{"doi":"10.1021/bi301648q","title":"Unique Proline-Rich Domain Regulates the Chaperone Function of AIPL1","abstract":null,"journal":"Biochemistry","year":2013,"id":656482,"datarank":0.4566783656585135,"base_score":3.044522437723423,"endowment":3.044522437723423,"self_citation_contribution":0.4566783656585135,"citation_network_contribution":0.0,"self_endowment_contribution":0.4566783656585135,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":20,"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":1713695,"name":"Gabriel Zoldak","orcid":null,"position":1,"is_corresponding":false},{"id":1713696,"name":"Thomas Kriehuber","orcid":null,"position":2,"is_corresponding":false},{"id":142403,"name":"Joanna Soroka","orcid":null,"position":3,"is_corresponding":false},{"id":1713697,"name":"Franz X. Schmid","orcid":null,"position":4,"is_corresponding":false},{"id":142566,"name":"Klaus Richter","orcid":null,"position":5,"is_corresponding":false},{"id":141322,"name":"Johannes Buchner","orcid":"0000-0003-1282-7737","position":6,"is_corresponding":false},{"id":1346179,"name":"Jing Li","orcid":"0000-0003-3209-8973","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Unique Proline-Rich Domain Regulates the Chaperone Function of AIPL1","abstract":"Human aryl hydrocarbon receptor (AHR) interacting protein (AIP) and AIP like 1 (AIPL1) are cochaperones of Hsp90 which share 49% sequence identity. Both proteins contain an N-terminal FKBP-like prolyl peptidyl isomerase (PPIase) domain followed by a tetratricopeptide repeat (TPR) domain. In addition, AIPL1 harbors a unique C-terminal proline-rich domain (PRD). Little is known about the functional relevance of the individual domains and how these contribute to the association with Hsp90. In this study, we show that these cochaperones differ from other Hsp90-associated PPIase as their FKBP domains are enzymatically inactive. Furthermore, in contrast to other large PPIases, AIP is inactive as a chaperone. AIPL1, however, exhibits chaperone activity and prevents the aggregation of non-native proteins. The unique proline-rich domain of AIPL1 is important for its chaperone function as its truncation severely affects the ability of AIPL1 to bind non-native proteins. Furthermore, the proline-rich domain decreased the affinity of AIPL1 for Hsp90, implying that this domain acts as a negative regulator of the Hsp90 interaction besides being necessary for efficient binding of AIPL1 to non-native proteins.","is_dataset_classified":null,"base_score":3.044522437723423,"endowment":3.044522437723423,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23418749","pmcid":null,"openalex_id":"https://openalex.org/W1983832983","authors":[],"funders":[],"total_grants":0,"fwci":1.6224,"citation_percentile":0.82677708,"influential_citations":0,"citation_trend":[{"year":2013,"count":3},{"year":2014,"count":4},{"year":2015,"count":3},{"year":2016,"count":1},{"year":2017,"count":4},{"year":2018,"count":1},{"year":2020,"count":1},{"year":2022,"count":2},{"year":2024,"count":1}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://pubs.acs.org/doi/pdf/10.1021/bi301648q","host_type":"publisher"},{"url":"https://doi.org/10.1021/bi301648q","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23418749","host_type":"repository"},{"url":"https://eref.uni-bayreuth.de/10539/","host_type":"repository"}],"fields_of_study":["Heat shock proteins research","Toxin Mechanisms and Immunotoxins","Signaling Pathways in Disease","Adaptor Proteins, Signal Transducing","Amino Acid Sequence","Carrier Proteins","Circular Dichroism","Eye Proteins","HSP90 Heat-Shock Proteins","Humans","Intracellular Signaling Peptides and Proteins","Molecular Chaperones","Molecular Sequence Data","Peptidylprolyl Isomerase","Proline","Protein Interaction Domains and Motifs","Protein Stability","Sequence Homology, Amino Acid","Structural Homology, Protein","Surface Plasmon Resonance","Tacrolimus Binding Proteins"],"mesh_terms":["Amino Acid Sequence","Carrier Proteins","Circular Dichroism","Eye Proteins","Humans","Molecular Sequence Data","Proline","Sequence Homology, Amino Acid","Molecular Chaperones","HSP90 Heat-Shock Proteins","Peptidylprolyl Isomerase","Surface Plasmon Resonance","Tacrolimus Binding Proteins","Structural Homology, Protein","Intracellular Signaling Peptides and Proteins","Adaptor Proteins, Signal Transducing","Protein Interaction Domains and Motifs","Protein Stability"],"keywords":["Tetratricopeptide","FKBP","Chaperone (clinical)","WW domain","Hsp90","CDC37","Cell biology","Regulator","Biology","Proline","Peptidylprolyl isomerase","Plasma protein binding","Isomerase","Biochemistry","Chemistry","Amino acid","Heat shock protein","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-11T21:03:35.133357Z","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":[]}