{"doi":"10.1007/bf00225883","title":"Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain","abstract":null,"journal":"Molecular and Cellular Biochemistry","year":1996,"id":635171,"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":438424,"name":"W. Todd Miller","orcid":"0000-0002-6566-0064","position":1,"is_corresponding":false},{"id":384653,"name":"Bin Xu","orcid":"0000-0002-1294-4506","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain","abstract":"To examine the interactions between Src homology domains and the tyrosine kinase catalytic domain of v-Src, various combinations of domains have been expressed in bacteria as fusion proteins. Constructs containing the isolated catalytic domain, SH2 + catalytic domain, and SH3 + SH2 + catalytic domains were active in autophosphorylation assays. For the catalytic domain of v-Src, but not for v-Abl, addition of exogenous Src SH3-SH2 domains stimulated the autophosphorylation activity. In contrast to results for autophosphorylation, constructs containing Src homology domains were more active towards a synthetic peptide substrate than the isolated catalytic domain. The ability of the SH2 and SH3 domains of v-Src to stabilize an active enzyme conformation was also confirmed by refolding after denaturation in guanidinium hydrochloride. Collectively the data suggest that, in addition to their roles in intermolecular protein-protein interactions, the Src homology regions of v-Src exert a positive influence on tyrosine kinase function, potentially by maintaining an active conformation of the catalytic domain.","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":"8791285","pmcid":null,"openalex_id":"https://openalex.org/W1975637940","authors":[],"funders":[{"funder_name":"NCI NIH HHS","grant_id":"CA58530","title":null}],"total_grants":1,"fwci":0.2656,"citation_percentile":0.50691148,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":1},{"year":2015,"count":1},{"year":2017,"count":1}],"oa_status":"closed","license":"https://www.springer.com/tdm","oa_locations":[{"url":"https://link.springer.com/content/pdf/10.1007/BF00225883.pdf","host_type":"publisher"},{"url":"https://link.springer.com/article/10.1007/BF00225883/fulltext.html","host_type":"publisher"},{"url":"http://link.springer.com/content/pdf/10.1007/BF00225883","host_type":"publisher"},{"url":"https://doi.org/10.1007/bf00225883","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/8791285","host_type":"repository"}],"fields_of_study":["Biochemical and Molecular Research","Monoclonal and Polyclonal Antibodies Research","Enzyme Structure and Function","Adenosine Triphosphate","Amino Acid Sequence","Escherichia coli","Glutathione Transferase","Molecular Sequence Data","Oncogene Protein pp60(v-src)","Oncogene Proteins v-abl","Peptides","Phosphorylation","Protein Conformation","Protein Folding","Protein-Tyrosine Kinases","Recombinant Fusion Proteins","src Homology Domains"],"mesh_terms":["Adenosine Triphosphate","Amino Acid Sequence","Escherichia coli","Glutathione Transferase","Molecular Sequence Data","Peptides","Phosphorylation","Protein Conformation","Protein-Tyrosine Kinases","Recombinant Fusion Proteins","Oncogene Protein pp60(v-src)","Oncogene Proteins v-abl","Protein Folding","src Homology Domains"],"keywords":["Autophosphorylation","Proto-oncogene tyrosine-protein kinase Src","SH2 domain","SH3 domain","Phosphotyrosine-binding domain","Tyrosine kinase","Chemistry","Biochemistry","Protein kinase domain","GRB2","Kinase","Protein kinase A","Signal transduction","Mutant"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Clean water and sanitation"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-06T14:44:52.961886Z","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":[]}