Emerin in health and disease

Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks

Olsen, J. V., Blagoev, B., Gnad, F., Maček, B., Kumar, C., Mortensen, P., & Mann, M. (2006) · Cell · doi:10.1016/j.cell.2006.09.026 · Cited by 3,484 · see citing works

Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions

Guelen, L., Pagie, L., Brasset, É., Meuleman, W. R. A., Faza, M. B., Talhout, W., Eussen, B. H. J., de Klein, A., Wessels, L. F. A., de Laat, W. L., et al. (2008) · Nature · doi:10.1038/nature06947 · Cited by 1,959 · see citing works

Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus

Wang, N., Tytell, J. D., & Ingber, D. E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2594 · Cited by 1,768 · see citing works

A quantitative atlas of mitotic phosphorylation

Dephoure, N., Zhou, C., Villén, J., Beausoleil, S. A., Bakalarski, C. E., Elledge, S. J., & Gygi, S. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805139105 · Cited by 1,608 · see citing works

Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis

Olsen, J., Vermeulen, M., Santamaría, A., Kumar, C., Miller, M. L., Jensen, L., Gnad, F., Cox, J., Jensen, T., Nigg, E., et al. (2010) · Science Signaling · doi:10.1126/scisignal.2000475 · Cited by 1,552 · see citing works

Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy

Bonne, G., di Barletta, M. R., Varnous, S., Bécane, H. M., Hammouda, E.-H., Merlini, L., Francesco Muntoni, A., Greenberg, C. R., Gary, F., Urtizberea, J. A., et al. (1999) · Nature Genetics · doi:10.1038/6799 · Cited by 1,353 · see citing works

Coupling of the nucleus and cytoplasm: Role of the LINC complex

Crisp, M., Liu, Q., Roux, K. J., Rattner, J. B., Shanahan, C. M., Burke, B. E., Stahl, P. D., & Hodzic, D. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200509124 · Cited by 1,339 · see citing works

Actin dynamics control SRF activity by regulation of its coactivator MAL

Miralles, F., Posern, G., Zaromytidou, A.-I., & Treisman, R. (2003) · Cell · doi:10.1016/s0092-8674(03)00278-2 · Cited by 1,327 · see citing works

Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease

Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317 · see citing works

Loss of a-Type Lamin Expression Compromises Nuclear Envelope Integrity Leading to Muscular Dystrophy

Sullivan, T. L., Escalante‐Alcalde, D., Bhatt, H., Anver, M. R., BHAT, N. K., Nagashima, K., Stewart, C. L., & Burke, B. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.913 · Cited by 1,197 · see citing works

Immunoaffinity profiling of tyrosine phosphorylation in cancer cells

Rush, A. J., Moritz, A., Lee, K. A., Guo, A., Goss, V. L., Spek, E. J., Zhang, H., Zha, X., Polakiewicz, R. D., & Comb, M. J. (2004) · Nature Biotechnology · doi:10.1038/nbt1046 · Cited by 1,126 · see citing works

Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction

Lammerding, J., Schulze, P. C., Takahashi, T., Kozlov, S. V., Sullivan, T. L., Kamm, R. D., Stewart, C. L., & Lee, R. T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419670 · Cited by 1,068 · see citing works

Molecular Maps of the Reorganization of Genome-Nuclear Lamina Interactions during Differentiation

Peric-Hupkes, D., Meuleman, W., Pagie, L., Bruggeman, S. W. M., Solovei, I., Brugman, W., Gräf, S., Flicek, P., Kerkhoven, R. M., van Lohuizen, M., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.03.016 · Cited by 1,050 · see citing works

Linking actin dynamics and gene transcription to drive cellular motile functions

Olson, E. N., & Nordheim, A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2890 · Cited by 958 · see citing works

The Regulation of Notch Signaling Controls Satellite Cell Activation and Cell Fate Determination in Postnatal Myogenesis

Conboy, I. M., & Rando, T. A. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00254-x · Cited by 905 · see citing works

Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy

Bione, S., Maestrini, E., Rivella, S., Mancini, M., Regis, S., Romeo, G., & Toniolo, D. (1994) · Nature Genetics · doi:10.1038/ng1294-323 · Cited by 886 · see citing works

LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation

Solovei, I., Wang, A. S., Thanisch, K., Schmidt, C. S., Krebs, S., Zwerger, M., Cohen, T. V., Devys, D., Foisner, R., Peichl, L., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.009 · Cited by 809 · see citing works

Transcriptional repression mediated by repositioning of genes to the nuclear lamina

Reddy, K. L., Zullo, J., Bertolino, E., & Singh, H. (2008) · Nature · doi:10.1038/nature06727 · Cited by 785 · see citing works

Nuclear Lamins: Their Structure, Assembly, and Interactions

Stuurman, N., Heins, S., & Aebi, U. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1998.3987 · Cited by 721 · see citing works

The Skeletal Muscle Satellite Cell: The Stem Cell That Came in From the Cold

Zammit, P. S., Partridge, T. A., & Yablonka‐Reuveni, Z. (2006) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.6r6995.2006 · Cited by 684 · see citing works

A Temporal Switch from Notch to Wnt Signaling in Muscle Stem Cells Is Necessary for Normal Adult Myogenesis

Brack, A. S., Conboy, I. M., Conboy, M. J., Shen, J., & Rando, T. A. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2007.10.006 · Cited by 682 · see citing works

Characterization of the Drosophila melanogaster genome at the nuclear lamina

Pickersgill, H., Kalverda, B., de Wit, E., Talhout, W., Fornerod, M., & van Steensel, B. (2006) · Nature Genetics · doi:10.1038/ng1852 · Cited by 656 · see citing works

Nuclear Membrane Proteins with Potential Disease Links Found by Subtractive Proteomics

Schirmer, E. C., Florens, L. A., Guan, T., Yates, J. R., & Gerace, L. (2003) · Science · doi:10.1126/science.1088176 · Cited by 654 · see citing works

Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis

Heald, R., & McKeon, F. (1990) · Cell · doi:10.1016/0092-8674(90)90470-y · Cited by 650 · see citing works

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle

Daub, H., Olsen, J. V., Bairlein, M., Gnad, F., Oppermann, F. S., Körner, R., Greff, Z., Kéri, G., Stemmann, O., & Mann, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.007 · Cited by 594 · see citing works

Recruitment to the Nuclear Periphery Can Alter Expression of Genes in Human Cells

Finlan, L. E., Sproul, D., Thomson, I., Boyle, S., Kerr, E. A., Perry, P., Ylstra, B., Chubb, J. R., & Bickmore, W. A. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000039 · Cited by 584 · see citing works

Dynamic O-GlcNAc Modification of Nucleocytoplasmic Proteins in Response to Stress

Zachara, N. E., O'Donnell, N., Cheung, W. D., Mercer, J. J., Marth, J. D., & Hart, G. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403773200 · Cited by 568 · see citing works

The nuclear lamins: flexibility in function

Burke, B. E., & Stewart, C. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3488 · Cited by 563 · see citing works

Type beta transforming growth factor is an inhibitor of myogenic differentiation.

Massagué, J., Cheifetz, S., Endo, T., & Nadal‐Ginard, B. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8206 · Cited by 550 · see citing works

Nesprin-1 and -2 are involved in the pathogenesis of Emery–Dreifuss muscular dystrophy and are critical for nuclear envelope integrity

Zhang, Q., Bethmann, C., Worth, N. F., Davies, J. D., Wasner, C., Feuer, A., Ragnauth, C. D., Yi, Q., Mellad, J. A., Warren, D. T., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm238 · Cited by 539 · see citing works

Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation

Foisner, R., & Gerace, L. (1993) · Cell · doi:10.1016/0092-8674(93)90355-t · Cited by 535 · see citing works

Wnt Signaling Induces the Myogenic Specification of Resident CD45+ Adult Stem Cells during Muscle Regeneration

Polesskaya, A., Seale, P., & Rudnicki, M. A. (2003) · Cell · doi:10.1016/s0092-8674(03)00437-9 · Cited by 515 · see citing works

Niche Regulation of Muscle Satellite Cell Self-Renewal and Differentiation

Kuang, S., Gillespie, M. A., & Rudnicki, M. A. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2007.12.012 · Cited by 507 · see citing works

SUN1 Interacts with Nuclear Lamin A and Cytoplasmic Nesprins To Provide a Physical Connection between the Nuclear Lamina and the Cytoskeleton

Haque, F., Lloyd, D. J., Smallwood, D. T., Dent, C. L., Shanahan, C. M., Fry, A. M., Trembath, R. C., & Shackleton, S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3738-3751.2006 · Cited by 504 · see citing works

The lamin protein family

Dittmer, T. A., & Misteli, T. (2011) · Genome biology · doi:10.1186/gb-2011-12-5-222 · Cited by 479 · see citing works

Constitutive nuclear lamina-genome interactions are highly conserved and associated with A/T-rich sequence

Meuleman, W., Peric-Hupkes, D., Kind, J., Beaudry, J.-B., Pagie, L., Kellis, M., Reinders, M., Wessels, L., & van Steensel, B. (2013) · Genome Research · doi:10.1101/gr.141028.112 · Cited by 462 · see citing works

Lamin A/C and emerin regulate MKL1–SRF activity by modulating actin dynamics

Ho, C. Y., Jaalouk, D. E., Vartiainen, M. K., & Lammerding, J. (2013) · Nature · doi:10.1038/nature12105 · Cited by 456 · see citing works

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation

Rigbolt, K. T. G., Prokhorova, T. A., Akimov, V., Henningsen, J., Johansen, P. T., Kratchmarova, I., Kassem, M., Mann, M., Olsen, J. V., & Blagoev, B. (2011) · Science Signaling · doi:10.1126/scisignal.2001570 · Cited by 451 · see citing works

DNA Sequence-Dependent Compartmentalization and Silencing of Chromatin at the Nuclear Lamina

Zullo, J., Demarco, I. A., Piqué-Regi, R., Gaffney, D. J., Epstein, C. B., Spooner, C. J., Luperchio, T. R., Bernstein, B., Pritchard, J. K., Reddy, K. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.035 · Cited by 448 · see citing works

Different Mutations in the LMNA Gene Cause Autosomal Dominant and Autosomal Recessive Emery-Dreifuss Muscular Dystrophy

di Barletta, M. R., Ricci, E., Galluzzi, G., Tonali, P. A., Mora, M., Morandi, L. O., Romorini, A., Voït, T., Ørstavik, K. H., Merlini, L., et al. (2000) · The American Journal of Human Genetics · doi:10.1086/302869 · Cited by 415 · see citing works

The inner nuclear membrane protein Sun1 mediates the anchorage of Nesprin-2 to the nuclear envelope

Padmakumar, V. C., Libotte, T., Lu, W., Zaim, H., Abraham, S., Noegel, A. A., Gotzmann, J., Foisner, R., & Karakesisoglou, I. (2005) · Journal of Cell Science · doi:10.1242/jcs.02471 · Cited by 410 · see citing works

The C. elegans Hook Protein, ZYG-12, Mediates the Essential Attachment between the Centrosome and Nucleus

Malone, C. J., Misner, L., Bot, N. L., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00985-1 · Cited by 406 · see citing works

Nuclear lamins and laminopathies

Worman, H. J. (2011) · The Journal of Pathology · doi:10.1002/path.2999 · Cited by 391 · see citing works

A genetic locus targeted to the nuclear periphery in living cells maintains its transcriptional competence

Kumaran, R. I., & Spector, D. L. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200706060 · Cited by 388 · see citing works

Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells

Lammerding, J., Hsiao, J., Schulze, P. C., Kozlov, S. V., Stewart, C. L., & Lee, R. T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502148 · Cited by 381 · see citing works

The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein

Manilal, S. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.6.801 · Cited by 380 · see citing works

β- N -acetylglucosamine (O-GlcNAc) is part of the histone code

Sakabe, K., Wang, Z., & Hart, G. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009023107 · Cited by 372 · see citing works

Primary Prevention of Sudden Death in Patients with Lamin A/C Gene Mutations

Meune, C., van Berlo, J. H., Anselme, F., Bonne, G., Pinto, Y. M., & Duboc, D. (2006) · New England Journal of Medicine · doi:10.1056/nejmc052632 · Cited by 365 · see citing works

MAN1, an Inner Nuclear Membrane Protein That Shares the LEM Domain with Lamina-associated Polypeptide 2 and Emerin

Lin, F., Blake, D. L., Callebaut, I., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4840 · Cited by 344 · see citing works

Emerin deficiency at the nuclear membrane in patients with Emery-Dreif uss muscular dystrophy

Nagano, A. J., Koga, R., Ogawa, M., Kurano, Y., Kawada, J., Okada, R., Hayashi, Y. K., Tsukahara, T., & Arahata, K. (1996) · Nature Genetics · doi:10.1038/ng0396-254 · Cited by 341 · see citing works

Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF

Lee, K. K., Haraguchi, T., Lee, R. S., Koujin, T., Hiraoka, Y., & Wilson, K. L. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.24.4567 · Cited by 336 · see citing works

Nuclear envelope dystrophies show a transcriptional fingerprint suggesting disruption of Rb–MyoD pathways in muscle regeneration

Bakay, M. A., Wang, Z., Melcon, G., Schiltz, L., Xuan, J., Zhao, P., Sartorelli, V., Seo, J., Pegoraro, E., Angelini, C. I., et al. (2006) · Brain · doi:10.1093/brain/awl023 · Cited by 331 · see citing works

Muscle regeneration: cellular and molecular events.

Karalaki, M., Fili, S., Philippou, Α., & Koutsilieris, M. (2009) · PubMed · Cited by 330 · see citing works

Knee extensor strength, activation, and size in very elderly people following strength training

Harridge, S. D. R., Kryger, A. I., & Stensgaard, A. (1999) · Muscle & Nerve · doi:10.1002/(sici)1097-4598(199907)22:7 · Cited by 322 · see citing works

Ufd2, a Novel Autoantigen in Scleroderma, Regulates Sister Chromatid Separation

Spinette, S., Christoph Lengauer, C., Mahoney, J. A., Jallepalli, P. V., Wang, Z., Casciola-Rosen, L., & Rosen, A. (2004) · Cell Cycle · doi:10.4161/cc.3.12.1345 · Cited by 309 · see citing works

Proteomic Analysis of Interchromatin Granule Clusters

Saitoh, N., Spahr, C. S., Patterson, S. D., et al. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-03-0253 · Cited by 307 · see citing works

Comparative Genomics, Evolution and Origins of the Nuclear Envelope and Nuclear Pore Complex

Mans, B., Anantharaman, V., Aravind, L., & Koonin, E. V. (2004) · Cell Cycle · doi:10.4161/cc.3.12.1316 · Cited by 304 · see citing works

Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry

Tao, W. A., Wollscheid, B., O'Brien, R., Eng, J. K., Li, X., Bodenmiller, B., Watts, J. D., Hood, L., & Aebersold, R. H. (2005) · Nature Methods · doi:10.1038/nmeth776 · Cited by 300 · see citing works

NUANCE, a giant protein connecting the nucleus and actin cytoskeleton

Zhen, Y., Libotte, T., Munck, M., et al. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.15.3207 · Cited by 293 · see citing works

Mammalian SUN Protein Interaction Networks at the Inner Nuclear Membrane and Their Role in Laminopathy Disease Processes

Haque, F., Mazzeo, D., Patel, J. T., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071910 · Cited by 287 · see citing works

The nucleoskeleton as a genome-associated dynamic 'network of networks'

Simon, D. N., & Wilson, K. L. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3207 · Cited by 282 · see citing works

Canonical Wnt signalling induces satellite-cell proliferation during adult skeletal muscle regeneration

Otto, A., Schmidt, C., Luke, G. N., Allen, S., Valášek, P., Francesco Muntoni, A., Lawrence‐Watt, D. J., & Patel, K. (2008) · Journal of Cell Science · doi:10.1242/jcs.026534 · Cited by 282 · see citing works

Nuclear lamins: key regulators of nuclear structure and activities

Prokocimer, M., Davidovich, M., Nissim‐Rafinia, M., Wiesel‐Motiuk, N., Bar, D. Z., Barkan, R., Meshorer, E., & Gruenbaum, Y. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00676.x · Cited by 272 · see citing works

The Molecular Regulation of Muscle Stem Cell FunctionPreprint

Rudnicki, M. A., Grand, F. L., McKinnell, I. W., & Kuang, S. (2008) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2008.73.064 · Cited by 261 · see citing works

Nesprin‐1α self‐associates and binds directly to emerin and lamin A in vitro

Mislow, J. M. K., Holaska, J. M., Kim, M. S., Lee, K. K., Segura‐Totten, M., Wilson, K. L., & McNally, E. M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03105-8 · Cited by 260 · see citing works

BAF is required for emerin assembly into the reforming nuclear envelope

Haraguchi, T., Koujin, T., Segura‐Totten, M., Lee, K. K., Matsuoka, Y., Yoneda, Y., Wilson, K. L., & Hiraoka, Y. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.24.4575 · Cited by 257 · see citing works

p53-cofactor JMY is a multifunctional actin nucleation factor

Zuchero, J. B., Coutts, A. S., Quinlan, M. E., Thangue, N. B. L., & Mullins, R. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1852 · Cited by 257 · see citing works

Mechanical Properties of the Cell Nucleus and the Effect of Emerin Deficiency

Rowat, A. C., Lammerding, J., & Ipsen, J. H. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.086454 · Cited by 257 · see citing works

Laminopathies and the long strange trip from basic cell biology to therapy

Worman, H. J., Fong, L. G., Muchir, A., & Young, S. G. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37679 · Cited by 256 · see citing works

Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiationPreprint

Frock, R. L., Kudlow, B. A., Evans, A. M., Jameson, S. A., Hauschka, S. D., & Kennedy, B. K. (2006) · Genes & Development · doi:10.1101/gad.1364906 · Cited by 256 · see citing works

Lamin-binding ProteinsPreprint

Wilson, K. L., & Foisner, R. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000554 · Cited by 253 · see citing works

The inner nuclear membrane protein Emerin regulates β‐catenin activity by restricting its accumulation in the nucleus

Markiewicz, E., Tilgner, K., Barker, N., van de Wetering, M., Clevers, H., Dorobek, M., Hausmanowa‐Petrusewicz, I., Ramaekers, F. C., Broers, J. L., Blankesteijn, W. M., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601230 · Cited by 246 · see citing works

Mutations of the FHL1 Gene Cause Emery-Dreifuss Muscular Dystrophy

Gueneau, L., Bertrand, A., Jaïs, J., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.07.015 · Cited by 241 · see citing works

Emery–Dreifuss muscular dystrophy – a 40 year retrospective

Emery, A. E. H. (2000) · Neuromuscular Disorders · doi:10.1016/s0960-8966(00)00105-x · Cited by 239 · see citing works

Transcriptional Repressor Germ Cell-less (GCL) and Barrier to Autointegration Factor (BAF) Compete for Binding to Emerin in Vitro

Holaska, J. M., Lee, K. K., Kowalski, A. K., & Wilson, K. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208811200 · Cited by 236 · see citing works

Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly

Haraguchi, T., Kojidani, T., Koujin, T., Shimi, T., Osakada, H., Mori, C., Yamamoto, A., & Hiraoka, Y. (2008) · Journal of Cell Science · doi:10.1242/jcs.033597 · Cited by 235 · see citing works

Emerin Caps the Pointed End of Actin Filaments: Evidence for an Actin Cortical Network at the Nuclear Inner Membrane

Holaska, J. M., Kowalski, A. K., & Wilson, K. L. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020231 · Cited by 233 · see citing works

LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction

Furukawa, K. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.15.2485 · Cited by 232 · see citing works

Btf, a Novel Death-Promoting Transcriptional Repressor That Interacts with Bcl-2-Related Proteins

Kasof, G. M., Goyal, L., & White, E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4390 · Cited by 225 · see citing works

Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM‐domain structures: one binds BAF and the other binds DNA

Cai, M., Huang, Y., Ghirlando, R., Wilson, K. L., Craigie, R., & Clore, G. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4399 · Cited by 225 · see citing works

The nuclear-envelope protein and transcriptional repressor LAP2β interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation

Somech, R., Shaklai, S., Geller, O., Amariglio, N., Simon, A. J., Rechavi, G., & Gal-Yam, E. N. (2005) · Journal of Cell Science · doi:10.1242/jcs.02521 · Cited by 223 · see citing works

Global Effects of Kinase Inhibitors on Signaling Networks Revealed by Quantitative Phosphoproteomics

Pan, C., Olsen, J. V., Daub, H., & Mann, M. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900285-mcp200 · Cited by 222 · see citing works

Accumulation of the Inner Nuclear Envelope Protein Sun1 Is Pathogenic in Progeric and Dystrophic Laminopathies

Chen, C., Chi, Y., Mutalif, R., Starost, M. F., Myers, T. G., Anderson, S. A., Stewart, C. L., & Jeang, K. (2012) · Cell · doi:10.1016/j.cell.2012.01.059 · Cited by 221 · see citing works

Loss of emerin at the nuclear envelope disrupts the Rb1/E2F and MyoD pathways during muscle regeneration

Melcon, G., Kozlov, S. V., Cutler, D. A., Sullivan, T., Hernandez, L. F., Zhao, P., Mitchell, S., Nader, G. A., Bakay, M. A., Rottman, J. N., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi479 · Cited by 220 · see citing works

Phosphoproteomic analysis of Her2/neu signaling and inhibition

Bose, R., Molina, H., Patterson, A., Bitok, J. K., Periaswamy, B., Bader, J. S., Pandey, A., & Cole, P. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603948103 · Cited by 215 · see citing works

LAP2 binds to BAF·DNA complexes: requirement for the LEM domain and modulation by variable regions

Shumaker, D. K., Lee, K. K., Tanhehco, Y. C., Craigie, R., & Wilson, K. L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1754 · Cited by 212 · see citing works

Emery-Dreifuss syndrome.

Emery, A. E. H. (1989) · Journal of Medical Genetics · doi:10.1136/jmg.26.10.637 · Cited by 211 · see citing works

Robust Phosphoproteomic Profiling of Tyrosine Phosphorylation Sites from Human T Cells Using Immobilized Metal Affinity Chromatography and Tandem Mass Spectrometry

Brill, L. M., Salomon, A. R., Ficarro, S. B., Mukherji, M., Stettler‐Gill, M., & Peters, E. C. (2004) · Analytical Chemistry · doi:10.1021/ac035352d · Cited by 210 · see citing works

The Nesprins Are Giant Actin-Binding Proteins, Orthologous to Drosophila melanogaster Muscle Protein MSP-300

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