{"doi":"10.1073/pnas.88.22.10312","title":"Nuclear matrins: identification of the major nuclear matrix proteins.","abstract":"<jats:p>A preparative two-dimensional polyacrylamide gel system was used to separate and purify the major Coomassie blue-stained proteins from the isolated rat liver nuclear matrix. Approximately 12 major proteins were consistently found. Of these, 5 proteins represented identified proteins, including nuclear lamins A, B, and C, the nucleolar protein B-23, and residual components of core heterogeneous nuclear ribonucleoproteins. The remaining eight major proteins termed the nuclear matrins consisted of matrin 3 (125 kDa, slightly acidic), matrin 4 (105 kDa, basic), matrins D-G (60-75 kDa, basic), and matrins 12 and 13 (42-48 kDa, acidic). Peptide mapping and two-dimensional immunoblot studies indicate that matrins D-G compose two pairs of related proteins (matrins D/E and F/G) and that none of the matrins resemble the nuclear lamins or any of the other major proteins detected on our two-dimensional gels. Subfractionation immunoblot experiments demonstrated the nearly exclusive localization of matrins F/G and other matrins to the nuclear matrix fraction of the cell. These results were further supported by indirect immunofluorescence microscopy that showed a strictly interior nuclear localization of the matrins in intact cells in contrast to the peripherally located nuclear lamins. We conclude that the nuclear matrins are a major class of proteins of the nuclear matrix interior and are distinct from the nuclear lamins.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1991,"id":603761,"datarank":0.7878410142069946,"base_score":5.25227342804663,"endowment":5.25227342804663,"self_citation_contribution":0.7878410142069946,"citation_network_contribution":0.0,"self_endowment_contribution":0.7878410142069946,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":190,"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":1548861,"name":"R Berezney","orcid":null,"position":1,"is_corresponding":false},{"id":1548860,"name":"H Nakayasu","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Nuclear matrins: identification of the major nuclear matrix proteins.","abstract":"<jats:p>A preparative two-dimensional polyacrylamide gel system was used to separate and purify the major Coomassie blue-stained proteins from the isolated rat liver nuclear matrix. Approximately 12 major proteins were consistently found. Of these, 5 proteins represented identified proteins, including nuclear lamins A, B, and C, the nucleolar protein B-23, and residual components of core heterogeneous nuclear ribonucleoproteins. The remaining eight major proteins termed the nuclear matrins consisted of matrin 3 (125 kDa, slightly acidic), matrin 4 (105 kDa, basic), matrins D-G (60-75 kDa, basic), and matrins 12 and 13 (42-48 kDa, acidic). Peptide mapping and two-dimensional immunoblot studies indicate that matrins D-G compose two pairs of related proteins (matrins D/E and F/G) and that none of the matrins resemble the nuclear lamins or any of the other major proteins detected on our two-dimensional gels. Subfractionation immunoblot experiments demonstrated the nearly exclusive localization of matrins F/G and other matrins to the nuclear matrix fraction of the cell. These results were further supported by indirect immunofluorescence microscopy that showed a strictly interior nuclear localization of the matrins in intact cells in contrast to the peripherally located nuclear lamins. We conclude that the nuclear matrins are a major class of proteins of the nuclear matrix interior and are distinct from the nuclear lamins.</jats:p>","is_dataset_classified":null,"base_score":5.25227342804663,"endowment":5.25227342804663,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"1946450","pmcid":"PMC52918","openalex_id":"https://openalex.org/W2085351745","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM-23922","title":null}],"total_grants":1,"fwci":3.4373,"citation_percentile":0.93506538,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":3},{"year":2014,"count":6},{"year":2015,"count":4},{"year":2016,"count":4},{"year":2017,"count":4},{"year":2018,"count":3},{"year":2019,"count":3},{"year":2020,"count":8},{"year":2021,"count":8},{"year":2022,"count":4},{"year":2023,"count":7},{"year":2024,"count":9},{"year":2025,"count":3}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://pnas.org/doi/pdf/10.1073/pnas.88.22.10312","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.88.22.10312","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/1946450","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/52918","host_type":"repository"}],"fields_of_study":["Nuclear Structure and Function","Ubiquitin and proteasome pathways","Animal Genetics and Reproduction","Animals","Antibodies","Antigens, Nuclear","Blotting, Western","Cell Nucleus","Electrophoresis, Gel, Two-Dimensional","Fluorescent Antibody Technique","Liver","Molecular Weight","Nuclear Matrix","Nuclear Proteins","Peptide Mapping","Rats"],"mesh_terms":["Animals","Antibodies","Cell Nucleus","Fluorescent Antibody Technique","Liver","Molecular Weight","Nuclear Proteins","Peptide Mapping","Blotting, Western","Electrophoresis, Gel, Two-Dimensional","Nuclear Matrix","Antigens, Nuclear","Rats"],"keywords":["Nuclear matrix","Lamin","Nuclear lamina","Nuclear protein","Cell nucleus","Molecular biology","Biology","Ribonucleoprotein","Biochemistry","Chemistry","Chromatin","Cytoplasm","Gene","RNA","Transcription factor"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-29T22:39:26.065299Z","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":[]}