{"doi":"10.1002/0470093765.ch5","title":"Nuclear Membrane Protein Emerin: Roles in Gene Regulation, Actin Dynamics and Human Disease","abstract":null,"journal":"Novartis Foundation Symposia","year":2005,"id":670924,"datarank":1.4251935880812474,"base_score":3.4011973816621555,"endowment":3.4011973816621555,"self_citation_contribution":0.5101796072493234,"citation_network_contribution":0.915013980831924,"self_endowment_contribution":0.5101796072493234,"citer_contribution":0.915013980831924,"corpus_percentile":null,"corpus_rank":null,"citation_count":29,"citer_count":27,"citers_with_citation_signal":26,"citers_with_endowment":26,"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":441242,"name":"James M. Holaska","orcid":"0000-0003-0273-9995","position":1,"is_corresponding":false},{"id":1752657,"name":"Rocio Montes de Oca","orcid":null,"position":2,"is_corresponding":false},{"id":1752658,"name":"Kathryn Tifft","orcid":null,"position":3,"is_corresponding":false},{"id":1752659,"name":"Michael Zastrow","orcid":null,"position":4,"is_corresponding":false},{"id":1752660,"name":"Miriam Segura‐Totten","orcid":null,"position":5,"is_corresponding":false},{"id":1596484,"name":"Malini Mansharamani","orcid":null,"position":6,"is_corresponding":false},{"id":1752661,"name":"Luiza Bengtsson","orcid":null,"position":7,"is_corresponding":false},{"id":731118,"name":"Katherine L. Wilson","orcid":"0000-0003-1402-4735","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Nuclear Membrane Protein Emerin: Roles in Gene Regulation, Actin Dynamics and Human Disease","abstract":"Loss of emerin, a nuclear membrane protein, causes Emery-Dreifuss muscular dystrophy (EDMD), characterized by muscle weakening, contractures of major tendons and potentially lethal cardiac conduction system defects. Emerin has a LEM-domain and therefore binds barrier-to-autointegration factor (BAF), a conserved chromatin protein essential for cell division. BAF recruits emerin to chromatin and regulates higher-order chromatin structure during nuclear assembly. Emerin also binds filaments formed by A-type lamins, mutations in which also cause EDMD. Other partners for emerin include nesprin-1alpha and transcriptional regulators such as germ cell-less (GCL). The binding affinities of these partners range from 4nM (nesprin-1alpha) to 200 nM (BAF), and are physiologically significant. Biochemical studies therefore provide a valid means to predict the properties of emerin-lamin complexes in vivo. Emerin and lamin A together form stable complexes with either BAF or GCL in vitro. BAF, however, competes with GCL for binding to emerin in vitro. These and additional partners, notably actin and nuclear myosin II, suggest disease-relevant roles for emerin in gene regulation and the mechanical interity of the nucleus.","is_dataset_classified":null,"base_score":3.4011973816621555,"endowment":3.4011973816621555,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"15773747","pmcid":null,"openalex_id":"https://openalex.org/W1606897310","authors":[],"funders":[{"funder_name":"NHLBI NIH HHS","grant_id":"T32 HL07227","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"F32 GM067397","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM48646","title":null}],"total_grants":3,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":1},{"year":2014,"count":3},{"year":2018,"count":2},{"year":2019,"count":2},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2023,"count":1}],"oa_status":"closed","license":"http://doi.wiley.com/10.1002/tdm_license_1.1","oa_locations":[{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2F0470093765.ch5","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/0470093765.ch5","host_type":"publisher"},{"url":"https://doi.org/10.1002/0470093765.ch5","host_type":"book series"},{"url":"https://pubmed.ncbi.nlm.nih.gov/15773747","host_type":"repository"}],"fields_of_study":["Nuclear Structure and Function","RNA Research and Splicing","Genomics and Chromatin Dynamics"],"mesh_terms":["Actins","Animals","Gene Expression Regulation","Humans","Membrane Proteins","Muscular Dystrophies","Nuclear Envelope","Nuclear Proteins","Thymopoietins"],"keywords":["Emerin","Lamin","Inner membrane","Cell biology","Biology","Chromatin","Nuclear protein","Nuclear lamina","Nuclear membrane","Actin","Molecular biology","Genetics","Gene","Transcription factor","Cytoplasm","Nucleus","Mitochondrion"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Good health and well-being"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T00:35:34.672750Z","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":[]}