{"doi":"10.1073/pnas.91.22.10655","title":"The LIM/double zinc-finger motif functions as a protein dimerization domain.","abstract":"<jats:p>Protein-protein interactions resulting in dimerization and heterodimerization are of central importance in the control of gene expression and cell function. Proteins that share the 52-residue LIM/double zinc-finger domain are involved in a wide range of developmental and cellular controls. Some of these functions have been hypothesized to involve protein dimerization. In the present report we demonstrate, using both in vitro and cell-based studies, that a representative LIM protein, human cysteine-rich protein (hCRP), can efficiently homodimerize. The dimerization ability of hCRP is mapped to the LIM domains, can be transferred to an unrelated protein by fusion of a single minimal LIM/double zinc-finger segment, occurs in the absence as well as the presence of DNA, and appears to depend on coordination of two zinc atoms in the finger doublet. These observations support a specific role for protein dimerization in the function of proteins containing the LIM/double zinc-finger domain and expand the general spectrum of potential interactions mediated by zinc-finger motifs.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1994,"id":31215,"datarank":13.145474402001113,"base_score":5.2832037287379885,"endowment":5.2832037287379885,"self_citation_contribution":0.7924805593106984,"citation_network_contribution":12.352993842690415,"self_endowment_contribution":0.7924805593106984,"citer_contribution":12.352993842690415,"corpus_percentile":null,"corpus_rank":null,"citation_count":196,"citer_count":195,"citers_with_citation_signal":177,"citers_with_endowment":177,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":167783,"name":"X Wang","orcid":null,"position":1,"is_corresponding":false},{"id":167784,"name":"D Song","orcid":null,"position":2,"is_corresponding":false},{"id":167785,"name":"N E Cooke","orcid":null,"position":3,"is_corresponding":false},{"id":167786,"name":"S A Liebhaber","orcid":null,"position":4,"is_corresponding":false},{"id":167782,"name":"R Feuerstein","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":5.2832037287379885,"endowment":5.2832037287379885,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"7938009","pmcid":"PMC45080","openalex_id":"https://openalex.org/W2032881439","authors":[],"funders":[],"total_grants":0,"fwci":13.3096,"citation_percentile":0.9927845,"influential_citations":6,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":7},{"year":2014,"count":5},{"year":2015,"count":2},{"year":2016,"count":4},{"year":2017,"count":2},{"year":2018,"count":2},{"year":2019,"count":3},{"year":2020,"count":5},{"year":2021,"count":5},{"year":2022,"count":1},{"year":2023,"count":3},{"year":2025,"count":4}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC45080","host_type":"GREEN"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.91.22.10655","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.91.22.10655","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/7938009","host_type":"repository"},{"url":"http://europepmc.org/pmc/articles/PMC45080","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/45080","host_type":"repository"}],"fields_of_study":["Cardiomyopathy and Myosin Studies","Cancer-related gene regulation","Neurogenetic and Muscular Disorders Research","Biology","Medicine","Amino Acid Sequence","Antibodies","Cloning, Molecular","DNA-Binding Proteins","Glutathione Transferase","Humans","Macromolecular Substances","Molecular Sequence Data","Mutagenesis, Site-Directed","Nuclear Proteins","Protein Conformation","Protein Multimerization","Proteins","Proto-Oncogene Proteins c-myc","Recombinant Fusion Proteins","TATA Box","Transcriptional Activation","Zinc Fingers"],"mesh_terms":["Amino Acid Sequence","Antibodies","Cloning, Molecular","DNA-Binding Proteins","Glutathione Transferase","Humans","Molecular Sequence Data","Nuclear Proteins","Protein Conformation","Proteins","Recombinant Fusion Proteins","Transcriptional Activation","Proto-Oncogene Proteins c-myc","Mutagenesis, Site-Directed","Zinc Fingers","TATA Box","Macromolecular Substances","Protein Multimerization"],"keywords":["Zinc finger","LIM domain","RING finger domain","PHD finger","Zinc","Fusion protein","Chemistry","Cysteine","Ring finger","Cell biology","Zinc finger nuclease","Gene","Biology","Biochemistry","Recombinant DNA","Enzyme"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-09T06:43:07.168979Z","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,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}