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Rev."},{"key":"10.1016\/j.tibs.2021.05.007_bb0410","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1038\/nm1266","article-title":"Genomic instability in laminopathy-based premature aging","volume":"11","author":"Liu","year":"2005","journal-title":"Nat. Med."},{"key":"10.1016\/j.tibs.2021.05.007_bb0415","first-page":"147","article-title":"Lamins are rapamycin targets that impact human longevity: a study in centenarians","volume":"127","author":"Lattanzi","year":"2014","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.tibs.2021.05.007_bb0420","first-page":"1","article-title":"Nuclear accumulation of UBC9 contributes to SUMOylation of lamin A\/C and nucleophagy in response to DNA damage","volume":"38","author":"Li","year":"2019","journal-title":"J. Exp. Clin. 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Chem."},{"key":"10.1016\/j.tibs.2021.05.007_bb0440","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1038\/s41467-018-05808-y","article-title":"Nuclear Nestin deficiency drives tumor senescence via lamin A\/C-dependent nuclear deformation","volume":"9","author":"Zhang","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2021.05.007_bb0445","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1016\/j.bbamcr.2018.05.008","article-title":"E3 ubiquitin ligase HECW2 targets PCNA and lamin B1","volume":"1865","author":"Krishnamoorthy","year":"2018","journal-title":"Biochim. Biophys. Acta Mol. 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Virol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0470","doi-asserted-by":"crossref","first-page":"11913","DOI":"10.1128\/JVI.01100-08","article-title":"Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production","volume":"82","author":"Lee","year":"2008","journal-title":"J. Virol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0475","doi-asserted-by":"crossref","first-page":"4524","DOI":"10.1128\/JVI.02456-09","article-title":"Simian Virus 40 T\/t antigens and lamin A\/C small interfering RNA rescue the phenotype of an Epstein-Barr Virus protein kinase (BGLF4) mutant","volume":"84","author":"Meng","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0480","doi-asserted-by":"crossref","first-page":"13979","DOI":"10.1074\/jbc.M109.063628","article-title":"Novel mode of phosphorylation-triggered reorganization of the nuclear lamina during nuclear egress of human cytomegalovirus","volume":"285","author":"Milbradt","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2021.05.007_bb0485","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.ppat.1005825","article-title":"The prolyl isomerase Pin1 promotes the herpesvirus-induced phosphorylation-dependent disassembly of the nuclear lamina required for nucleocytoplasmic egress","volume":"12","author":"Milbradt","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.tibs.2021.05.007_bb0490","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.virol.2009.06.051","article-title":"Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins","volume":"392","author":"Cano-Monreal","year":"2009","journal-title":"Virology"},{"key":"10.1016\/j.tibs.2021.05.007_bb0495","first-page":"1","article-title":"Baculovirus infection induces disruption of the nuclear lamina","volume":"7","author":"Zhang","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.tibs.2021.05.007_bb0500","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/JVI.00979-19","article-title":"Cellular p32 is a critical regulator of porcine circovirus type 2 nuclear egress","volume":"93","author":"Wang","year":"2019","journal-title":"J. Virol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0505","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1016\/j.cell.2012.03.032","article-title":"Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling","volume":"149","author":"Speese","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.tibs.2021.05.007_bb0510","series-title":"New Concepts of Antiviral Therapy","first-page":"309","article-title":"Maribavir: a promising new antiherpes therapeutic agent","author":"Biron","year":"2006"},{"key":"10.1016\/j.tibs.2021.05.007_bb0515","doi-asserted-by":"crossref","first-page":"515","DOI":"10.3390\/microorganisms8040515","article-title":"The cytomegalovirus protein kinase pUL97: host interactions, regulatory mechanisms and antiviral drug targeting","volume":"8","author":"Steingruber","year":"2020","journal-title":"Microorganisms"},{"key":"10.1016\/j.tibs.2021.05.007_bb0520","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1128\/CDLI.8.6.1279-1281.2001","article-title":"Inhibition of ganciclovir-susceptible and -resistant human cytomegalovirus clinical isolates by the benzimidazole L-riboside 1263W94","volume":"8","author":"McSharry","year":"2001","journal-title":"Clin. Diagn. Lab. Immunol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0525","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1007\/BF01726689","article-title":"Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin","volume":"99","author":"H\u00f6ger","year":"1990","journal-title":"Chromosoma"},{"key":"10.1016\/j.tibs.2021.05.007_bb0530","first-page":"283","article-title":"Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones","volume":"47","author":"H\u00f6ger","year":"1988","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0535","doi-asserted-by":"crossref","first-page":"1392","DOI":"10.1016\/j.jmb.2008.12.024","article-title":"The supramolecular organization of the C. elegans nuclear lamin filament","volume":"386","author":"Ben-Harush","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0540","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1038\/nature21382","article-title":"The molecular architecture of lamins in somatic cells","volume":"543","author":"Turgay","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.tibs.2021.05.007_bb0545","doi-asserted-by":"crossref","first-page":"4307","DOI":"10.1073\/pnas.1810070116","article-title":"Concentric organization of A- and B-type lamins predicts their distinct roles in the spatial organization and stability of the nuclear lamina","volume":"116","author":"Nmezi","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2021.05.007_bb0550","doi-asserted-by":"crossref","first-page":"3409","DOI":"10.1101\/gad.1735208","article-title":"The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription","volume":"22","author":"Shimi","year":"2008","journal-title":"Genes Dev."},{"key":"10.1016\/j.tibs.2021.05.007_bb0555","doi-asserted-by":"crossref","first-page":"4075","DOI":"10.1091\/mbc.E15-07-0461","article-title":"Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy","volume":"26","author":"Shimi","year":"2015","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.tibs.2021.05.007_bb0560","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1083\/jcb.147.5.913","article-title":"Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy","volume":"147","author":"Sullivan","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0565","doi-asserted-by":"crossref","first-page":"10100","DOI":"10.1073\/pnas.1812622115","article-title":"Fibroblasts lacking nuclear lamins do not have nuclear blebs or protrusions but nevertheless have frequent nuclear membrane ruptures","volume":"115","author":"Chen","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2021.05.007_bb0570","doi-asserted-by":"crossref","first-page":"3248","DOI":"10.1073\/pnas.1300215110","article-title":"Mechanical model of blebbing in nuclear lamin meshworks","volume":"110","author":"Funkhouser","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2021.05.007_bb0575","doi-asserted-by":"crossref","first-page":"4683","DOI":"10.1091\/mbc.e11-06-0504","article-title":"Deficiencies in lamin B1 and lamin B2 cause neurodevelopmental defects and distinct nuclear shape abnormalities in neurons","volume":"22","author":"Coffinier","year":"2011","journal-title":"Mol. Biol. 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Chem."},{"key":"10.1016\/j.tibs.2021.05.007_bb0595","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/j.jmb.2004.08.093","article-title":"Crystal structure of the human lamin A coil 2B dimer: Implications for the head-to-tail association of nuclear lamins","volume":"343","author":"Strelkov","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0600","doi-asserted-by":"crossref","first-page":"3757","DOI":"10.1038\/s41467-019-11684-x","article-title":"Structural basis for lamin assembly at the molecular level","volume":"10","author":"Ahn","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2021.05.007_bb0605","doi-asserted-by":"crossref","first-page":"107404","DOI":"10.1016\/j.jsb.2019.10.006","article-title":"Lateral A11 type tetramerization in lamins","volume":"209","author":"Lilina","year":"2020","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0610","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/j.febslet.2012.01.007","article-title":"Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1","volume":"586","author":"Ruan","year":"2012","journal-title":"FEBS Lett."},{"key":"10.1016\/j.tibs.2021.05.007_bb0615","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1093\/abbs\/gmw046","article-title":"Non-homologous end joining: advances and frontiers","volume":"48","author":"Yang","year":"2016","journal-title":"Acta Biochim. Biophys. Sin. Shanghai"},{"key":"10.1016\/j.tibs.2021.05.007_bb0620","doi-asserted-by":"crossref","first-page":"2540","DOI":"10.1242\/jcs.033597","article-title":"Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly","volume":"121","author":"Haraguchi","year":"2008","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.tibs.2021.05.007_bb0625","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1083\/jcb.151.6.1155","article-title":"Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells","volume":"151","author":"Moir","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.tibs.2021.05.007_bb0630","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1016\/j.celrep.2014.07.036","article-title":"Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser\/Thr-based signaling","volume":"8","author":"Sharma","year":"2014","journal-title":"Cell Rep."},{"key":"10.1016\/j.tibs.2021.05.007_bb0635","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.2001497","article-title":"Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells","volume":"4","author":"Kettenbach","year":"2011","journal-title":"Sci. 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