{"doi":"10.1016/j.bbrc.2011.10.056","title":"Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain","abstract":null,"journal":"Biochemical and Biophysical Research Communications","year":2011,"id":659432,"datarank":0.5742962094733643,"base_score":3.828641396489095,"endowment":3.828641396489095,"self_citation_contribution":0.5742962094733643,"citation_network_contribution":0.0,"self_endowment_contribution":0.5742962094733643,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":45,"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":1721389,"name":"Ahmad Trad","orcid":null,"position":1,"is_corresponding":false},{"id":740535,"name":"Joachim Grötzinger","orcid":null,"position":2,"is_corresponding":false},{"id":1721387,"name":"Inken Lorenzen","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain","abstract":"A disintegrin and metalloprotease protein 17 (ADAM17) is a transmembrane zinc dependent metalloprotease. The catalytic activity of the enzyme results in the shedding of a broad range of membrane proteins. The release of the corresponding ectodomains induces a switch in various physiological and pathophysiological processes. So far there is not much information about the molecular mechanism of ADAM17 activation available. As for other transmembrane proteases, multimerisation may play a critical role in the activation and function of ADAM17. The present work demonstrates that ADAM17 indeed exists as a multimer in the cell membrane and that this multimerisation is mediated by its EGF-like domain.","is_dataset_classified":null,"base_score":3.828641396489095,"endowment":3.828641396489095,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22033402","pmcid":null,"openalex_id":"https://openalex.org/W2060063240","authors":[],"funders":[{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"unidentified","title":"unidentified"},{"funder_name":"Excellence Cluster ‘Inflammation at Interfaces’","grant_id":"","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"","title":null}],"total_grants":3,"fwci":2.7311,"citation_percentile":0.91521492,"influential_citations":0,"citation_trend":[{"year":2012,"count":8},{"year":2013,"count":9},{"year":2014,"count":4},{"year":2015,"count":8},{"year":2016,"count":2},{"year":2017,"count":3},{"year":2018,"count":3},{"year":2019,"count":1},{"year":2020,"count":3},{"year":2021,"count":3},{"year":2023,"count":1}],"oa_status":"closed","license":"Elsevier TDM","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0006291X11018535?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0006291X11018535?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.bbrc.2011.10.056","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22033402","host_type":"repository"},{"url":"https://dx.doi.org/10.1016/j.bbrc.2011.10.056","host_type":""}],"fields_of_study":["HER2/EGFR in Cancer Research","Cell Adhesion Molecules Research","Biochemical and Structural Characterization","0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":["ADAM17 Protein","Animals","Cell Membrane","Epidermal Growth Factor","Humans","Protein Structure, Tertiary","Immunoprecipitation","Mice","ADAM Proteins","Protein Multimerization","HEK293 Cells"],"keywords":["Disintegrin","Metalloproteinase","Proteases","Transmembrane protein","Cell biology","Transmembrane domain","Chemistry","Function (biology)","Enzyme","Receptor","Biochemistry","Biology","Epidermal Growth Factor","Cell Membrane","ADAM17 Protein","Protein Structure, Tertiary","ADAM Proteins","Mice","HEK293 Cells","Animals","Humans","Immunoprecipitation","Protein Multimerization"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T06:53:19.598304Z","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":[]}