Wilson, K. L. The nuclear envelope, muscular dystrophy and gene expression. Trends Cell Biol.10, 125–129 (2000). CASPubMed Google Scholar
Gerace, L. & Burke, B. Functional organization of the nuclear envelope. Ann. Rev. Cell Biol.4, 335–374 (1988). CASPubMed Google Scholar
Stuurman, N., Heins, S. & Aebi, U. Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol.122, 42–66 (1998). CASPubMed Google Scholar
Gerace, L., Blum, A. & Blobel, G. Immunocytochemical localization of the major polypeptides of the nuclear complex–lamina fraction: interphase and mitotic distribution. J. Cell Biol.79, 546–566 (1978). CASPubMed Google Scholar
Fisher, D. Z., Chaudhary, N. & Blobel, G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl Acad. Sci. USA83, 6450–6454 (1986). CASPubMedPubMed Central Google Scholar
Hoeger, T. H., Krohne, G. & Franke, W. W. Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones. Eur. J. Cell Biol.47, 283–290 (1988). CAS Google Scholar
Hoeger, T. H., Zatloukal, K., Waizenegger, I. & Krohne, G. Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin. Chromosoma99, 379–390 (1990). CAS Google Scholar
Peter, M. et al. Cloning and sequencing of cDNA clones encoding chicken lamins A and B1 and comparison of the primary structures of vertebrate A- and B-type lamins. J. Mol. Biol.208, 393–404 (1989). CASPubMed Google Scholar
Vorburger, K., Lehner, C. F., Kitten, G. T., Eppenberger, H. M. & Nigg, E. A. A second higher vertebrate B-type lamin: cDNA sequence determination and in vitro processing of chicken lamin B2. J. Mol. Biol.208, 405–415 (1989). CASPubMed Google Scholar
Furukawa, K. & Hotta, Y. cDNA cloning of a germ cell-specific lamin B3 from mouse spermatocytes and analysis of its ectopic expression in somatic cells. EMBO J.12, 97–106 (1993). CASPubMedPubMed Central Google Scholar
Rolls, M. M. et al. A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein. J. Cell Biol.146, 29–44 (1999). CASPubMedPubMed Central Google Scholar
Berger, R. et al. The characterization and localization of the mouse thymopoietin/lamina-associated polypeptide 2 gene and its alternatively spliced products. Genome Res.6, 361–370 (1996). CASPubMed Google Scholar
Foisner, R. & Gerace, L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell73, 1267–1279 (1993). CASPubMed Google Scholar
Harris, C. A. et al. Three distinct human thymopoietins are derived from alternatively spliced mRNAs. Proc. Natl Acad. Sci. USA91, 6283–6287 (1994). CASPubMedPubMed Central Google Scholar
Bione, S. et al. Identification of a novel X-linked gene responsible for Emery–Dreifuss muscular dystrophy. Nature Genet.8, 323–327 (1994). CASPubMed Google Scholar
Manilal, S., Nguyen, T. M., Sewry, C. A. & Morris, G. E. The Emery–Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Mol. Genet.5, 801–808 (1996). CASPubMed Google Scholar
Lin, F. et al. MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin. J. Biol. Chem.275, 4840–4847 (2000). CASPubMed Google Scholar
Cai, M. et al. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. EMBO J.20, 4399–4407 (2001). CASPubMedPubMed Central Google Scholar
Wolff, N. et al. Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery–Dreifuss muscular dystrophy. FEBS Lett.501, 171–176 (2001). CASPubMed Google Scholar
Laguri, C. et al. Structural characterization of the LEM motif common to three human inner nuclear membrane proteins. Structure (Camb.)9, 503–511 (2001). CAS Google Scholar
Shumaker, D. K., Lee, K. K., Tanhehco, Y. C., Craigie, R. & Wilson, K. L. LAP2 binds to BAF–DNA complexes: requirement for the LEM domain and modulation by variable regions. EMBO J.20, 1754–1764 (2001). CASPubMedPubMed Central Google Scholar
Zheng, R. et al. Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc. Natl Acad. Sci. USA97, 8997–9002 (2000). CASPubMedPubMed Central Google Scholar
Ye, Q., Callebaut, I., Pezhman, A., Courvalin, J. C. & Worman, H. J. Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. J. Biol. Chem.272, 14983–14989 (1997). CASPubMed Google Scholar
Martins, S. B. et al. HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics. J. Cell Sci.113, 3703–3713 (2000). CASPubMed Google Scholar
Glass, C. A. et al. The α-helical rod domain of human lamins A and C contains a chromatin binding site. EMBO J.12, 4413–4424 (1993). CASPubMedPubMed Central Google Scholar
Ellenberg, J. et al. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol.138, 1193–1206 (1997).This study supports selective retention as a means of localizing INM proteins. CASPubMedPubMed Central Google Scholar
Östlund, C., Ellenberg, J., Hallberg, E., Lippincott-Schwartz, J. & Worman, H. J. Intracellular trafficking of emerin, the Emery–Dreifuss muscular dystrophy protein. J. Cell Sci.112, 1709–1719 (1999). PubMed Google Scholar
Powell, L. & Burke, B. Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina. J. Cell Biol.111, 2225–2234 (1990). CASPubMed Google Scholar
Soullam, B. & Worman, H. J. Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. J. Cell Biol.130, 15–27 (1995).This paper provided early evidence for selective retention as a mechanism for INM protein localization. CASPubMed Google Scholar
Torrisi, M. R. & Bonatti, S. Immunocytochemical study of the partition and distribution of Sindbis virus glycoproteins in freeze-fractured membranes of infected baby hamster kidney cells. J. Cell Biol.101, 1300–1306 (1985). CASPubMed Google Scholar
Torrisi, M. R., Lotti, L. V., Pavan, A., Migliaccio, G. & Bonatti, S. Free diffusion to and from the inner nuclear membrane of newly synthesized plasma membrane glycoproteins. J. Cell Biol.104, 733–737 (1987). CASPubMed Google Scholar
Bergmann, J. E. & Singer, S. J. Immunoelectron microscopic studies of the intracellular transport of the membrane glycoprotein (G) of vesicular stomatitis virus in infected Chinese hamster ovary cells. J. Cell Biol.97, 1777–1787 (1983). CASPubMed Google Scholar
Clements, L., Manilal, S., Love, D. R. & Morris, G. E. Direct interaction between emerin and lamin A. Biochem. Biophys. Res. Commun.267, 709–714 (2000). CASPubMed Google Scholar
Sakaki, M. et al. Interaction between emerin and nuclear lamins. J. Biochem. (Tokyo)129, 321–327 (2001). CAS Google Scholar
Sullivan, T. et al. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J. Cell Biol.147, 913–920 (1999).The development of the first animal model for EDMD and conclusive demonstration of a role for A-type lamins in the maintenance of NE integrityin vivo. CASPubMedPubMed Central Google Scholar
Lee, K. K. et al. Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans. Mol. Biol. Cell13, 892–901 (2002). CASPubMedPubMed Central Google Scholar
Malone, C. J., Fixsen, W. D., Horvitz, H. R. & Han, M. UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development. Development126, 3171–3181 (1999). CASPubMed Google Scholar
Starr, D. A. et al. unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration. Development128, 5039–5050 (2001). CASPubMed Google Scholar
Apel, E. D., Lewis, R. M., Grady, R. M. & Sanes, J. R. Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction. J. Biol. Chem.275, 31986–31995 (2000).Syne-1 and its relatives (Myne-1 and nesprins) might alter our view of molecular interactions at the nuclear periphery. We anticipate some interesting developments as the functions of these proteins are unravelled. CASPubMed Google Scholar
Mislow, J. M., Kim, M. S., Davis, D. B. & McNally, E. M. Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C. J. Cell Sci.115, 61–70 (2002). CASPubMed Google Scholar
Zhang, Q. et al. Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues. J. Cell Sci.114, 4485–4498 (2001). CASPubMed Google Scholar
Bonne, G. et al. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery–Dreifuss muscular dystrophy. Nature Genet.21, 285–288 (1999).This study showed the first link between A-type lamins and muscular dystrophy. CASPubMed Google Scholar
Fatkin, D. et al. Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N. Engl. J. Med.341, 1715–1724 (1999). CASPubMed Google Scholar
Cao, H. & Hegele, R. A. Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy. Hum. Mol. Genet.9, 109–112 (2000). CASPubMed Google Scholar
Shackleton, S. et al. LMNA, encoding lamin A/C, is mutated in partial lipodystrophy. Nature Genet.24, 153–156 (2000). CASPubMed Google Scholar
Manilal, S. et al. Mutations in Emery–Dreifuss muscular dystrophy and their effects on emerin protein expression. Hum. Mol. Genet.7, 855–864 (1998). CASPubMed Google Scholar
Yates, J. R. & Wehnert, M. The Emery–Dreifuss muscular dystrophy mutation database. Neuromuscul. Disord.9, 199 (1999). CASPubMed Google Scholar
Yates, J. R. et al. Genotype–phenotype analysis in X-linked Emery–Dreifuss muscular dystrophy and identification of a missense mutation associated with a milder phenotype. Neuromuscul. Disord.9, 159–165 (1999). CASPubMed Google Scholar
Di Blasi, C. et al. Unusual expression of emerin in a patient with X-linked Emery–Dreifuss muscular dystrophy. Neuromuscul. Disord.10, 567–571 (2000). CASPubMed Google Scholar
Ellis, J. A., Craxton, M., Yates, J. R. & Kendrick-Jones, J. Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery–Dreifuss muscular dystrophy phenotype. J. Cell Sci.111, 781–792 (1998). CASPubMed Google Scholar
Ellis, J. A. et al. Two distal mutations in the gene encoding emerin have profoundly different effects on emerin protein expression. Neuromuscul. Disord.10, 24–30 (2000). CASPubMed Google Scholar
Fairley, E. A., Kendrick-Jones, J. & Ellis, J. A. The Emery–Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane. J. Cell Sci.112, 2571–2582 (1999). CASPubMed Google Scholar
Lin, F. & Worman, H. J. Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C. J. Biol. Chem.268, 16321–16326 (1993). CASPubMed Google Scholar
Bonne, G. et al. Clinical and molecular genetic spectrum of autosomal dominant Emery–Dreifuss muscular dystrophy due to mutations of the lamin A/C gene. Ann. Neurol.48, 170–180 (2000). CASPubMed Google Scholar
Östlund, C., Bonne, G., Schwartz, K. & Worman, H. J. Properties of lamin A mutants found in Emery–Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy. J. Cell Sci.114, 4435–4445 (2001). PubMed Google Scholar
Raharjo, W. H., Enarson, P., Sullivan, T., Stewart, C. L. & Burke, B. Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery–Dreifuss muscular dystrophy. J. Cell Sci.114, 4447–4457 (2001). CASPubMed Google Scholar
Fidzianska, A., Toniolo, D. & Hausmanowa-Petrusewicz, I. Ultrastructural abnormality of sarcolemmal nuclei in Emery–Dreifuss muscular dystrophy (EDMD). J. Neurol. Sci.159, 88–93 (1998). CASPubMed Google Scholar
Ognibene, A. et al. Nuclear changes in a case of X-linked Emery–Dreifuss muscular dystrophy. Muscle Nerve22, 864–869 (1999). CASPubMed Google Scholar
Muchir, A. et al. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum. Mol. Genet.9, 1453–1459 (2000). CASPubMed Google Scholar
Brodsky, G. L. et al. Lamin A/C gene mutation associated with dilated cardiomyopathy with variable skeletal muscle involvement. Circulation101, 473–476 (2000). CASPubMed Google Scholar
De Sandre-Giovannoli, A. et al. Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. Am. J. Hum. Genet.70, 726–736 (2002). CASPubMedPubMed Central Google Scholar
Speckman, R. A. et al. Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C. Am. J. Hum. Genet.66, 1192–1198 (2000). CASPubMedPubMed Central Google Scholar
Raffaele Di Barletta, M. et al. Different mutations in the LMNA gene cause autosomal dominant and autosomal recessive Emery–Dreifuss muscular dystrophy. Am. J. Hum. Genet.66, 1407–1412 (2000). CASPubMedPubMed Central Google Scholar
Genschel, J. & Schmidt, H. H. Mutations in the LMNA gene encoding lamin A/C. Hum. Mutat.16, 451–459 (2000). CASPubMed Google Scholar
Garg, A., Speckman, R. A. & Bowcock, A. M. Multisystem dystrophy syndrome due to novel missense mutations in the amino-terminal head and α-helical rod domains of the lamin A/C gene. Am. J. Med.112, 549–555 (2002). CASPubMed Google Scholar
Cutler, D. A., Sullivan, T., Marcus-Samuels, B., Stewart, C. L. & Reitman, M. L. Characterization of adiposity and metabolism in _Lmna_-deficient mice. Biochem. Biophys. Res. Commun.291, 522–527 (2002). CASPubMed Google Scholar
Dhe-Paganon, S., Werner, E. D., Chi, Y. I. & Shoelson, S. E. Structure of the globular tail of nuclear lamin. J. Biol. Chem.277, 17381–17384 (2002).This paper shows the structure of the lamin A carboxy-terminal domain and provides important new insight into effects of disease-linkedLMNAmutations. CASPubMed Google Scholar
Krimm, I. et al. The Ig-like structure of the C-terminal domain of lamin a/c, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy. Structure (Camb.)10, 811–823 (2002).This study shows the structural analysis of the lamin A carboxy-terminal domain. It provides a valuable description of the effects of EDMD and FPLD mutations on the domain organization. CAS Google Scholar
Vigouroux, C. et al. Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene. J. Cell Sci.114, 4459–4468 (2001). CASPubMed Google Scholar
Lenz-Böhme, B. et al. Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae. J. Cell Biol.137, 1001–1016 (1997). PubMedPubMed Central Google Scholar
Liu, J. et al. Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol. Biol. Cell11, 3937–3947 (2000).An impressive demonstration of why lamins are essential for the maintenance of nuclear structure. CASPubMedPubMed Central Google Scholar
Hutchison, C. J., Alvarez-Reyes, M. & Vaughan, O. A. Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes? J. Cell Sci.114, 9–19 (2001). CASPubMed Google Scholar
Morris, G. E. & Manilal, S. Heart to heart: from nuclear proteins to Emery–Dreifuss muscular dystrophy. Hum. Mol. Genet.8, 1847–1851 (1999). CASPubMed Google Scholar
Newport, J. W., Wilson, K. L. & Dunphy, W. G. A lamin-independent pathway for nuclear envelope assembly. J. Cell Biol.111, 2247–2259 (1990). CASPubMed Google Scholar
Vallee, R. B., Tai, C. & Faulkner, N. E. LIS1: cellular function of a disease-causing gene. Trends Cell Biol.11, 155–160 (2001). CASPubMed Google Scholar
Xiang, X., Osmani, A. H., Osmani, S. A., Xin, M. & Morris, N. R. NudF, a nuclear migration gene in Aspergillus nidulans, is similar to the human LIS-1 gene required for neuronal migration. Mol. Biol. Cell6, 297–310 (1995). CASPubMedPubMed Central Google Scholar
Swan, A., Nguyen, T. & Suter, B. Drosophila Lissencephaly-1 functions with Bic-D and dynein in oocyte determination and nuclear positioning. Nature Cell Biol.1, 444–449 (1999). CASPubMed Google Scholar
Lei, Y. & Warrior, R. The Drosophila Lissencephaly-1 (DLis1) gene is required for nuclear migration. Dev. Biol.226, 57–72 (2000). CASPubMed Google Scholar
Liu, Z., Xie, T. & Steward, R. Lis1, the Drosophila homolog of a human lissencephaly disease gene, is required for germline cell division and oocyte differentiation. Development126, 4477–4488 (1999). CASPubMed Google Scholar
Guillemin, K., Williams, T. & Krasnow, M. A. A nuclear lamin is required for cytoplasmic organization and egg polarity in Drosophila. Nature Cell Biol.3, 848–851 (2001). CASPubMed Google Scholar
Mosley-Bishop, K. L., Li, Q., Patterson, L. & Fischer, J. A. Molecular analysis of the klarsicht gene and its role in nuclear migration within differentiating cells of the Drosophila eye. Curr. Biol.9, 1211–1220 (1999). CASPubMed Google Scholar
Ozaki, T. et al. Complex formation between lamin A and the retinoblastoma gene product: identification of the domain on lamin A required for its interaction. Oncogene9, 2649–2653 (1994). CASPubMed Google Scholar
Lloyd, D. J., Trembath, R. C. & Shackleton, S. A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies. Hum. Mol. Genet.11, 769–777 (2002). CASPubMed Google Scholar
Pahl, H. L. & Baeuerle, P. A. The ER-overload response: activation of NF-κB. Trends Biochem. Sci.22, 63–67 (1997). CASPubMed Google Scholar
Kapiloff, M. S., Schillace, R. V., Westphal, A. M. & Scott, J. D. mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes. J. Cell Sci.112, 2725–2736 (1999). CASPubMed Google Scholar
Moir, R. D. et al. Review: the dynamics of the nuclear lamins during the cell cycle — relationship between structure and function. J. Struct. Biol.129, 324–334 (2000). CASPubMed Google Scholar
Roeber, R.-A., Weber, K. & Osborn, M. Differential timing of lamin A/C expression in the various organs of the mouse embryo and the young animal: a developmental study. Development105, 365–378 (1989). Google Scholar
Stewart, C. & Burke, B. Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B. Cell51, 383–392 (1987). CASPubMed Google Scholar
Roeber, R.-A., Sauter, H., Weber, K. & Osborn, M. Cells of the cellular immune and hemopoietic system of the mouse lack lamins A/C: distinction versus other somatic cells. J. Cell Sci.95, 587–598 (1990). CAS Google Scholar
Pendas, A. M. et al. Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice. Nature Genet.31, 94–99 (2002). CASPubMed Google Scholar
Emery, A. E. & Dreifuss, F. E. Unusual type of benign X-linked muscular dystrophy. J. Neurol. Neurosurg. Psychiatry29, 338–342 (1966). CASPubMedPubMed Central Google Scholar
Nagano, A. et al. Emerin deficiency at the nuclear membrane in patients with Emery–Dreifuss muscular dystrophy. Nature Genet.12, 254–259 (1996). CASPubMed Google Scholar
Garg, A., Peshock, R. M. & Fleckenstein, J. L. Adipose tissue distribution pattern in patients with familial partial lipodystrophy (Dunnigan variety). J. Clin. Endocrinol. Metab.84, 170–174 (1999). CASPubMed Google Scholar
Brown, C. A. et al. Novel and recurrent mutations in lamin A/C in patients with Emery–Dreifuss muscular dystrophy. Am. J. Med. Genet.102, 359–367 (2001). CASPubMed Google Scholar
Senior, A. & Gerace, L. Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina. J. Cell Biol.107, 2029–2036 (1988).Identification of the first INM-specific proteins, which are members of the LAP1 family. CASPubMed Google Scholar
Martin, L., Crimaudo, C. & Gerace, L. cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane. J. Biol. Chem.270, 8822–8828 (1995). CASPubMed Google Scholar
Furukawa, K., Panté, N., Aebi, U. & Gerace, L. Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope. EMBO J.14, 1626–1636 (1995). CASPubMedPubMed Central Google Scholar
Harris, C. A. et al. Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO β to rat lamin-associated polypeptide 2. Genomics28, 198–205 (1995). CASPubMed Google Scholar
Holmer, L., Pezhman, A. & Worman, H. J. The human lamin B receptor/sterol reductase multigene family. Genomics54, 469–476 (1998). CASPubMed Google Scholar
Worman, H. J., Evans, C. D. & Blobel, G. The lamin B receptor of the nuclear envelope inner membrane: a polytopic protein with eight potential transmembrane domains. J. Cell Biol.111, 1535–1542 (1990). CASPubMed Google Scholar
Dreger, M., Bengtsson, L., Schoneberg, T., Otto, H. & Hucho, F. Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane. Proc. Natl Acad. Sci. USA98, 11943–11948 (2001). CASPubMedPubMed Central Google Scholar
Mansharamani, M., Hewetson, A. & Chilton, B. S. Cloning and characterization of an atypical Type IV P-type ATPase that binds to the RING motif of RUSH transcription factors. J. Biol. Chem.276, 3641–3649 (2001). CASPubMed Google Scholar
Novelli, G. et al. Mandibuloacral dysplasia is caused by a mutation in _LMNA_-encoding lamin A/C. Am. J. Hum. Genet.71, 426–431 (2002). CASPubMedPubMed Central Google Scholar