{"doi":"10.1016/j.bbrc.2007.12.072","title":"Peptidyl-prolyl-tRNA at the ribosomal P-site reacts poorly with puromycin","abstract":null,"journal":"Biochemical and Biophysical Research Communications","year":2008,"id":684693,"datarank":0.6414999178524083,"base_score":4.276666119016055,"endowment":4.276666119016055,"self_citation_contribution":0.6414999178524083,"citation_network_contribution":0.0,"self_endowment_contribution":0.6414999178524083,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":71,"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":1788817,"name":"Koreaki Ito","orcid":null,"position":1,"is_corresponding":false},{"id":1788816,"name":"Hiroki Muto","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Peptidyl-prolyl-tRNA at the ribosomal P-site reacts poorly with puromycin","abstract":"Despite remarkable recent progress in our chemical and structural understanding of the mechanisms of peptide bond formation by the ribosome, only very limited information is available about whether amino acid side chains affect the rate of peptide bond formation. Here, we generated a series of peptidyl-tRNAs that end with different tRNA-attached amino acids in the P-site of the Escherichia coli ribosome and compared their reactivity with puromycin, a rapidly A-site-accessing analog of aminoacyl-tRNAs. Among the 20 amino acids examined, proline was found to receive exceptionally slow peptidyl transfer to puromycin. These results raise a possibility that the peptidyl transferase activity of the ribosome may have some specificity with regard to the P-site amino acids.","is_dataset_classified":null,"base_score":4.276666119016055,"endowment":4.276666119016055,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"18155161","pmcid":null,"openalex_id":"https://openalex.org/W2058464545","authors":[],"funders":[{"funder_name":"Japan Science and Technology Agency","grant_id":"","title":null},{"funder_name":"Ministry of Education, Culture, Sports, Science and Technology","grant_id":"","title":null},{"funder_name":"Core Research for Evolutional Science and Technology","grant_id":"","title":null}],"total_grants":3,"fwci":1.528,"citation_percentile":0.81763164,"influential_citations":0,"citation_trend":[{"year":2012,"count":3},{"year":2013,"count":6},{"year":2014,"count":10},{"year":2015,"count":5},{"year":2016,"count":7},{"year":2017,"count":4},{"year":2018,"count":1},{"year":2019,"count":3},{"year":2020,"count":2},{"year":2021,"count":2},{"year":2022,"count":4},{"year":2023,"count":7},{"year":2024,"count":4},{"year":2026,"count":2}],"oa_status":"closed","license":"https://www.elsevier.com/legal/tdmrep-license","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0006291X07027027?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0006291X07027027?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.bbrc.2007.12.072","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/18155161","host_type":"repository"}],"fields_of_study":["RNA and protein synthesis mechanisms","RNA modifications and cancer","Peptidase Inhibition and Analysis"],"mesh_terms":["Bacterial Outer Membrane Proteins","Escherichia coli","Nucleic Acid Hybridization","Proline","Puromycin","Ribosomes","RNA, Transfer, Amino Acyl","Amino Acid Substitution","Escherichia coli Proteins","Mutant Proteins"],"keywords":["Puromycin","Peptidyl transferase","Ribosome","Peptide bond","Amino acid","Transfer RNA","Ribosomal RNA","P-site","Aminoacyl-tRNA","Chemistry","Biochemistry","Translation (biology)","A-site","Peptide","Stereochemistry","Biology","Protein biosynthesis","Binding site","RNA"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-18T14:46:28.404699Z","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":[]}