{"doi":"10.1016/j.jmgm.2014.11.012","title":"Cloning and molecular modeling of a thermostable carboxylesterase from the chicken uropygial glands","abstract":null,"journal":"Journal of Molecular Graphics and Modelling","year":2015,"id":660036,"datarank":0.24141568686511508,"base_score":1.6094379124341003,"endowment":1.6094379124341003,"self_citation_contribution":0.24141568686511508,"citation_network_contribution":0.0,"self_endowment_contribution":0.24141568686511508,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":4,"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":1722971,"name":"Fakher Frikha","orcid":null,"position":1,"is_corresponding":false},{"id":1722972,"name":"Hanen Louati","orcid":null,"position":2,"is_corresponding":false},{"id":1722973,"name":"Madiha Bou Ali","orcid":null,"position":3,"is_corresponding":false},{"id":1722974,"name":"Hela Gargouri","orcid":null,"position":4,"is_corresponding":false},{"id":1722975,"name":"Youssef Gargouri","orcid":null,"position":5,"is_corresponding":false},{"id":1722976,"name":"Nabil Miled","orcid":null,"position":6,"is_corresponding":false},{"id":1722970,"name":"Ahmed Fendri","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Cloning and molecular modeling of a thermostable carboxylesterase from the chicken uropygial glands","abstract":"Starting from total uropygial glands mRNAs, chicken uropygial carboxylesterase (cuCES) cDNA was synthesized by RT-PCR and cloned into the PGEM-T vector. Amino acid sequence of the cuCES is compared to that of human liver carboxylesterase 1 (hCES1). Given the high amino acid sequence homology between the two enzymes, a 3-D structure model of the chicken carboxylesterase was built using the structure of hCES1 as template. By following this model and utilizing molecular dynamics (MD) simulations, the resistance of the chicken carboxylesterase at high temperatures could be explained. The docking of substrate analogs into the cuCES active site was used to explain the fact that the chicken carboxylesterase cannot hydrolyze efficiently large substrate molecules.","is_dataset_classified":null,"base_score":1.6094379124341003,"endowment":1.6094379124341003,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"25541525","pmcid":null,"openalex_id":"https://openalex.org/W1970014848","authors":[],"funders":[{"funder_name":"Tunisian Ministry of Higher Education and Scientific Research","grant_id":"","title":null}],"total_grants":1,"fwci":0.3899,"citation_percentile":0.59107555,"influential_citations":0,"citation_trend":[{"year":2015,"count":1},{"year":2017,"count":2},{"year":2019,"count":1}],"oa_status":"closed","license":"https://www.elsevier.com/legal/tdmrep-license","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S1093326314002009?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1093326314002009?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.jmgm.2014.11.012","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/25541525","host_type":"repository"}],"fields_of_study":["Enzyme Catalysis and Immobilization","Protein Hydrolysis and Bioactive Peptides","Cholinesterase and Neurodegenerative Diseases","Amino Acid Sequence","Animals","Avian Proteins","Base Sequence","Carboxylesterase","Catalytic Domain","Chickens","Cloning, Molecular","Enzyme Stability","Escherichia coli","Hot Temperature","Humans","Isoenzymes","Kinetics","Liver","Molecular Docking Simulation","Molecular Dynamics Simulation","Molecular Sequence Data","Perianal Glands","Recombinant Proteins","Sequence Alignment","Sequence Homology, Amino Acid","Substrate Specificity"],"mesh_terms":["Amino Acid Sequence","Animals","Base Sequence","Chickens","Cloning, Molecular","Enzyme Stability","Escherichia coli","Hot Temperature","Humans","Isoenzymes","Kinetics","Liver","Molecular Sequence Data","Perianal Glands","Recombinant Proteins","Substrate Specificity","Sequence Alignment","Sequence Homology, Amino Acid","Catalytic Domain","Avian Proteins","Carboxylesterase","Molecular Dynamics Simulation","Molecular Docking Simulation"],"keywords":["Carboxylesterase","Complementary DNA","Homology modeling","Molecular cloning","Biology","Biochemistry","Peptide sequence","Enzyme","Amino acid","Molecular biology","Cloning (programming)","Chemistry","Gene","Thermostability","Nucleotide sequencing","Docking","3D Structure Modeling","Molecular Dynamic","Chicken Uropygial Carboxylesterase"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T08:15:50.915586Z","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":[]}