ACS Pharmacology and Translational Science最新文献_第6页

Exploring G Protein-Coupled Receptors in Hematological Cancers. 血液学癌症中G蛋白偶联受体的研究

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-21 eCollection Date: 2024-12-13 DOI: 10.1021/acsptsci.4c00473

Choi Har Tsang, Pawel Kozielewicz

{"title":"Exploring G Protein-Coupled Receptors in Hematological Cancers.","authors":"Choi Har Tsang, Pawel Kozielewicz","doi":"10.1021/acsptsci.4c00473","DOIUrl":"10.1021/acsptsci.4c00473","url":null,"abstract":"Hematological cancers, such as lymphomas and leukemias, pose significant challenges in oncology, necessitating a deeper understanding of their molecular landscape to enhance therapeutic strategies. This article critically examines and discusses recent research on the roles of G protein-coupled receptors (GPCRs) in myeloma, lymphomas, and leukemias with a particular focus on pediatric acute lymphoblastic (lymphocytic) leukemia (ALL). By utilizing RNA sequencing (RNA-seq), we analyzed GPCR expression patterns in pediatric ALL samples (aged 3-12 years old), with a further focus on Class A orphan GPCRs. Our analysis revealed distinct GPCR expression profiles in pediatric ALL, identifying several candidates with aberrant upregulated expression compared with healthy counterparts. Among these GPCRs, GPR85, GPR65, and GPR183 have varying numbers of studies in the field of hematological cancers and pediatric ALL. Furthermore, we explored missense mutations of pediatric ALL in relation to the RNA gene expression findings, providing insights into the genetic underpinnings of this disease. By integrating both RNA-seq and missense mutation data, this article aims to provide an insightful and broader perspective on the potential correlations between specific GPCR and their roles in pediatric ALL.","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"4000-4009"},"PeriodicalIF":4.9,"publicationDate":"2024-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11651347/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142855619","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}

引用次数: 0

Screened Fv-Antibodies against the Angiotensin-Converting Enzyme 2 (ACE2) Receptor Neutralizing the Infection of SARS-CoV-2 筛选出的抗血管紧张素转换酶2（ACE2）受体的Fv-抗体能中和SARS-CoV-2病毒感染

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-19 DOI: 10.1021/acsptsci.4c0044110.1021/acsptsci.4c00441

Jaeyong Jung, Soonil Kwon, Jeong Soo Sung, Hyung Eun Bae, Min-Jung Kang, Joachim Jose, Misu Lee* and Jae-Chul Pyun*,

引用次数: 0

Discovery of 7,9-Dibromo-dihydrodibenzofuran as a Potent Casein Kinase 2 (CK2) Inhibitor: Synthesis, Biological Evaluation, and Structural Studies on E-/Z-Isomers. 7,9-二溴二氢二苯并呋喃作为强效酪蛋白激酶2 （CK2）抑制剂的发现：E-/ z异构体的合成、生物学评价和结构研究

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-19 eCollection Date: 2024-12-13 DOI: 10.1021/acsptsci.4c00426

Hendrik Rumler, Claudia Schmithals, Christian Werner, Andre Bollacke, Dagmar Aichele, Claudia Götz, Karsten Niefind, Bernhard Wünsch, Joachim Jose

{"title":"Discovery of 7,9-Dibromo-dihydrodibenzofuran as a Potent Casein Kinase 2 (CK2) Inhibitor: Synthesis, Biological Evaluation, and Structural Studies on E-/Z-Isomers.","authors":"Hendrik Rumler, Claudia Schmithals, Christian Werner, Andre Bollacke, Dagmar Aichele, Claudia Götz, Karsten Niefind, Bernhard Wünsch, Joachim Jose","doi":"10.1021/acsptsci.4c00426","DOIUrl":"10.1021/acsptsci.4c00426","url":null,"abstract":"The human protein kinase CK2 is a promising target for cancer treatment. Only two CK2 inhibitors have reached clinical trials until today. Among others, a dibenzofuran scaffold has emerged as highly prospective for the development of new CK2 inhibitors. Thirty-three newly synthesized dibenzofuran-based compounds were tested on their inhibitory potential in vitro. 7,9-Dichloro-8-hydroxy-4-[(phenylamino)methylene]-1,2-dihydro-dibenzo[b,d]furan-3(4H)-one (12b) and 7,9-dibromo-8-hydroxy-4-[(phenylamino)methylene]-1,2-dihydro-dibenzo[b,d]furan-3(4H)-one (12c) showed the lowest IC50 values with 5.8 nM for both. The dibenzofuran-based CK2 inhibitors crossed the cell membrane of LNCaP human prostate carcinoma cells and reduced intracellular CK2 activity. Among 70 kinases from different representative subgroups of the human kinome, CK2 was most strongly inhibited by compound 12c. Co-crystallization of 12c together with CK2α indicated a π-halogen bond of the bromine at position C9 with the gatekeeper amino acid Phe113. CK2α could bind both the E- and Z-isomers of 12c. Our results provide new insights into the structure-activity relationships of dibenzofuran derivatives.","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"3846-3866"},"PeriodicalIF":4.9,"publicationDate":"2024-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11651316/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142855680","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}

引用次数: 0

Discovery of 7,9-Dibromo-dihydrodibenzofuran as a Potent Casein Kinase 2 (CK2) Inhibitor: Synthesis, Biological Evaluation, and Structural Studies on E-/Z-Isomers 7,9-二溴二氢二苯并呋喃作为强效酪蛋白激酶2 （CK2）抑制剂的发现：E-/ z异构体的合成、生物学评价和结构研究

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-19 DOI: 10.1021/acsptsci.4c0042610.1021/acsptsci.4c00426

Hendrik Rumler, Claudia Schmithals, Christian Werner, Andre Bollacke, Dagmar Aichele, Claudia Götz, Karsten Niefind, Bernhard Wünsch and Joachim Jose*,

{"title":"Discovery of 7,9-Dibromo-dihydrodibenzofuran as a Potent Casein Kinase 2 (CK2) Inhibitor: Synthesis, Biological Evaluation, and Structural Studies on E-/Z-Isomers","authors":"Hendrik Rumler, Claudia Schmithals, Christian Werner, Andre Bollacke, Dagmar Aichele, Claudia Götz, Karsten Niefind, Bernhard Wünsch and Joachim Jose*, ","doi":"10.1021/acsptsci.4c0042610.1021/acsptsci.4c00426","DOIUrl":"https://doi.org/10.1021/acsptsci.4c00426https://doi.org/10.1021/acsptsci.4c00426","url":null,"abstract":"The human protein kinase CK2 is a promising target for cancer treatment. Only two CK2 inhibitors have reached clinical trials until today. Among others, a dibenzofuran scaffold has emerged as highly prospective for the development of new CK2 inhibitors. Thirty-three newly synthesized dibenzofuran-based compounds were tested on their inhibitory potential in vitro. 7,9-Dichloro-8-hydroxy-4-[(phenylamino)methylene]-1,2-dihydro-dibenzo[b,d]furan-3(4H)-one (12b) and 7,9-dibromo-8-hydroxy-4-[(phenylamino)methylene]-1,2-dihydro-dibenzo[b,d]furan-3(4H)-one (12c) showed the lowest IC50 values with 5.8 nM for both. The dibenzofuran-based CK2 inhibitors crossed the cell membrane of LNCaP human prostate carcinoma cells and reduced intracellular CK2 activity. Among 70 kinases from different representative subgroups of the human kinome, CK2 was most strongly inhibited by compound 12c. Co-crystallization of 12c together with CK2α indicated a π-halogen bond of the bromine at position C9 with the gatekeeper amino acid Phe113. CK2α could bind both the E- and Z-isomers of 12c. Our results provide new insights into the structure–activity relationships of dibenzofuran derivatives.","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"3846–3866 3846–3866"},"PeriodicalIF":4.9,"publicationDate":"2024-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142842768","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}

引用次数: 0

Screened Fv-Antibodies against the Angiotensin-Converting Enzyme 2 (ACE2) Receptor Neutralizing the Infection of SARS-CoV-2. 筛选抗血管紧张素转换酶2受体fv抗体中和SARS-CoV-2感染。

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-19 eCollection Date: 2024-12-13 DOI: 10.1021/acsptsci.4c00441

Jaeyong Jung, Soonil Kwon, Jeong Soo Sung, Hyung Eun Bae, Min-Jung Kang, Joachim Jose, Misu Lee, Jae-Chul Pyun

引用次数: 0

Covalent Fragments Acting as Tyrosine Mimics for Mutant p53-Y220C Rescue by Nucleophilic Aromatic Substitution 共价片段作为酪氨酸模拟物通过亲核芳香取代拯救突变体p53-Y220C

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-18 DOI: 10.1021/acsptsci.4c0041410.1021/acsptsci.4c00414

Theresa Klett, Jason Stahlecker, Simon Jaag, Benedikt Masberg, Cornelius Knappe, Michael Lämmerhofer, Murray Coles, Thilo Stehle and Frank M. Boeckler*,

{"title":"Covalent Fragments Acting as Tyrosine Mimics for Mutant p53-Y220C Rescue by Nucleophilic Aromatic Substitution","authors":"Theresa Klett, Jason Stahlecker, Simon Jaag, Benedikt Masberg, Cornelius Knappe, Michael Lämmerhofer, Murray Coles, Thilo Stehle and Frank M. Boeckler*, ","doi":"10.1021/acsptsci.4c0041410.1021/acsptsci.4c00414","DOIUrl":"https://doi.org/10.1021/acsptsci.4c00414https://doi.org/10.1021/acsptsci.4c00414","url":null,"abstract":"The tumor suppressor p53 is frequently mutated in human cancers. The Y220C mutant is the ninth most common p53 cancer mutant and is classified as a structural mutant, as it leads to strong thermal destabilization and degradation by creating a solvent-accessible hydrophobic cleft. To identify small molecules that thermally stabilize p53, we employed DSF to screen SNAr-type electrophiles from our covalent fragment library (CovLib) for binding to different structural (Y220C, R282W) and DNA contact (R273H) mutants of p53. The reactive fragments SN001, SN006, and SN007 were detected to specifically stabilize Y220C, indicating the arylation of Cys220 in the mutational cleft, as confirmed by X-ray crystallography. The fragments occupy the central cavity and mimic the ring system of the WT tyrosine lost by the mutation. Surpassing previously reported noncovalent ligands, SN001 stabilized T-p53C-Y220C concentration-dependently up to 4.45 °C and, due to its small size, represents a promising starting point for optimization.","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"3984–3999 3984–3999"},"PeriodicalIF":4.9,"publicationDate":"2024-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142850034","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}

引用次数: 0

Covalent Fragments Acting as Tyrosine Mimics for Mutant p53-Y220C Rescue by Nucleophilic Aromatic Substitution. 共价片段作为酪氨酸模拟物通过亲核芳香取代拯救突变体p53-Y220C。

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-18 eCollection Date: 2024-12-13 DOI: 10.1021/acsptsci.4c00414

Theresa Klett, Jason Stahlecker, Simon Jaag, Benedikt Masberg, Cornelius Knappe, Michael Lämmerhofer, Murray Coles, Thilo Stehle, Frank M Boeckler

{"title":"Covalent Fragments Acting as Tyrosine Mimics for Mutant p53-Y220C Rescue by Nucleophilic Aromatic Substitution.","authors":"Theresa Klett, Jason Stahlecker, Simon Jaag, Benedikt Masberg, Cornelius Knappe, Michael Lämmerhofer, Murray Coles, Thilo Stehle, Frank M Boeckler","doi":"10.1021/acsptsci.4c00414","DOIUrl":"10.1021/acsptsci.4c00414","url":null,"abstract":"The tumor suppressor p53 is frequently mutated in human cancers. The Y220C mutant is the ninth most common p53 cancer mutant and is classified as a structural mutant, as it leads to strong thermal destabilization and degradation by creating a solvent-accessible hydrophobic cleft. To identify small molecules that thermally stabilize p53, we employed DSF to screen SNAr-type electrophiles from our covalent fragment library (CovLib) for binding to different structural (Y220C, R282W) and DNA contact (R273H) mutants of p53. The reactive fragments SN001, SN006, and SN007 were detected to specifically stabilize Y220C, indicating the arylation of Cys220 in the mutational cleft, as confirmed by X-ray crystallography. The fragments occupy the central cavity and mimic the ring system of the WT tyrosine lost by the mutation. Surpassing previously reported noncovalent ligands, SN001 stabilized T-p53C-Y220C concentration-dependently up to 4.45 °C and, due to its small size, represents a promising starting point for optimization.","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"3984-3999"},"PeriodicalIF":4.9,"publicationDate":"2024-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11651176/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142855340","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}

引用次数: 0

Developing MYC Degraders Bearing the Von Hippel-Lindau Ligand to Target the "Undruggable" MYC. 开发携带Von Hippel-Lindau配体的MYC降解剂以靶向“不可药物”的MYC。

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-15 eCollection Date: 2024-12-13 DOI: 10.1021/acsptsci.4c00452

Christos Siokatas, Alexandra Lampropoulou, Alexandra Smina, Katerina Soupsana, Martha Kontostathi, Athina-Vasiliki Karra, Theodoros Karampelas, Anastasia S Politou, Savvas Christoforidis, Constantin Tamvakopoulos, Vasiliki Sarli

{"title":"Developing MYC Degraders Bearing the Von Hippel-Lindau Ligand to Target the \"Undruggable\" MYC.","authors":"Christos Siokatas, Alexandra Lampropoulou, Alexandra Smina, Katerina Soupsana, Martha Kontostathi, Athina-Vasiliki Karra, Theodoros Karampelas, Anastasia S Politou, Savvas Christoforidis, Constantin Tamvakopoulos, Vasiliki Sarli","doi":"10.1021/acsptsci.4c00452","DOIUrl":"10.1021/acsptsci.4c00452","url":null,"abstract":"Although small-molecule inhibitors with moderate efficacy targeting MYC have been previously described, to this point, research efforts have failed to bring a suitable small-molecule MYC inhibitor to the clinic. Herein, the discovery of a series of novel MYC degraders bearing VHL to target the \"undruggable\" MYC is presented. The molecules are based on connecting a known MYC binder to a VHL ligand or pomalidomide to induce MYC degradation in various cancer cells known to express MYC. Representative compounds from our work induced MYC degradation in a time- and dose-dependent manner. Selected compounds, CSI86 and CSI107, displayed antiproliferative activity (IC50 values of 13-18 μM) against breast and prostate cancer cells. The lead molecules were further evaluated in terms of cell uptake, potential to degrade MYC, and pharmacokinetics in mice. Encouraging results presented herein suggest that the presented analogs may serve as prototype structures of future therapeutic agents for the treatment of MYC-dependent tumors. MYC protein degraders can well complement the more established inhibition approaches that have been presented in the past (e.g., disruption of the MYC-MAX complex formation by small-molecule inhibitors).","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"3955-3968"},"PeriodicalIF":4.9,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11650737/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142855476","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}

引用次数: 0

Developing MYC Degraders Bearing the Von Hippel–Lindau Ligand to Target the “Undruggable” MYC 开发携带Von Hippel-Lindau配体的MYC降解剂以靶向“不可药物”的MYC

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-15 DOI: 10.1021/acsptsci.4c0045210.1021/acsptsci.4c00452

Christos Siokatas, Alexandra Lampropoulou, Alexandra Smina, Katerina Soupsana, Martha Kontostathi, Athina-Vasiliki Karra, Theodoros Karampelas, Anastasia S. Politou, Savvas Christoforidis, Constantin Tamvakopoulos* and Vasiliki Sarli*,

{"title":"Developing MYC Degraders Bearing the Von Hippel–Lindau Ligand to Target the “Undruggable” MYC","authors":"Christos Siokatas, Alexandra Lampropoulou, Alexandra Smina, Katerina Soupsana, Martha Kontostathi, Athina-Vasiliki Karra, Theodoros Karampelas, Anastasia S. Politou, Savvas Christoforidis, Constantin Tamvakopoulos* and Vasiliki Sarli*, ","doi":"10.1021/acsptsci.4c0045210.1021/acsptsci.4c00452","DOIUrl":"https://doi.org/10.1021/acsptsci.4c00452https://doi.org/10.1021/acsptsci.4c00452","url":null,"abstract":"Although small-molecule inhibitors with moderate efficacy targeting MYC have been previously described, to this point, research efforts have failed to bring a suitable small-molecule MYC inhibitor to the clinic. Herein, the discovery of a series of novel MYC degraders bearing VHL to target the “undruggable” MYC is presented. The molecules are based on connecting a known MYC binder to a VHL ligand or pomalidomide to induce MYC degradation in various cancer cells known to express MYC. Representative compounds from our work induced MYC degradation in a time- and dose-dependent manner. Selected compounds, CSI86 and CSI107, displayed antiproliferative activity (IC50 values of 13–18 μM) against breast and prostate cancer cells. The lead molecules were further evaluated in terms of cell uptake, potential to degrade MYC, and pharmacokinetics in mice. Encouraging results presented herein suggest that the presented analogs may serve as prototype structures of future therapeutic agents for the treatment of MYC-dependent tumors. MYC protein degraders can well complement the more established inhibition approaches that have been presented in the past (e.g., disruption of the MYC–MAX complex formation by small-molecule inhibitors).","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"3955–3968 3955–3968"},"PeriodicalIF":4.9,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acsptsci.4c00452","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142842933","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}

引用次数: 0

Aptamer Proteolysis-Targeting Chimeras (PROTACs): A Novel Strategy to Combat Drug Resistance in Estrogen Receptor α-Positive Breast Cancer. 适体蛋白水解靶向嵌合体（PROTACs）：对抗雌激素受体α阳性乳腺癌耐药的新策略

IF 4.9

ACS Pharmacology and Translational Science Pub Date : 2024-11-14 eCollection Date: 2024-12-13 DOI: 10.1021/acsptsci.4c00469

Ying Feng, Zhilin Zhang, Haowei Zhang, Hui Guo, Chunyan Tan, Naihan Xu, Ying Tan, Yuyang Jiang

{"title":"Aptamer Proteolysis-Targeting Chimeras (PROTACs): A Novel Strategy to Combat Drug Resistance in Estrogen Receptor α-Positive Breast Cancer.","authors":"Ying Feng, Zhilin Zhang, Haowei Zhang, Hui Guo, Chunyan Tan, Naihan Xu, Ying Tan, Yuyang Jiang","doi":"10.1021/acsptsci.4c00469","DOIUrl":"10.1021/acsptsci.4c00469","url":null,"abstract":"Breast cancer with positive expression of estrogen receptor α (ERα+) accounts for 70% of breast cancer cases, whose predominant treatment is currently endocrine therapy. The main strategy of endocrine therapy for ERα+ breast cancer is to inhibit the ERα signaling pathway and downregulate ERα levels, which often results in mutations in the ligand-binding domain (LBD) of ERα, leading to significant resistance to subsequent treatment in patients. To combat drug resistance, we first proposed a novel aptamer PROTAC strategy through specifically targeted degradation of ERα via targeting the DNA-binding domain (DBD) of ERα. We proved that this strategy is capable of targeting ERα for degradation through ubiquitination, leading to the inhibition of proliferation in ERα+ breast cancer cells and tamoxifen-resistant breast cancer cells. Furthermore, we investigated the mechanisms involved in overcoming resistance. By circumventing drug resistance associated with LBD mutations in ERα, our approach provides a promising avenue for the discovery of new therapeutic agents.","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"7 12","pages":"3945-3954"},"PeriodicalIF":4.9,"publicationDate":"2024-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11650730/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142855790","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}

引用次数: 0