Future medicinal chemistry最新文献

Design, synthesis, anti-breast cancer and in silico studies of substituted triphenyl imidazole-N-alkyl linked indole derivatives. 取代三苯基咪唑- n -烷基连接吲哚衍生物的设计、合成、抗乳腺癌和硅研究。

IF 3.4 4区医学

Future medicinal chemistry Pub Date : 2025-08-04 DOI: 10.1080/17568919.2025.2539673

Arun Kumar, Sounok Sengupta, Ashok Kumar Yadav, Raman Preet Singh, Tripti Sinha, Pratiti Bhattacharjee, Biswarup Basu, G Marriapan, Sanjib Bhattacharyya, Deepak Kumar

{"title":"Design, synthesis, anti-breast cancer and in silico studies of substituted triphenyl imidazole-N-alkyl linked indole derivatives.","authors":"Arun Kumar, Sounok Sengupta, Ashok Kumar Yadav, Raman Preet Singh, Tripti Sinha, Pratiti Bhattacharjee, Biswarup Basu, G Marriapan, Sanjib Bhattacharyya, Deepak Kumar","doi":"10.1080/17568919.2025.2539673","DOIUrl":"https://doi.org/10.1080/17568919.2025.2539673","url":null,"abstract":"Aim: Cancer is an affliction on societies worldwide, chemotherapy, though effective, has its limitations, indicating the need for new therapeutic agents. Imidazole and indole are two important bioactive heterocycles important for developing newer anticancer molecules.We synthesized a series of substituted imidazole-linked indole derivatives and evaluated them for anticancer activity on MCF-7 cells. Further in silico, cell cycle and apoptosis studies was done for the most active compounds.Materials and methods: Compounds were synthesized by preparing substituted triphenyl imidazoles from benzaldehydes and were further linked to indoles using N-chloroalkyl indoles. The synthesized compounds were characterized and tested for anticancer activity using MTT-assay on MCF-7 cells, followed by a cell-cycle and apoptosis assay of most active compound using flow cytometry. The most active compound was subjected to docking studies using PyRx with the EGFR protein 4HJO, followed by a molecular dynamics simulation using Desmond. Finally, DFT calculations were performed using ORCA 6.0 followed by QSAR analysis of the compounds.Results: Compounds were confirmed by 1H NMR, 13C NMR, mass spectroscopy, and showed IC50 values of 26.52 to 39.05 µM on MCF-7 cells. The most active compound 11i produced apoptosis at its IC50 in MCF-7 cells and arrested the cell cycle in G2/M phase. 11i also had good interactions with 4HJO which confirmed its stability in both molecular dynamics and DFT studies. QSAR studies predicted the relevant structural features for the biological activity.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1-18"},"PeriodicalIF":3.4,"publicationDate":"2025-08-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144775054","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Piperidines as dual inhibitors of tyrosinase and pancreatic lipase: in vitro and in silico mechanistic insights. 哌啶作为酪氨酸酶和胰脂肪酶的双重抑制剂：体外和硅机制的见解。

IF 3.4 4区医学

Future medicinal chemistry Pub Date : 2025-08-01 DOI: 10.1080/17568919.2025.2539672

Nafeesa Naeem, Ehsan Ullah Mughal, Bushra Shakoor, Amina Sadiq, Gehan Ahmed Othman, Ercan Bursal, Fuat Yetişsin

{"title":"Piperidines as dual inhibitors of tyrosinase and pancreatic lipase: in vitro and in silico mechanistic insights.","authors":"Nafeesa Naeem, Ehsan Ullah Mughal, Bushra Shakoor, Amina Sadiq, Gehan Ahmed Othman, Ercan Bursal, Fuat Yetişsin","doi":"10.1080/17568919.2025.2539672","DOIUrl":"https://doi.org/10.1080/17568919.2025.2539672","url":null,"abstract":"Aims: This study aimed to explore the dual inhibitory potential of a series of piperidine derivatives against tyrosinase and pancreatic lipase. For the first time, these compounds were evaluated concurrently for their inhibitory effects on both enzymes, targeting potential therapeutic applications in hyperpigmentation and obesity-related disorders.Materials and methods: A total of eight piperidine-based compounds were synthesized and assessed for in vitro inhibitory activity against mushroom tyrosinase and pancreatic lipase. The most active derivatives underwent kinetic studies to determine the mode of inhibition using Lineweaver-Burk plots. Structure-activity relationship (SAR) analysis was performed to identify key substituents influencing bioactivity. Furthermore, molecular docking, molecular dynamics (MD) simulations, and density functional theory (DFT) calculations were conducted to elucidate the binding interactions and electronic properties associated with inhibition.Results: Among the tested compounds, several exhibited significant dual inhibitory activity, with low micromolar IC50 values against both enzymes. Kinetic analysis revealed competitive inhibition for the lead compound. Docking and MD simulations confirmed stable binding within the active sites of both enzymes, supported by favorable DFT descriptors.Conclusions: These findings reveal, for the first time, that piperidine derivatives possess promising dual inhibitory activity against tyrosinase and pancreatic lipase, supported by both experimental and computational evidence.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1-18"},"PeriodicalIF":3.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144759667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The current landscape of quinazoline derivatives with in vivo anticancer therapeutic potential-part II. 具有体内抗癌治疗潜力的喹唑啉衍生物的现状-第二部分。

IF 3.4 4区医学

Future medicinal chemistry Pub Date : 2025-07-30 DOI: 10.1080/17568919.2025.2539670

Shanshan Huang, Zhi Xu, Yan Zhang, Jialin Zhu, Wenjun Zhou

引用次数: 0

Exploring norfloxacin analogs in combating antimicrobial resistance: design, mechanistic insights and structure activity relationship. 探索诺氟沙星类似物在抗微生物药物耐药性中的作用：设计、机制和结构活性关系。

IF 3.2 4区医学

Future medicinal chemistry Pub Date : 2025-07-21 DOI: 10.1080/17568919.2025.2533108

Aanchal Khanna, Karanvir Singh, Jyoti, Nitish Kumar, Harmandeep Kaur, Rakshit Badhwar, Jagtar Singh, Preet Mohinder Singh Bedi

{"title":"Exploring norfloxacin analogs in combating antimicrobial resistance: design, mechanistic insights and structure activity relationship.","authors":"Aanchal Khanna, Karanvir Singh, Jyoti, Nitish Kumar, Harmandeep Kaur, Rakshit Badhwar, Jagtar Singh, Preet Mohinder Singh Bedi","doi":"10.1080/17568919.2025.2533108","DOIUrl":"https://doi.org/10.1080/17568919.2025.2533108","url":null,"abstract":"Norfloxacin (NF), a fluoroquinolone (FN) antibiotic, has garnered significant attention for its broad-spectrum antimicrobial activity, particularly against gram-negative bacteria. This review article explores the structural modifications and derivatives of NF that enhance its efficacy and broaden its antimicrobial spectrum. We systematically analyze various chemical modifications, including substitutions at the 7 and 8 positions of the quinolone core, and their impact on antibacterial potency, pharmacokinetics, and resistance profiles. Additionally, we discuss the mechanisms of action of NF derivatives, their effectiveness against resistant strains, and the potential for synergistic combinations with other antimicrobial agents. The review highlights promising candidates from recent studies, emphasizing the need for continued research into NF derivatives as potential therapeutic options in the fight against multidrug-resistant infections. Ultimately, this article aims to provide a comprehensive overview of the advancements in NF derivatives, contributing to the development of novel antimicrobial strategies.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1-17"},"PeriodicalIF":3.2,"publicationDate":"2025-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144674394","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Epigenetic therapy meets targeted protein degradation: HDAC-PROTACs in cancer treatment. 表观遗传治疗满足靶向蛋白降解：HDAC-PROTACs在癌症治疗中的应用。

IF 3.2 4区医学

Future medicinal chemistry Pub Date : 2025-07-16 DOI: 10.1080/17568919.2025.2533113

Md Sadique Hussain, Liming Zhang, Amita Joshi Rana, Mudasir Maqbool, Sumel Ashique, Yumna Khan, Vikas Jakhmola, Ali Hanbashi, Wedad Mawkili, Gyas Khan

{"title":"Epigenetic therapy meets targeted protein degradation: HDAC-PROTACs in cancer treatment.","authors":"Md Sadique Hussain, Liming Zhang, Amita Joshi Rana, Mudasir Maqbool, Sumel Ashique, Yumna Khan, Vikas Jakhmola, Ali Hanbashi, Wedad Mawkili, Gyas Khan","doi":"10.1080/17568919.2025.2533113","DOIUrl":"https://doi.org/10.1080/17568919.2025.2533113","url":null,"abstract":"Epigenetic therapy and targeted protein degradation have converged in the development of histone deacetylases (HDACs)-targeting proteolysis-targeting chimeras (PROTACs), offering a novel approach to cancer treatment. Unlike traditional HDAC inhibitors, HDAC-PROTACs facilitate selective degradation of HDACs via the ubiquitin-proteasome system, effectively eliminating both enzymatic and scaffolding functions. These bifunctional molecules recruit HDACs to E3 ligases, triggering ubiquitination and subsequent proteasomal degradation. PROTACs demonstrate catalytic activity, requiring lower dosages while sustaining prolonged effects compared to inhibitors. Advances in PROTAC chemistry have led to the development of selective degraders targeting distinct HDAC classes. Class I HDAC-targeting PROTACs, such as PROTAC 1 and PROTAC 2, induce robust degradation of HDAC1-3 with nanomolar DC50 values, showing promising anti-cancer activity. Similarly, class IIa and IIb HDAC PROTACs, including selective HDAC4 and HDAC6 degraders, exhibit potent anti-proliferative effects in leukemia, lymphoma, and multiple myeloma models. Despite these advancements, challenges persist in optimizing selectivity, linker design, and bioavailability while mitigating off-target effects. Future strategies include enhancing tumor-specific delivery, refining ligand-E3 ligase compatibility, and integrating combination therapies to overcome resistance. This review explores the mechanistic insights, therapeutic potential, and challenges associated with HDAC-targeting PROTACs, highlighting their promising role in precision oncology.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1-13"},"PeriodicalIF":3.2,"publicationDate":"2025-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144642219","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Green synthesis, in vitro, and in silico assessments of hydrazone-Schiff bases as potential antileishmanial agents. 作为潜在抗利什曼原虫药物的腙希夫碱的绿色合成、体外和计算机评价。

IF 3.2 4区医学

Future medicinal chemistry Pub Date : 2025-07-16 DOI: 10.1080/17568919.2025.2533114

Sadia Khan, Sher Wali Khan, Momin Khan, Saira Nayab, Muhammad Naveed Umar, Syed Wadood Ali Shah, Haroon Ur Rashid

{"title":"Green synthesis, in vitro, and in silico assessments of hydrazone-Schiff bases as potential antileishmanial agents.","authors":"Sadia Khan, Sher Wali Khan, Momin Khan, Saira Nayab, Muhammad Naveed Umar, Syed Wadood Ali Shah, Haroon Ur Rashid","doi":"10.1080/17568919.2025.2533114","DOIUrl":"https://doi.org/10.1080/17568919.2025.2533114","url":null,"abstract":"Aims: To synthesize and assess hydrazone Schiff bases using green chemistry principles for potential antileishmanial activity.Materials & methods: Sixteen hydrazone Schiff bases, including seven novel compounds (SSB2, SSB4, SSB5, RSB4, SSB14, SSB15, and SSB31), were synthesized under solvent-free conditions using grinding technique. The compounds were structurally confirmed via FT-IR, 1 H NMR, and 1 3 C NMR spectroscopy. Their in vitro antileishmanial activities were evaluated versus Leishmania tropica promastigotes and amastigotes. Molecular docking studies targeted leishmanolysin enzyme, while Absorption, Distribution, Metabolism, Excretion, and Toxicity (ADMET) and Density Functional Theory (DFT) analyses were used to predict pharmacokinetics, drug-likeness and stability.Results: Most compounds showed moderate to good activity, with SSB28, SSB35, SSB36, and RSB4 displaying IC₅₀ values between 4 ± 0.5 and 8.0 ± 0.2 µg/mL. SSB28 was the most potent, with its IC₅₀ values of 4 ± 0.5 and 4.5 ± 0.4 µg/mL versus Promastigote and amastigote respectively as compared to the reference drug Amphotericin-B (IC50 2.0 and 2.3 ± 0.5 µg/mL). Docking studies indicated strong binding of SSB28 to leishmanolysin. ADMET and DFT results showed that SSB28 possesses favorable pharmacokinetics and low predicted toxicity.Conclusions: SSB28 is an encouraging antileishmanial lead derivative with potent activity, environmental compatibility, and predicted safety making it a feasible candidate for further drug development.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1-17"},"PeriodicalIF":3.2,"publicationDate":"2025-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144649075","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Exploring digestive enzymes' differential affectivity of synthesized 2-thienyl-based chalcones. 探索消化酶对合成的2-噻吩基查尔酮的差异性影响。

IF 3.4 4区医学

Future medicinal chemistry Pub Date : 2025-07-01 Epub Date: 2025-07-04 DOI: 10.1080/17568919.2025.2527583

Prabhjot Kaur, Urmila Berar, Neera Raghav

{"title":"Exploring digestive enzymes' differential affectivity of synthesized 2-thienyl-based chalcones.","authors":"Prabhjot Kaur, Urmila Berar, Neera Raghav","doi":"10.1080/17568919.2025.2527583","DOIUrl":"10.1080/17568919.2025.2527583","url":null,"abstract":"Aim: This study aimed to synthesize thiophene-based chalcones using green and conventional methods and evaluate their modulatory effects on key digestive enzymes-α-amylase, lipase, and trypsin for potential therapeutic applications in metabolic disorders.Materials & methods: A series of twenty 2-acetylthiophene-based chalcones were synthesized via Claisen-Schmidt condensation using conventional, grinding, and ultrasonication methods. The compounds were characterized using FTIR, NMR, and melting point analysis. In vitro enzyme assays were conducted to assess activity against α-amylase, lipase, and trypsin. Molecular docking, drug-likeness, and ADMET profiling were performed in silico to predict binding interactions and pharmacokinetic properties.Results: Ultrasonication offered the highest yield in the shortest time. Chalcones inhibited lipase (40.18-74.23%) and trypsin (40.86-73.91%), with compounds 3q and 3r showing the strongest inhibition (IC₅₀ = 1.25 × 10-8 M and 1.17 × 10-8 M, respectively). Unexpectedly, α-amylase activation (50.18-75.18%) was observed, with compound 3g being the most effective. Docking studies supported enzyme binding, and ADMET analysis confirmed favorable safety profiles.Conclusions: Thiophene-based chalcones exhibit promising digestive enzyme modulatory properties, particularly as lipase and trypsin inhibitors, with potential application in managing obesity and related metabolic disorders.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1535-1545"},"PeriodicalIF":3.4,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12309531/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144559766","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Overcoming translational barriers in RNA-protein docking: enhancing computational accuracy for targeted drug discovery. 克服rna -蛋白对接中的翻译障碍：提高靶向药物发现的计算准确性。

IF 3.4 4区医学

Future medicinal chemistry Pub Date : 2025-07-01 Epub Date: 2025-07-18 DOI: 10.1080/17568919.2025.2533061

Habiba Akram, Muneeb Ur Rahman, Sharjeel Mazhar, Farheen Qamer, Ayesha Yousaf

{"title":"Overcoming translational barriers in RNA-protein docking: enhancing computational accuracy for targeted drug discovery.","authors":"Habiba Akram, Muneeb Ur Rahman, Sharjeel Mazhar, Farheen Qamer, Ayesha Yousaf","doi":"10.1080/17568919.2025.2533061","DOIUrl":"10.1080/17568919.2025.2533061","url":null,"abstract":"RNA-protein interactions can play a crucial role in the regulation of gene expression, cellular processes, and progression of diseases, thus making them one of the major targets for drug discovery. Although knowledge of these complex interactions remains limited, owing to less structural resolution data, computational, and translational challenges. The review overviews the evolution of advanced computational docking tools and recent cutting-edge innovations in RNA-protein interaction research, by highlighting advanced and highly precise approaches such as cryo-electron microscopy (cryo-EM), nuclear magnetic resonance (NMR) spectroscopy, and novel molecular docking models like DiffDock. Furthermore, the integration of multi-omics data and machine learning approaches in drug discovery not only improves precision but also the speed and efficiency of docking, thus highlighting the dynamic and highly complex nature of RNA molecules. The major translational hurdles that limit the bridging between computational predictions and clinical applications are also highlighted, thus demanding more interdisciplinary collaborations to achieve the desired biomolecular targets. By emphasizing computational modeling, structural biology, clinical pharmacology, and translational barriers in RNA-protein docking, the article provides a comprehensive framework to speed up the highly specific, accurate, and precise drug discovery of novel therapeutics targeting RNA-protein interactions.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1623-1640"},"PeriodicalIF":3.4,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12309545/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144658887","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Progress and challenges in the development of clinically viable Piezo1 inhibitors. 临床可行的Piezo1抑制剂的发展进展和挑战。

IF 3.4 4区医学

Future medicinal chemistry Pub Date : 2025-07-01 Epub Date: 2025-07-11 DOI: 10.1080/17568919.2025.2532996

Daniel Baecker

引用次数: 0

Benzimidazole derivatives as potent α-amylase inhibitors: synthesis, characterization and in vitro α-amylase inhibition. 苯并咪唑衍生物α-淀粉酶抑制剂：合成、表征及体外α-淀粉酶抑制作用。

IF 3.4 4区医学

Future medicinal chemistry Pub Date : 2025-07-01 Epub Date: 2025-07-16 DOI: 10.1080/17568919.2025.2527585

Shantaben K Kangad, Sachin M Sitapara, Deepika Maliwal, Chintan Somaiya, Raghuvir R S Pissurlenkar, V N Patolia

{"title":"Benzimidazole derivatives as potent α-amylase inhibitors: synthesis, characterization and in vitro α-amylase inhibition.","authors":"Shantaben K Kangad, Sachin M Sitapara, Deepika Maliwal, Chintan Somaiya, Raghuvir R S Pissurlenkar, V N Patolia","doi":"10.1080/17568919.2025.2527585","DOIUrl":"10.1080/17568919.2025.2527585","url":null,"abstract":"Aim: This study aims to evaluate the α-amylase inhibitory potential of newly synthesized benzimidazole derivatives, assessing their viability as prospective antidiabetic agents.Materials & methods: A series of 2-(4-(1H-benzo[d]imidazol-2-yl)piperidin-1-yl)-N-phenylacetamide derivatives (7a-7j) were synthesized via an efficient synthetic route. The structural elucidation of these compounds was accomplished using advanced spectroscopic techniques, including mass spectrometry, FT-IR, 1H & 13C NMR, and elemental analysis. The α-amylase inhibitory activity of the synthesized compounds was evaluated in vitro, with IC₅₀ values determined to quantify their efficacy. To gain insights into the molecular interactions, molecular docking studies were conducted, followed by extensive molecular dynamics (MD) simulations.Result & discussion: All synthesized derivatives exhibited varying degrees of α-amylase inhibitory activity, with IC₅₀ values ranging from 1.10 ± 0.05 to 12.50 ± 0.30 μM. Notably, compounds 7b, 7c, and 7i demonstrated superior inhibitory effects, with IC₅₀ values of 1.20 ± 0.05, 1.40 ± 0.10, and 1.10 ± 0.05 μM, respectively, surpassing the standard drug acarbose (IC₅₀ = 1.70 ± 0.10 μM).Conclusion: The synthesized benzimidazole derivatives, notably compounds 7b, 7c, and 7i, demonstrated potent α-amylase inhibitory activity, surpassing the standard drug acarbose. These findings highlight their potential as lead compounds for developing novel antidiabetic agents.","PeriodicalId":12475,"journal":{"name":"Future medicinal chemistry","volume":" ","pages":"1521-1533"},"PeriodicalIF":3.4,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12309533/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144642216","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0