JACS Au最新文献

{"title":"Celebrating 5 Years of the ACS Au Journal Family.","authors":"Paul D Goring, Amelia Newman, Christopher W Jones, Shelley D Minteer","doi":"10.1021/jacsau.5c00142","DOIUrl":"https://doi.org/10.1021/jacsau.5c00142","url":null,"abstract":"","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 2","pages":"408-410"},"PeriodicalIF":8.5,"publicationDate":"2025-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11863147/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143525529","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Celebrating 5 Years of the ACS Au Journal Family","authors":"Paul D. Goring, Amelia Newman, Christopher W. Jones* and Shelley D. Minteer*, ","doi":"10.1021/jacsau.5c0014210.1021/jacsau.5c00142","DOIUrl":"https://doi.org/10.1021/jacsau.5c00142https://doi.org/10.1021/jacsau.5c00142","url":null,"abstract":"","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 2","pages":"408–410 408–410"},"PeriodicalIF":8.5,"publicationDate":"2025-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00142","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143473802","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural Basis for Inhibition of Urate Reabsorption in URAT1.","authors":"Junping Fan, Wenjun Xie, Han Ke, Jing Zhang, Jin Wang, Haijun Wang, Nianxin Guo, Yingjie Bai, Xiaoguang Lei","doi":"10.1021/jacsau.4c01188","DOIUrl":"10.1021/jacsau.4c01188","url":null,"abstract":"<p><p>The urate transporter 1 (URAT1) is the primary urate transporter in the kidney responsible for urate reabsorption and, therefore, is crucial for urate homeostasis. Hyperuricemia causes the common human disease gout and other pathological consequences. Inhibition of urate reabsorption through URAT1 has been shown as a promising strategy in alleviating hyperuricemia, and clinical and preclinical drug candidates targeting URAT1 are emerging. However, how small molecules inhibit URAT1 remains undefined, and the lack of accurate URAT1 complex structures hinders the development of better therapeutics. Here, we present cryoelectron microscopy structures of a humanized rat URAT1 bound with benzbromarone, lingdolinurad, and verinurad, elucidating the structural basis for drug recognition and inhibition. The three small molecules reside in the URAT1 central cavity with different binding modes, locking URAT1 in an inward-facing conformation. This study provides mechanistic insights into the drug modulation of URAT1 and sheds light on the rational design of potential URAT1-specific therapeutics for treating hyperuricemia.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1308-1319"},"PeriodicalIF":8.5,"publicationDate":"2025-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937972/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143733623","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural Basis for Inhibition of Urate Reabsorption in URAT1","authors":"Junping Fan*,&nbsp;Wenjun Xie,&nbsp;Han Ke,&nbsp;Jing Zhang,&nbsp;Jin Wang,&nbsp;Haijun Wang,&nbsp;Nianxin Guo,&nbsp;Yingjie Bai and Xiaoguang Lei*,&nbsp;","doi":"10.1021/jacsau.4c0118810.1021/jacsau.4c01188","DOIUrl":"https://doi.org/10.1021/jacsau.4c01188https://doi.org/10.1021/jacsau.4c01188","url":null,"abstract":"<p >The urate transporter 1 (URAT1) is the primary urate transporter in the kidney responsible for urate reabsorption and, therefore, is crucial for urate homeostasis. Hyperuricemia causes the common human disease gout and other pathological consequences. Inhibition of urate reabsorption through URAT1 has been shown as a promising strategy in alleviating hyperuricemia, and clinical and preclinical drug candidates targeting URAT1 are emerging. However, how small molecules inhibit URAT1 remains undefined, and the lack of accurate URAT1 complex structures hinders the development of better therapeutics. Here, we present cryoelectron microscopy structures of a humanized rat URAT1 bound with benzbromarone, lingdolinurad, and verinurad, elucidating the structural basis for drug recognition and inhibition. The three small molecules reside in the URAT1 central cavity with different binding modes, locking URAT1 in an inward-facing conformation. This study provides mechanistic insights into the drug modulation of URAT1 and sheds light on the rational design of potential URAT1-specific therapeutics for treating hyperuricemia.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1308–1319 1308–1319"},"PeriodicalIF":8.5,"publicationDate":"2025-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.4c01188","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143675806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PAM-Independent CRISPR-Cas12a System for Specific Assays of Single Nucleotide Variants","authors":"Jinlong Ai,&nbsp;Jinhai Deng,&nbsp;Jingjing Hu,&nbsp;Xingxiang Pu*,&nbsp;Tongyan Yuan,&nbsp;Yuling Teng,&nbsp;Han Li,&nbsp;Bojie Chen,&nbsp;Jinlian Du,&nbsp;Ling Jiang*,&nbsp;Xiaoyan Chen,&nbsp;Erhu Xiong* and Ronghua Yang,&nbsp;","doi":"10.1021/jacsau.5c0001110.1021/jacsau.5c00011","DOIUrl":"https://doi.org/10.1021/jacsau.5c00011https://doi.org/10.1021/jacsau.5c00011","url":null,"abstract":"<p >The CRISPR-Cas12a system has been extensively utilized in nucleic acid detection owing to its remarkable sensitivity and specificity. Nonetheless, its strict dependency on the presence of a protospacer adjacent motif (PAM) within double-stranded DNA (dsDNA) introduces considerable limitations, thereby constraining its applicability, flexibility, and broader accessibility in molecular diagnostics. Here, we communicate a universal, robust, and high-fidelity method for a PAM-independent nucleic acid assay based on the CRISPR-Cas12a system, named TRACER (mutant <u>t</u>arget-<u>r</u>ecognized P<u>A</u>M-independent <u>C</u>RISPR-Cas12a <u>e</u>nzyme <u>r</u>eporting system). TRACER can effectively distinguish target nucleic acids at concentrations as low as 0.5 aM, thereby enabling it to identify the presence of a 0.1% single nucleotide variant (SNV)-included mutant-type gene in heterozygotes. Thus, TRACER exhibits comparable sensitivity, specificity, and accuracy to Sanger sequencing in analyzing the SNV-related clinical tumor samples. Overall, TRACER introduces a brand-new perspective for SNV assays by eliminating the dependency on PAM sites and significantly expands the application range of the CRISPR-Cas12a system, thus holding immense potential for clinical diagnostics, biomedical research, and drug discovery.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1392–1401 1392–1401"},"PeriodicalIF":8.5,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00011","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143675805","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PAM-Independent CRISPR-Cas12a System for Specific Assays of Single Nucleotide Variants.","authors":"Jinlong Ai, Jinhai Deng, Jingjing Hu, Xingxiang Pu, Tongyan Yuan, Yuling Teng, Han Li, Bojie Chen, Jinlian Du, Ling Jiang, Xiaoyan Chen, Erhu Xiong, Ronghua Yang","doi":"10.1021/jacsau.5c00011","DOIUrl":"10.1021/jacsau.5c00011","url":null,"abstract":"<p><p>The CRISPR-Cas12a system has been extensively utilized in nucleic acid detection owing to its remarkable sensitivity and specificity. Nonetheless, its strict dependency on the presence of a protospacer adjacent motif (PAM) within double-stranded DNA (dsDNA) introduces considerable limitations, thereby constraining its applicability, flexibility, and broader accessibility in molecular diagnostics. Here, we communicate a universal, robust, and high-fidelity method for a PAM-independent nucleic acid assay based on the CRISPR-Cas12a system, named TRACER (mutant target-recognized PAM-independent CRISPR-Cas12a enzyme reporting system). TRACER can effectively distinguish target nucleic acids at concentrations as low as 0.5 aM, thereby enabling it to identify the presence of a 0.1% single nucleotide variant (SNV)-included mutant-type gene in heterozygotes. Thus, TRACER exhibits comparable sensitivity, specificity, and accuracy to Sanger sequencing in analyzing the SNV-related clinical tumor samples. Overall, TRACER introduces a brand-new perspective for SNV assays by eliminating the dependency on PAM sites and significantly expands the application range of the CRISPR-Cas12a system, thus holding immense potential for clinical diagnostics, biomedical research, and drug discovery.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1392-1401"},"PeriodicalIF":8.5,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11938009/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143733818","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Positive Charge in an Antimalarial Compound Unlocks Broad-Spectrum Antibacterial Activity.","authors":"Maria Braun-Cornejo, Mitchell Platteschorre, Vincent de Vries, Patricia Bravo, Vidhisha Sonawane, Mostafa M Hamed, Jörg Haupenthal, Norbert Reiling, Matthias Rottmann, Dennis Piet, Peter Maas, Eleonora Diamanti, Anna K H Hirsch","doi":"10.1021/jacsau.4c00935","DOIUrl":"10.1021/jacsau.4c00935","url":null,"abstract":"<p><p>In this study, we synthesized a library of eNTRy-rule-compliant compounds by introducing ionizable nitrogen atoms to an antimalarial compound. These positively charged derivatives gained activity against both Gram-negative and -positive bacteria, <i>Mycobacterium tuberculosis</i>, and boosted <i>Plasmodium falciparum</i> inhibition to the double-digit nanomolar range. Overcoming and remaining inside the cell envelope of Gram-negative bacteria (GNB) is one of the major difficulties in antibacterial drug discovery and development. The eNTRy rules (N = ionizable nitrogen, T = low three-dimensionality, R = rigidity) can be a useful structural guideline to improve accumulation of small molecules in GNB. With the aim of unlocking Gram-negative activity, we added amines and (cyclic) <i>N</i>-alkyl guanidines to an already flat and rigid pyrazole-amide class as a representative example for our investigation. To test their performance, we compared these eNTRy-rule-compliant compounds to closely related noncompliant ones through phenotypic screening of various pathogens (<i>P. falciparum</i>, <i>Escherichia coli</i>, <i>Acinetobacter baumannii</i>, <i>Pseudomonas aeruginosa</i>, <i>Staphylococcus aureus</i>, <i>Streptococcus pneumoniae</i>, and <i>M. tuberculosis</i>), obtaining a handful of broad-spectrum hits. The results support the working hypothesis and even extend its applicability. The studied pyrazole-amide class adheres to the eNTRy rules; noncompliant compounds do not kill any of the bacteria tested, while compliant compounds largely showed growth inhibition of Gram-negative, -positive, and <i>M. tuberculosis</i> bacteria in the single-digit micromolar range.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1146-1156"},"PeriodicalIF":8.5,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11938010/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143733857","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"³¹P NMR Chemical Shift Anisotropy in Paramagnetic Lanthanide Phosphide Complexes.","authors":"Jack Baldwin, Katherine L Bonham, Toby R C Thompson, Gemma K Gransbury, George F S Whitehead, Iñigo J Vitorica-Yrezabal, Daniel Lee, Nicholas F Chilton, David P Mills","doi":"10.1021/jacsau.4c01018","DOIUrl":"10.1021/jacsau.4c01018","url":null,"abstract":"<p><p>Lanthanide (Ln) magnetic resonance imaging and chiral shift reagents generally exploit ¹H NMR shifts, as paramagnetic broadening tends to preclude the use of heavier, less sensitive nuclei. Here, we report the solution and solid-state ³¹P NMR shifts of an isostructural series of distorted trigonal bipyramidal Ln(III) <i>tris</i>-silylphosphide complexes, [Ln{P(SiMe₃)₂}₃(THF)₂] (<b>1-Ln</b>; Ln = La, Ce, Pr, Nd, Sm); <b>1-Ln</b> was also characterized by elemental analysis; single-crystal and powder X-ray diffraction; multinuclear NMR, EPR, ATR-IR, and UV-vis-NIR spectroscopy; and SQUID magnetometry. Breaking assumptions, we observed paramagnetically broadened ³¹P NMR spectra for the Ln-bound P atoms for the <b>1-Ln</b> family; in solution, <b>1-Nd</b> showed the most downfield chemical shift (δ{³¹P} = 2570.14 ppm) and <b>1-Sm</b> the most upfield value (δ{³¹P} = -259.21 ppm). We determined the span of the chemical shift anisotropies (CSAs) for solid <b>1-Ln</b> using magic angle spinning NMR spectroscopy; the CSA was largest for <b>1-Pr</b> (<b>Ω</b>{³¹P} ≈ 2000 ppm), consistent with a combination of paramagnetism and the relatively large differences in pyramidalization of the three P atoms in the solid-state. Density functional theory calculations for <b>1-La</b> were in excellent agreement with the experimentally determined ³¹P NMR parameters. We find good agreement of experimental ¹H NMR chemical shifts with <i>ab initio</i>-calculated values for paramagnetic <b>1-Ln</b>, while the shifts of heavier ¹³C, ²⁹Si, and ³¹P nuclei are not well-reproduced due to the current limitations of paramagnetic NMR calculations for nuclei with large contact shifts.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1196-1212"},"PeriodicalIF":8.5,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937968/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143733621","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Positive Charge in an Antimalarial Compound Unlocks Broad-Spectrum Antibacterial Activity","authors":"Maria Braun-Cornejo,&nbsp;Mitchell Platteschorre,&nbsp;Vincent de Vries,&nbsp;Patricia Bravo,&nbsp;Vidhisha Sonawane,&nbsp;Mostafa M. Hamed,&nbsp;Jörg Haupenthal,&nbsp;Norbert Reiling,&nbsp;Matthias Rottmann,&nbsp;Dennis Piet,&nbsp;Peter Maas,&nbsp;Eleonora Diamanti and Anna K. H. Hirsch*,&nbsp;","doi":"10.1021/jacsau.4c0093510.1021/jacsau.4c00935","DOIUrl":"https://doi.org/10.1021/jacsau.4c00935https://doi.org/10.1021/jacsau.4c00935","url":null,"abstract":"<p >In this study, we synthesized a library of eNTRy-rule-compliant compounds by introducing ionizable nitrogen atoms to an antimalarial compound. These positively charged derivatives gained activity against both Gram-negative and -positive bacteria, <i>Mycobacterium tuberculosis</i>, and boosted <i>Plasmodium falciparum</i> inhibition to the double-digit nanomolar range. Overcoming and remaining inside the cell envelope of Gram-negative bacteria (GNB) is one of the major difficulties in antibacterial drug discovery and development. The eNTRy rules (N = ionizable nitrogen, T = low three-dimensionality, R = rigidity) can be a useful structural guideline to improve accumulation of small molecules in GNB. With the aim of unlocking Gram-negative activity, we added amines and (cyclic) <i>N</i>-alkyl guanidines to an already flat and rigid pyrazole-amide class as a representative example for our investigation. To test their performance, we compared these eNTRy-rule-compliant compounds to closely related noncompliant ones through phenotypic screening of various pathogens (<i>P. falciparum</i>, <i>Escherichia coli</i>, <i>Acinetobacter baumannii</i>, <i>Pseudomonas aeruginosa</i>, <i>Staphylococcus aureus</i>, <i>Streptococcus pneumoniae</i>, and <i>M. tuberculosis</i>), obtaining a handful of broad-spectrum hits. The results support the working hypothesis and even extend its applicability. The studied pyrazole-amide class adheres to the eNTRy rules; noncompliant compounds do not kill any of the bacteria tested, while compliant compounds largely showed growth inhibition of Gram-negative, -positive, and <i>M. tuberculosis</i> bacteria in the single-digit micromolar range.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1146–1156 1146–1156"},"PeriodicalIF":8.5,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.4c00935","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143675802","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"31P NMR Chemical Shift Anisotropy in Paramagnetic Lanthanide Phosphide Complexes","authors":"Jack Baldwin,&nbsp;Katherine L. Bonham,&nbsp;Toby R. C. Thompson,&nbsp;Gemma K. Gransbury,&nbsp;George F. S. Whitehead,&nbsp;Iñigo J. Vitorica-Yrezabal,&nbsp;Daniel Lee*,&nbsp;Nicholas F. Chilton* and David P. Mills*,&nbsp;","doi":"10.1021/jacsau.4c0101810.1021/jacsau.4c01018","DOIUrl":"https://doi.org/10.1021/jacsau.4c01018https://doi.org/10.1021/jacsau.4c01018","url":null,"abstract":"<p >Lanthanide (Ln) magnetic resonance imaging and chiral shift reagents generally exploit ¹H NMR shifts, as paramagnetic broadening tends to preclude the use of heavier, less sensitive nuclei. Here, we report the solution and solid-state ³¹P NMR shifts of an isostructural series of distorted trigonal bipyramidal Ln(III) <i>tris</i>-silylphosphide complexes, [Ln{P(SiMe₃)₂}₃(THF)₂] (<b>1-Ln</b>; Ln = La, Ce, Pr, Nd, Sm); <b>1-Ln</b> was also characterized by elemental analysis; single-crystal and powder X-ray diffraction; multinuclear NMR, EPR, ATR-IR, and UV–vis-NIR spectroscopy; and SQUID magnetometry. Breaking assumptions, we observed paramagnetically broadened ³¹P NMR spectra for the Ln-bound P atoms for the <b>1-Ln</b> family; in solution, <b>1-Nd</b> showed the most downfield chemical shift (δ{³¹P} = 2570.14 ppm) and <b>1-Sm</b> the most upfield value (δ{³¹P} = −259.21 ppm). We determined the span of the chemical shift anisotropies (CSAs) for solid <b>1-Ln</b> using magic angle spinning NMR spectroscopy; the CSA was largest for <b>1-Pr</b> (<b>Ω</b>{³¹P} ≈ 2000 ppm), consistent with a combination of paramagnetism and the relatively large differences in pyramidalization of the three P atoms in the solid-state. Density functional theory calculations for <b>1-La</b> were in excellent agreement with the experimentally determined ³¹P NMR parameters. We find good agreement of experimental ¹H NMR chemical shifts with <i>ab initio</i>-calculated values for paramagnetic <b>1-Ln</b>, while the shifts of heavier ¹³C, ²⁹Si, and ³¹P nuclei are not well-reproduced due to the current limitations of paramagnetic NMR calculations for nuclei with large contact shifts.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 3","pages":"1196–1212 1196–1212"},"PeriodicalIF":8.5,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.4c01018","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143675803","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}