{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nguyen HT"],"funding":["Qu? ??i m?i s?ng t?o Vingroup","Viet Nam National University Ho Chi Minh City"],"pagination":["17432-17443"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9134431"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(20)"],"pubmed_abstract":["We report a new pathway to synthesize pyrano[2,3-<i>c</i>]pyrazoles and their binding mode to p38 MAP kinase. Pyrano[2,3-<i>c</i>]pyrazole derivatives have been prepared through a four-component reaction of benzyl alcohols, ethyl acetoacetate, phenylhydrazine, and malononitrile in the presence of sulfonated amorphous carbon and eosin Y as catalysts. All products were characterized by melting point, <sup>1</sup>H and <sup>13</sup>C NMR, and HRMS (ESI). The products were screened <i>in silico</i> for their binding activities to both the ATP-binding pocket and the lipid-binding pocket of p38 MAP kinase, using a structure-based flexible docking provided by the engine ADFR. The results showed that eight synthesized compounds had a higher affinity to the lipid pocket than to the other target sit"],"journal":["ACS omega"],"pubmed_title":["A New Pathway for the Preparation of Pyrano[2,3-<i>c</i>]pyrazoles and molecular Docking as Inhibitors of p38 MAP Kinase."],"pmcid":["PMC9134431"],"funding_grant_id":["C2020-18-09","VINIF.2020.TS.104"],"pubmed_authors":["Truong MH","Tran PH","Vo NT","Le TV","Nguyen HT","Nguyen HD"],"additional_accession":[]},"is_claimable":false,"name":"A New Pathway for the Preparation of Pyrano[2,3-<i>c</i>]pyrazoles and molecular Docking as Inhibitors of p38 MAP Kinase.","description":"We report a new pathway to synthesize pyrano[2,3-<i>c</i>]pyrazoles and their binding mode to p38 MAP kinase. Pyrano[2,3-<i>c</i>]pyrazole derivatives have been prepared through a four-component reaction of benzyl alcohols, ethyl acetoacetate, phenylhydrazine, and malononitrile in the presence of sulfonated amorphous carbon and eosin Y as catalysts. All products were characterized by melting point, <sup>1</sup>H and <sup>13</sup>C NMR, and HRMS (ESI). The products were screened <i>in silico</i> for their binding activities to both the ATP-binding pocket and the lipid-binding pocket of p38 MAP kinase, using a structure-based flexible docking provided by the engine ADFR. The results showed that eight synthesized compounds had a higher affinity to the lipid pocket than to the other target sit","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2026-05-10T01:43:47.01Z","creation":"2025-02-19T02:58:53.216Z"},"accession":"S-EPMC9134431","cross_references":{"pubmed":["35647469"],"doi":["10.1021/acsomega.2c01814"]}}