovirus neutralization assay, scFv C4 showed potent neutralizingactivity against the wild-type, Gamma, and Delta variants, with IC₅₀ values below 4 μg/mL. These findings highlight thepotential utility of these scFvs as candidate reagents for the developmentof improved diagnostic platforms and as scaffolds for next-generationmonoclonal antibody-based therapeutics.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2739–2749"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148589290","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"2-Amino-3,4-Dihydroquinazolines Exhibit Potent Antimalarial Activity by Targeting Plasmepsin X","authors":"Madeline G. Dans,&nbsp;Jon Kyle Awalt,&nbsp;Nghi Nguyen,&nbsp;Josephine Palandri,&nbsp;Anna Ngo,&nbsp;Kate E. Jarman,&nbsp;Jin H. Jeon,&nbsp;Tomas Yeo,&nbsp;Heekuk Park,&nbsp;Anne-Catrin Uhlemann,&nbsp;Emma Y. Mao,&nbsp;Maria R. Gancheva,&nbsp;Danny W. Wilson,&nbsp;Partha Mukherjee,&nbsp;Arnish Chakraborty,&nbsp;Mojca Kristan,&nbsp;Lindsay Stewart,&nbsp;Colin J. Sutherland,&nbsp;Delphine Baud,&nbsp;Stephen Brand,&nbsp;David A. Fidock,&nbsp;Paul F. Jackson,&nbsp;Alan F. Cowman,&nbsp;Brad E. Sleebs","doi":"10.1021/acsinfecdis.6c00258","DOIUrl":"10.1021/acsinfecdis.6c00258","url":null,"abstract":"<p>Theemergence of resistance to most clinically used antimalarialsnecessitates the discovery of new chemotypes. A phenotypic screenagainst asexual <em>Plasmodium falciparum</em> identified the 2-amino-3,4-dihydroquinazoline scaffold, previouslydeveloped as a β-secretase 1 inhibitor for Alzheimer’sdisease. Evaluation of hit analogues against malarial aspartyl proteasesrevealed potent inhibition of plasmepsin X. Structure-activity analysisshowed that key motifs on the hit scaffold are required for drivingbiochemical and antimalarial but are associated with poor selectivityagainst human aspartyl proteases and low metabolic stability. PlasmepsinX was validated as the molecular target through forward genetics,activity against mutant parasites, and inhibition of plasmepsin Xsubstrate processing. 2-Amino-3,4-dihydroquinazoline analogs exhibitmoderate asexual killing rates, low-to-moderate resistance risk, nocross-resistance with multidrug-resistant strains, and transmission-blockingactivity. Further optimization of potency and metabolic stabilitywill be required to achieve in vivo efficacy and realize the potentialof this antimalarial class.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2713–2726"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148416994","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Total Synthesis and Antibacterial Evaluation of (−)- and (+)-epi-Perrottetinene","authors":"Vijay Kumar,&nbsp;Anjali Gangwar,&nbsp;Sunandhani Khajuria,&nbsp;Sapna Saini,&nbsp;Muzamil Samad,&nbsp;Varun Pratap Singh,&nbsp;Rashmi Sharma,&nbsp;Parvinder Pal Singh","doi":"10.1021/acsinfecdis.6c00166","DOIUrl":"10.1021/acsinfecdis.6c00166","url":null,"abstract":"<p>Antimicrobialresistance (AMR) is a critical threat to global publichealth, with emerging resistance to <em>Staphylococcus aureus</em>, including methicillin-resistant <em>S</em>. <em>aureus</em> (MRSA), often referred to as a silent pandemic. Despite ongoingefforts in the fight against AMR, the drug discovery pipeline remainsunderdeveloped, highlighting the urgent need to explore natural andsynthetic approaches. Cannabinoid-inspired natural products representan underexplored chemical space with antimicrobial potential. Herein,we report an efficient, scalable, and enantioselective synthesis andantimicrobial evaluation of <em>epi</em>-perrottetinene (<em>epi</em>-PET), an unnatural bibenzyl-based cannabinoid analogof liverwort-derived perrottetinene. The synthetic strategy employsinexpensive starting materials and a Lewis acid-mediated Friedel–Craftscyclization to enable regioselective access to both Δ⁸- and Δ⁹-<em>epi</em>-PET isomers. Biologicalevaluation revealed potent antibacterial activity against Gram-positivepathogens, with particularly strong efficacy against drug-sensitiveand drug-resistant <em>S</em>. <em>aureus</em> strains,including MRSA clinical isolates. Notably, the lead compound <strong>E</strong> exhibited remarkable activity, with MIC values ≤1.2 μg/mL. Compound <strong>E</strong> remained effective againstefflux pump-overexpressing strains and bacterial biofilms and eradicatedintracellular bacteria, while displaying low hemolytic activity (3.4%of rabbit erythrocytes) and minimal cytotoxicity toward mammaliancell lines (N2a and RAW). Mechanistic studies indicate that bacterialmembrane disruption is a key contributor to the observed bactericidalactivity, consistent with rapid killing and a low propensity for resistancedevelopment. The work establishes <em>epi</em>-perrottetineneas a promising cannabinoid-inspired antibacterial scaffold and highlightsthe potential of nonclassical cannabinoids as a source of new chemicalmatter for addressing antimicrobial resistance.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2681–2694"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148434201","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction to “Treponema pallidum Flagellin FlaB3 Activates Inflammation and Inhibits Autophagy in HMC3 Cells via the TLR4 Pathway”","authors":"Fangzhi Du,&nbsp;Zhiyu Lu,&nbsp;Qingyun Wu,&nbsp;Xu Zhang,&nbsp;Xiaoli Zheng,&nbsp;Ruili Zhang,&nbsp;Qianqiu Wang","doi":"10.1021/acsinfecdis.6c00571","DOIUrl":"10.1021/acsinfecdis.6c00571","url":null,"abstract":"","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2892–2893"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148358358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antimicrobial α-Peptoids/Polypeptoids: Molecular Design and Therapeutic Assemblies","authors":"Mengyuan Hu,&nbsp;Yiyu Gong,&nbsp;Hailing Han,&nbsp;Jing Sun","doi":"10.1021/acsinfecdis.6c00243","DOIUrl":"10.1021/acsinfecdis.6c00243","url":null,"abstract":"<p>Theglobal health crisis of antibiotic-resistant bacteria necessitatesthe development of novel antimicrobial agents. Natural antimicrobialpeptides (AMPs) represent a promising therapeutic strategy, but theirsusceptibility to proteolytic degradation in vivo severely limitstheir clinical application. Peptoids, or <em>N</em>-substitutedglycine oligomers, have emerged as a robust biomimetic alternative.By shifting the side chain from the α-carbon to the backbonenitrogen atom, peptoids lack amide hydrogen donors, rendering themresistant to protease hydrolysis while maintaining a peptide-mimeticarchitecture. In this review, we first compare synthetic strategies(solid-phase synthesis versus solution polymerization) and outlinekey molecular design principles that govern antimicrobial activityand biocompatibility. We further assess self-assembled supramolecularstructures that confer emergent properties, ranging from enhancedmembrane penetration to stimuli-responsive release. Finally, we discussprevailing challenges and propose future directions for translatingthese promising materials into effective antimicrobial therapies.Beyond combining recent advances, this review establishes a molecular-to-assemblyframework to guide the design of next-generation antimicrobial agents.</p>","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2438–2464"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148429404","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction to “Coordinated Regulation of TLR2 Signaling by Neu1 Sialidase and the Siglec-5/Siglec-14 Receptor Pair during Mycoplasma pneumoniae Infection”","authors":"Haodang Luo,&nbsp;Qianrui Zeng,&nbsp;Na Xie,&nbsp;Chi Zhang,&nbsp;Chang Liu,&nbsp;Shutong Chen,&nbsp;Caihong Yan,&nbsp;Chun Li,&nbsp;Haiying Wu,&nbsp;Jun He,&nbsp;Yanhua Zeng,&nbsp;Xiaoxing You","doi":"10.1021/acsinfecdis.6c00680","DOIUrl":"https://doi.org/10.1021/acsinfecdis.6c00680","url":null,"abstract":"","PeriodicalId":17,"journal":{"name":"ACS Infectious Diseases","volume":"12 8","pages":"2895–2896"},"PeriodicalIF":4.5,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729837","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}