{"doi":"10.18388/abp.2014_953","title":"[5-(Benzyloxy)-1H-indol-1-yl]acetic acid, an aldose reductase inhibitor and PPARγ ligand","abstract":null,"journal":"Acta Biochimica Polonica","year":2015,"id":687018,"datarank":0.32958368660043297,"base_score":2.1972245773362196,"endowment":2.1972245773362196,"self_citation_contribution":0.32958368660043297,"citation_network_contribution":0.0,"self_endowment_contribution":0.32958368660043297,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":8,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1794799,"name":"Magdalena Majekova","orcid":null,"position":1,"is_corresponding":false},{"id":1794800,"name":"Ivana Milackova","orcid":null,"position":2,"is_corresponding":false},{"id":1794801,"name":"Beatriz Díez-Dacal","orcid":null,"position":3,"is_corresponding":false},{"id":1794803,"name":"Dolores Pérez-Sala","orcid":null,"position":4,"is_corresponding":false},{"id":1794804,"name":"Muserref Seyma Ceyhan","orcid":null,"position":5,"is_corresponding":false},{"id":1794805,"name":"Sreeparna Banerjee","orcid":null,"position":6,"is_corresponding":false},{"id":1794806,"name":"Milan Stefek","orcid":null,"position":7,"is_corresponding":false},{"id":1794798,"name":"Marta Soltesova Prnova","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"[5-(Benzyloxy)-1H-indol-1-yl]acetic acid, an aldose reductase inhibitor and PPARγ ligand","abstract":"Based on overlapping structural requirements for both efficient aldose reductase inhibitors and PPAR ligands, [5-(benzyloxy)-1H-indol-1-yl]acetic acid (compound 1) was assessed for inhibition of aldose reductase and ability to interfere with PPARγ. Aldose reductase inhibition by 1 was characterized by IC50 in submicromolar and low micromolar range, for rat and human enzyme, respectively. Selectivity in relation to the closely related rat kidney aldehyde reductase was characterized by approx. factor 50. At organ level in isolated rat lenses, compound 1 significantly inhibited accumulation of sorbitol in a concentration-dependent manner. To identify crucial interactions within the enzyme binding site, molecular docking simulations were performed. Based on luciferase reporter assays, compound 1 was found to act as a ligand for PPARγ, yet with rather low activity. On balance, compound 1 is suggested as a promising lead-like scaffold for agents with the potential to interfere with multiple targets in diabetes.","is_dataset_classified":null,"base_score":2.1972245773362196,"endowment":2.1972245773362196,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26345091","pmcid":null,"openalex_id":"https://openalex.org/W1654650032","authors":[],"funders":[],"total_grants":0,"fwci":0.1455,"citation_percentile":0.48450838,"influential_citations":0,"citation_trend":[{"year":2018,"count":1},{"year":2019,"count":3},{"year":2020,"count":1},{"year":2021,"count":2},{"year":2022,"count":1}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.18388/abp.2014_953","host_type":"journal"},{"url":"https://doi.org/10.18388/abp.2014_953","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/26345091","host_type":"repository"},{"url":"https://hdl.handle.net/11511/42379","host_type":"repository"}],"fields_of_study":["Aldose Reductase and Taurine","Prenatal Substance Exposure Effects","Cannabis and Cannabinoid Research","Acetic Acid","Aldehyde Reductase","Animals","Binding Sites","Diabetes Mellitus","Enzyme Inhibitors","Humans","Indoleacetic Acids","Indoles","Inhibitory Concentration 50","Kidney","Lens, Crystalline","Ligands","Luciferases","Male","Molecular Conformation","PPAR gamma","Protein Binding","Rats","Rats, Wistar","Thiazoles"],"mesh_terms":["Aldehyde Reductase","Animals","Binding Sites","Diabetes Mellitus","Enzyme Inhibitors","Humans","Indoleacetic Acids","Indoles","Kidney","Lens, Crystalline","Ligands","Luciferases","Male","Molecular Conformation","Protein Binding","Thiazoles","Rats, Wistar","Acetic Acid","Inhibitory Concentration 50","PPAR gamma","Rats"],"keywords":["Aldose reductase","Aldehyde Reductase","Chemistry","Aldo-keto reductase","Ligand (biochemistry)","Sorbitol","Biochemistry","Enzyme","Aldose reductase inhibitor","Reductase","IC50","Docking (animal)","Aldose","Stereochemistry","Sorbinil","In vitro","Receptor"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-18T21:06:36.125200Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}