Pub Date : 2026-01-28DOI: 10.1016/j.ejmech.2026.118620
Raed M. Al-Zoubi, Alaa Farhan, Basma Hanbali, Sally R. Al-Zoubi, Ahmad R. Al-Qudimat, Mazhar Salim Al Zoubi, Abbas Khan, Mohanad Shkoor, Asia Al Jabiry, Abdulilah D. Bani-Yaseen, Abdelali Agouni
{"title":"Inhibiting CK2 in Breast Cancer: From Molecular Targets to Drug Candidates","authors":"Raed M. Al-Zoubi, Alaa Farhan, Basma Hanbali, Sally R. Al-Zoubi, Ahmad R. Al-Qudimat, Mazhar Salim Al Zoubi, Abbas Khan, Mohanad Shkoor, Asia Al Jabiry, Abdulilah D. Bani-Yaseen, Abdelali Agouni","doi":"10.1016/j.ejmech.2026.118620","DOIUrl":"https://doi.org/10.1016/j.ejmech.2026.118620","url":null,"abstract":"","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"58 1","pages":""},"PeriodicalIF":6.7,"publicationDate":"2026-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146072535","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}
Pub Date : 2026-01-28DOI: 10.1016/j.ejmech.2026.118621
Safeh Khemiri , Marine O. Faucher , Stephane Bourg , Sarah Attoumani-Madi , Carole Yaacoub , Franck Touret , Marc Farag , Mattéo Fermiana Vitorino , Pascal Bonnet , Patrice Vanelle , Samia Aci-Seche , Bruno Coutard , Karine Barral
There are currently no antiviral drugs available to treat or prevent life-threatening human non-poliovirus enterovirus infections, such as those caused by CV-B3, EV-A71 or EV-D68. Our aim is to develop novel inhibitors that target the non-structural ATPase/Helicase 2C protein, which is involved in the RNA replication process that is essential for enterovirus replication, among other functions. In this study, we describe the optimization of (S)-fluoxetine, a promising hit identified through drug repurposing that binds to an allosteric site on the CV-B3 2C ATPase domain. Our optimization process was guided by rational design, X-ray crystallographic structures, computational docking, and validation by enzyme and cell-based assays, leading to several new inhibitors, among which compound 53 (CV–B3 EC50 = 0.5 μM and EV-D68 EC50 = 0.4 μM), a novel anti-enterovirus with higher selectivity indexes than (S)-fluoxetine.
{"title":"New fluoxetine analogues as anti-enterovirus agents targeting 2C protein","authors":"Safeh Khemiri , Marine O. Faucher , Stephane Bourg , Sarah Attoumani-Madi , Carole Yaacoub , Franck Touret , Marc Farag , Mattéo Fermiana Vitorino , Pascal Bonnet , Patrice Vanelle , Samia Aci-Seche , Bruno Coutard , Karine Barral","doi":"10.1016/j.ejmech.2026.118621","DOIUrl":"10.1016/j.ejmech.2026.118621","url":null,"abstract":"<div><div>There are currently no antiviral drugs available to treat or prevent life-threatening human non-poliovirus enterovirus infections, such as those caused by CV-B3, EV-A71 or EV-D68. Our aim is to develop novel inhibitors that target the non-structural ATPase/Helicase 2C protein, which is involved in the RNA replication process that is essential for enterovirus replication, among other functions. In this study, we describe the optimization of (<em>S</em>)-fluoxetine, a promising hit identified through drug repurposing that binds to an allosteric site on the CV-B3 2C ATPase domain. Our optimization process was guided by rational design, X-ray crystallographic structures, computational docking, and validation by enzyme and cell-based assays, leading to several new inhibitors, among which compound <strong>53</strong> (CV–B3 EC<sub>50</sub> = 0.5 μM and EV-D68 EC<sub>50</sub> = 0.4 μM), a novel anti-enterovirus with higher selectivity indexes than (<em>S</em>)-fluoxetine.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"306 ","pages":"Article 118621"},"PeriodicalIF":5.9,"publicationDate":"2026-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146071902","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}
Pub Date : 2026-01-24DOI: 10.1016/j.ejmech.2026.118597
Vishnu Kavumkal Omanakuttan, Mathy Froeyen, Sandra Claes, Brent Van Bosstraeten, Katrijn Boon, Dominique Schols, Luc Van Meervelt, Tom Van Loy, Wim Dehaen, Steven De Jonghe
A previously reported triazolo[4,5-d]pyrimidine analogue displaying dual CCR7/CXCR2 antagonism was subjected to an optimisation campaign aiming at the discovery of potent and selective CCR7 antagonists. A range of substituted thiol groups was introduced at position 5 of the triazolo[4,5-d]pyrimidine core. In addition, a scaffold hopping approach was pursued yielding three novel skeletons. Unfortunately, none of these modifications led to improved CCR7 antagonistic potency or selectivity, when compared to the original lead compound. A broad chemokine receptor screening revealed that these originally CCR7/CXCR2 antagonists display very pronounced CCR2 antagonism. Finally, molecular modeling was applied in order to rationalize these experimental findings.
{"title":"Synthesis, structure-activity relationship study and molecular modeling of triazolo[4,5-d]pyrimidines targeting an intracellular allosteric binding site of various chemokine receptors","authors":"Vishnu Kavumkal Omanakuttan, Mathy Froeyen, Sandra Claes, Brent Van Bosstraeten, Katrijn Boon, Dominique Schols, Luc Van Meervelt, Tom Van Loy, Wim Dehaen, Steven De Jonghe","doi":"10.1016/j.ejmech.2026.118597","DOIUrl":"https://doi.org/10.1016/j.ejmech.2026.118597","url":null,"abstract":"A previously reported triazolo[4,5-<em>d</em>]pyrimidine analogue displaying dual CCR7/CXCR2 antagonism was subjected to an optimisation campaign aiming at the discovery of potent and selective CCR7 antagonists. A range of substituted thiol groups was introduced at position 5 of the triazolo[4,5-<em>d</em>]pyrimidine core. In addition, a scaffold hopping approach was pursued yielding three novel skeletons. Unfortunately, none of these modifications led to improved CCR7 antagonistic potency or selectivity, when compared to the original lead compound. A broad chemokine receptor screening revealed that these originally CCR7/CXCR2 antagonists display very pronounced CCR2 antagonism. Finally, molecular modeling was applied in order to rationalize these experimental findings.","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"29 1","pages":""},"PeriodicalIF":6.7,"publicationDate":"2026-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146043114","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}
Pub Date : 2026-01-23DOI: 10.1016/j.ejmech.2026.118616
Xiong Chen , Zong-Zheng Li , Xing-Yu Yao, Xiao-Min Han, Kai-Le Zeng, Hao-Yun Chen, Wen-Jing Gao, Tian-Yue Zhu, Lei Niu, Tao Zhuang
Dual-acting ligands targeting the sigma-1 receptor (σ1R) and histamine H3 receptor (H3R) are emerging as promising candidates for novel and safe analgesics. In this work, we designed, synthesized, and evaluated twenty-nine 3-indolealkylamines as dual σ1R/H3R ligands. In vitro radioligand receptor binding assay or surface plasmon resonance assay were performed to determine their affinities toward σ1R or H3R. Among them, compound 67 demonstrated high binding affinity for both σ1R (Kᵢ = 8.8 nM) and H3R (KD = 31.2 nM). Further in vivo pharmacological evaluations confirmed its antagonistic activity at both receptors. Compound 67 exhibited significant antinociceptive effects in the acetic acid-induced constriction test (ED50 = 0.18 mg/kg) and paclitaxel-induced neuropathic pain model (ED50 = 0.06 mg/kg), which demonstrated potency superior to that of marketed drug gabapentin. Moreover, compound 67 showed no side effects in the open-field test and rotarod test, and acute toxicity studies revealed a high safety profile with an excellent therapeutic window (LD50 > 250 mg/kg, TI > 1388.9). These findings demonstrated that compound 67 is a promising dual σ1R/H3R ligand to develop safe and effective analgesics.
{"title":"Discovery of 3-indolealkylamines as novel dual-target σ1R/H3R ligands with potent analgesia","authors":"Xiong Chen , Zong-Zheng Li , Xing-Yu Yao, Xiao-Min Han, Kai-Le Zeng, Hao-Yun Chen, Wen-Jing Gao, Tian-Yue Zhu, Lei Niu, Tao Zhuang","doi":"10.1016/j.ejmech.2026.118616","DOIUrl":"10.1016/j.ejmech.2026.118616","url":null,"abstract":"<div><div>Dual-acting ligands targeting the sigma-1 receptor (σ<sub>1</sub>R) and histamine H<sub>3</sub> receptor (H<sub>3</sub>R) are emerging as promising candidates for novel and safe analgesics. In this work, we designed, synthesized, and evaluated twenty-nine 3-indolealkylamines as dual σ<sub>1</sub>R/H<sub>3</sub>R ligands. <em>In vitro</em> radioligand receptor binding assay or surface plasmon resonance assay were performed to determine their affinities toward σ<sub>1</sub>R or H<sub>3</sub>R. Among them, compound <strong>67</strong> demonstrated high binding affinity for both σ<sub>1</sub>R (Kᵢ = 8.8 nM) and H<sub>3</sub>R (K<sub>D</sub> = 31.2 nM). Further <em>in vivo</em> pharmacological evaluations confirmed its antagonistic activity at both receptors. Compound <strong>67</strong> exhibited significant antinociceptive effects in the acetic acid-induced constriction test (ED<sub>50</sub> = 0.18 mg/kg) and paclitaxel-induced neuropathic pain model (ED<sub>50</sub> = 0.06 mg/kg), which demonstrated potency superior to that of marketed drug gabapentin. Moreover, compound <strong>67</strong> showed no side effects in the open-field test and rotarod test, and acute toxicity studies revealed a high safety profile with an excellent therapeutic window (LD<sub>50</sub> > 250 mg/kg, TI > 1388.9). These findings demonstrated that compound <strong>67</strong> is a promising dual σ<sub>1</sub>R/H<sub>3</sub>R ligand to develop safe and effective analgesics.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"306 ","pages":"Article 118616"},"PeriodicalIF":5.9,"publicationDate":"2026-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146033859","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}
Pub Date : 2026-01-23DOI: 10.1016/j.ejmech.2026.118615
Shuang Luo , Zhiyun Peng , Guangcheng Wang
To achieve new multi-target inhibitors simultaneously acting on α-glucosidase, α-amylase, and protein tyrosine phosphatase 1B (PTP1B), twenty-one novel carbazole-5-phenyl-1,3,4-oxadiazole derivatives (5a-5u) were synthesized and screened for in vitro enzyme inhibitory activity. All synthesized derivatives 5a-5u showed noticeable anti-α-glucosidase and anti-α-amylase activities (IC50: 9.79 ± 0.21–132.65 ± 1.52 μM, 6.15 ± 0.11–25.16 ± 0.75 μM, respectively) in comparison with the standard acarbose (IC50: 210.57 ± 0.91 μM, 26.17 ± 1.12 μM, respectively). The compound 5l that possessed the best inhibition activity on both α-glucosidase and α-amylase (IC50 = 9.79 ± 0.21, 6.36 ± 0.16 μM, respectively) also exhibited a fine inhibitory effect on PTP1B with an IC50 value of 19.08 ± 4.52 μM, as the reference drug ursolic acid of 4.43 ± 0.40 μM. Kinetic measurement, multispectral techniques, and molecular docking study were used to reveal the interaction mechanism of preferred compound 5l with α-glucosidase, α-amylase, and PTP1B. The derivative 5l could inhibit the activity of these enzyme proteins via binding to the enzyme or its substrate complex, quenching their intrinsic fluorescence, or affecting the conformation of enzyme proteins, and forming hydrophobic interactions and hydrogen bonds with them. In conjunction with the potential properties of compound 5l in inhibiting the postprandial blood glucose rise and low cytotoxicity, the title derivatives are expected to become lead molecules in developing new multi-target antidiabetes drugs.
{"title":"Construction and biological evaluation of novel carbazole-5-phenyl-1,3,4-oxadiazole derivatives as multi-target hypoglycemic agents","authors":"Shuang Luo , Zhiyun Peng , Guangcheng Wang","doi":"10.1016/j.ejmech.2026.118615","DOIUrl":"10.1016/j.ejmech.2026.118615","url":null,"abstract":"<div><div>To achieve new multi-target inhibitors simultaneously acting on α-glucosidase, α-amylase, and protein tyrosine phosphatase 1B (PTP1B), twenty-one novel carbazole-5-phenyl-1,3,4-oxadiazole derivatives (<strong>5a-5u</strong>) were synthesized and screened for <em>in vitro</em> enzyme inhibitory activity. All synthesized derivatives <strong>5a-5u</strong> showed noticeable anti-α-glucosidase and anti-α-amylase activities (IC<sub>50</sub>: 9.79 ± 0.21–132.65 ± 1.52 μM, 6.15 ± 0.11–25.16 ± 0.75 μM, respectively) in comparison with the standard acarbose (IC<sub>50</sub>: 210.57 ± 0.91 μM, 26.17 ± 1.12 μM, respectively). The compound <strong>5l</strong> that possessed the best inhibition activity on both α-glucosidase and α-amylase (IC<sub>50</sub> = 9.79 ± 0.21, 6.36 ± 0.16 μM, respectively) also exhibited a fine inhibitory effect on PTP1B with an IC<sub>50</sub> value of 19.08 ± 4.52 μM, as the reference drug ursolic acid of 4.43 ± 0.40 μM. Kinetic measurement, multispectral techniques, and molecular docking study were used to reveal the interaction mechanism of preferred compound <strong>5l</strong> with α-glucosidase, α-amylase, and PTP1B. The derivative <strong>5l</strong> could inhibit the activity of these enzyme proteins <em>via</em> binding to the enzyme or its substrate complex, quenching their intrinsic fluorescence, or affecting the conformation of enzyme proteins, and forming hydrophobic interactions and hydrogen bonds with them. In conjunction with the potential properties of compound <strong>5l</strong> in inhibiting the postprandial blood glucose rise and low cytotoxicity, the title derivatives are expected to become lead molecules in developing new multi-target antidiabetes drugs.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"306 ","pages":"Article 118615"},"PeriodicalIF":5.9,"publicationDate":"2026-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146043115","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}
Pub Date : 2026-01-22DOI: 10.1016/j.ejmech.2026.118605
Zhijie Wang , HaiQi He , Jianwei Xu , Xiaotong Liao , Jun Tan , Chenglong Xu , Jiamin Tan , Lirong Zhang , Qin Wang , Xixiang Yang , Yichang Ren , Guangfa Wang , Yanle Zhi , Jianjun Chen
Programmed cell death protein-1 (PD-1)/programmed cell death-ligand 1 (PD-L1) inhibitors are widely recognized as an effective therapeutic strategy for treating various types of tumors. However, single-target PD-1/PD-L1 inhibitors frequently encounter primary resistance or secondary resistance, posing significant challenges to clinical treatment and creating an urgent need for novel therapeutic approaches. In this study, we designed and synthesized a dual PD-L1/JAK inhibitor PJ27 for the first time, which showed significant and balanced inhibitory activities against PD-1/PD-L1 (IC50 = 414 nM) and JAK1 (IC50 = 786 nM). Besides, PJ27 exhibited remarkable in vitro immune activation effects. Furthermore, PJ27 potently and dose-dependently inhibited tumor growth in the LLC lung cancer mouse model without obvious toxicity. Moreover, PJ27 enhanced the infiltration of CD3+ CD8+ and CD3+ CD4+ cells into the tumor microenvironment. Additionally, kinase spectrum analysis demonstrated that PJ27 possessed favorable selectivity towards JAK1. Collectively, PJ27 represented the first dual PD-L1/JAK inhibitor deserving further research as a tumor immunotherapy agent.
{"title":"Discovery of the first dual PD-L1/JAK inhibitor with enhanced in vivo antitumor immunity","authors":"Zhijie Wang , HaiQi He , Jianwei Xu , Xiaotong Liao , Jun Tan , Chenglong Xu , Jiamin Tan , Lirong Zhang , Qin Wang , Xixiang Yang , Yichang Ren , Guangfa Wang , Yanle Zhi , Jianjun Chen","doi":"10.1016/j.ejmech.2026.118605","DOIUrl":"10.1016/j.ejmech.2026.118605","url":null,"abstract":"<div><div>Programmed cell death protein-1 (PD-1)/programmed cell death-ligand 1 (PD-L1) inhibitors are widely recognized as an effective therapeutic strategy for treating various types of tumors. However, single-target PD-1/PD-L1 inhibitors frequently encounter primary resistance or secondary resistance, posing significant challenges to clinical treatment and creating an urgent need for novel therapeutic approaches. In this study, we designed and synthesized a dual PD-L1/JAK inhibitor <strong>PJ27</strong> for the first time, which showed significant and balanced inhibitory activities against PD-1/PD-L1 (IC<sub>50</sub> = 414 nM) and JAK1 (IC<sub>50</sub> = 786 nM). Besides, <strong>PJ27</strong> exhibited remarkable <em>in vitro</em> immune activation effects. Furthermore, <strong>PJ27</strong> potently and dose-dependently inhibited tumor growth in the LLC lung cancer mouse model without obvious toxicity. Moreover, <strong>PJ27</strong> enhanced the infiltration of CD3<sup>+</sup> CD8<sup>+</sup> and CD3<sup>+</sup> CD4<sup>+</sup> cells into the tumor microenvironment. Additionally, kinase spectrum analysis demonstrated that <strong>PJ27</strong> possessed favorable selectivity towards JAK1. Collectively, <strong>PJ27</strong> represented the first dual PD-L1/JAK inhibitor deserving further research as a tumor immunotherapy agent.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"306 ","pages":"Article 118605"},"PeriodicalIF":5.9,"publicationDate":"2026-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146021849","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}
Pub Date : 2026-01-21DOI: 10.1016/j.ejmech.2026.118611
Wuxin Liu , Chenyu Tian , Mengqiu Zhou , Xinhua Wang , Lu Yang , Chong Huang , Shengyong Yang , Linli Li
G protein-coupled receptor 68 (GPR68), a proton-sensing GPCR, has emerged as a key player in inflammatory diseases. Its expression is substantially upregulated in the inflamed intestinal mucosa of inflammatory bowel disease (IBD) patients, and pharmacological inhibition of GPR68 has been shown to ameliorate colitis in preclinical models, highlighting GPR68 as a promising therapeutic target. Herein, we report the discovery of diphenylethane derivatives as a novel class of potent GPR68 antagonists. Structure-activity relationship (SAR) of these compounds was analyzed, which led to the identification of a potent GPR68 antagonist (18l) with an IC50 value of 0.081 ± 0.006 μM. The lead compound demonstrated significant inhibition of GPR68-mediated signaling and reduced the production of key pro-inflammatory cytokines. In a dextran sulfate sodium (DSS)-induced mouse model of IBD, 18l effectively alleviated disease symptoms. It also showed good pharmacokinetic properties and a commendable safety profile. Overall, compound 18l could be a promising lead compound for the treatment of IBD and deserves further in-depth studies.
{"title":"Discovery and structure-activity relationship analyses of 1,2-diphenylethane derivatives as a new class of GPR68 antagonists and the therapeutic effect in an inflammatory bowel disease model","authors":"Wuxin Liu , Chenyu Tian , Mengqiu Zhou , Xinhua Wang , Lu Yang , Chong Huang , Shengyong Yang , Linli Li","doi":"10.1016/j.ejmech.2026.118611","DOIUrl":"10.1016/j.ejmech.2026.118611","url":null,"abstract":"<div><div>G protein-coupled receptor 68 (GPR68), a proton-sensing GPCR, has emerged as a key player in inflammatory diseases. Its expression is substantially upregulated in the inflamed intestinal mucosa of inflammatory bowel disease (IBD) patients, and pharmacological inhibition of GPR68 has been shown to ameliorate colitis in preclinical models, highlighting GPR68 as a promising therapeutic target. Herein, we report the discovery of diphenylethane derivatives as a novel class of potent GPR68 antagonists. Structure-activity relationship (SAR) of these compounds was analyzed, which led to the identification of a potent GPR68 antagonist (<strong>18l</strong>) with an IC<sub>50</sub> value of 0.081 ± 0.006 μM. The lead compound demonstrated significant inhibition of GPR68-mediated signaling and reduced the production of key pro-inflammatory cytokines. In a dextran sulfate sodium (DSS)-induced mouse model of IBD, <strong>18l</strong> effectively alleviated disease symptoms. It also showed good pharmacokinetic properties and a commendable safety profile. Overall, compound <strong>18l</strong> could be a promising lead compound for the treatment of IBD and deserves further in-depth studies.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"306 ","pages":"Article 118611"},"PeriodicalIF":5.9,"publicationDate":"2026-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146014762","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}
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