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

Activation of β-Catenin-Tcf Signaling in Colon Cancer by Mutations in β-Catenin or APC

Morin, P. J., Sparks, A. B., Kořínek, V., Barker, N., Clevers, H. C., Vogelstein, B., & Kinzler, K. W. (1997) · Science · doi:10.1126/science.275.5307.1787 · Cited by 4,000

Functional interaction of β-catenin with the transcription factor LEF-1

Behrens, J., von Kries, J. P., Kühl, M., Bruhn, L., Wedlich, D., Grosschedl, R., & Birchmeier, W. (1996) · Nature · doi:10.1038/382638a0 · Cited by 2,912

A role for Wnt signalling in self-renewal of haematopoietic stem cells

Reya, T., Duncan, A. W., Ailles, L., Domen, J., Scherer, D. C., Willert, K., Hintz, L., Nusse, R., & Weissman, I. L. (2003) · Nature · doi:10.1038/nature01593 · Cited by 2,159

The β-Catenin/TCF-4 Complex Imposes a Crypt Progenitor Phenotype on Colorectal Cancer Cells

van de Wetering, M., Sancho, E., Verweij, C., de Lau, W., Oving, I., Hurlstone, A., van der Horn, K., Batlle, E., Coudreuse, D., Haramis, A.-P., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)01014-0 · Cited by 2,030

XTcf-3 Transcription Factor Mediates β-Catenin-Induced Axis Formation in Xenopus Embryos

Molenaar, M., van de Wetering, M., Oosterwegel, M., Peterson-Maduro, J., Godsave, S., Korinek, V., Roose, J., Destrée, O., & Clevers, H. (1996) · Cell · doi:10.1016/s0092-8674(00)80112-9 · Cited by 1,824

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., Muntoni, F., Greenberg, C. R., Gary, F., Urtizberea, J. A., et al. (1999) · Nature Genetics · doi:10.1038/6799 · Cited by 1,384

Missense Mutations in the Rod Domain of the Lamin A/C Gene as Causes of Dilated Cardiomyopathy and Conduction-System Disease

Fatkin, D., MacRae, C. A., Sasaki, T., Wolff, M. R., Porcu, M., Frenneaux, M. P., Atherton, J. J., Vidaillet, H. J., Jr., Spudich, S., Girolami, U. D., et al. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912023412302 · Cited by 1,366

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. R., Nagashima, K., Stewart, C. L., & Burke, B. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.913 · Cited by 1,224

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 913

Identification of essential genes in cultured mammalian cells using small interfering RNAs

Harborth, J., Elbashir, S. M., Bechert, K., Tuschl, T., & Weber, K. K. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.24.4557 · Cited by 828

Unique and Shared Functions of Nuclear Lamina LEM Domain Proteins in Drosophila

Barton, L. J., Wilmington, S. R., Martin, M. J., Skopec, H. M., Lovander, K. E., Pinto, B. S., & Geyer, P. (2014) · Genetics · doi:10.1534/genetics.114.162941 · Cited by 38

Identification of an emerin–β-catenin complex in the heart important for intercalated disc architecture and β-catenin localisation

Wheeler, M., Warley, A., Roberts, R. G., Ehler, E., & Ellis, J. A. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0219-8 · Cited by 38

Attenuation of Wnt/β-catenin activity reverses enhanced generation of cardiomyocytes and cardiac defects caused by the loss of emerin

Stubenvoll, A., Rice, M., Wietelmann, A., Wheeler, M., & Braun, T. W. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu498 · Cited by 42

The Cellular Mastermind(?)—Mechanotransduction and the Nucleus

Kaminski, A., Fedorchak, G. R., & Lammerding, J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394624-9.00007-5 · Cited by 38

LAP2 Is Widely Overexpressed in Diverse Digestive Tract Cancers and Regulates Motility of Cancer Cells

Kim, H.-J., Hwang, S.-H., Han, M.-E., Baek, S., Sim, H.-E., Yoon, S., Baek, S., Kim, B.-S., Kim, J.-H., Kim, S.-Y., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039482 · Cited by 34

Chromatin epigenetics and nuclear lamina keep the nucleus in shape: Examples from natural and accelerated aging

Carollo, P. S., & Barra, V. (2022) · Biology of the Cell · doi:10.1111/boc.202200023 · Cited by 31

iTRAQ-based analysis of progerin expression reveals mitochondrial dysfunction, reactive oxygen species accumulation and altered proteostasis

Mateos, J., Landeira-Abia, A., Fafián‐Labora, J., Fernández‐Pernas, P., Lesende‐Rodriguez, I., Fernández‐Puente, P., Fernández-Moreno, M., Delmiro, A., Martín, M. A., Blanco, F. J., et al. (2015) · Stem Cell Research & Therapy · doi:10.1186/s13287-015-0110-5 · Cited by 37

Protein sequestration at the nuclear periphery as a potential regulatory mechanism in premature aging

Serebryannyy, L., & Misteli, T. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201706061 · Cited by 37

Nuclear mechanotransduction in stem cells

Hamouda, M. S., Labouesse, C., & Chalut, K. J. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.05.005 · Cited by 34

Nuclear Envelope Regulation of Signaling Cascades

Choi, J. C., & Worman, H. J. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-8032-8_9 · Cited by 34

Regulation of adipogenesis and osteogenesis in mesenchymal stem cells by vascular endothelial growth factor A

Berendsen, A. D., & Olsen, B. R. (2015) · Journal of Internal Medicine · doi:10.1111/joim.12364 · Cited by 31

Upsetting the Balance: When Viruses Manipulate Cell Polarity Control

Thomas, M., & Banks, L. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.04.016 · Cited by 31

The emerin-binding transcription factor Lmo7 is regulated by association with p130Cas at focal adhesions

Wozniak, M. A., Baker, B. M., Chen, C. S., & Wilson, K. L. (2013) · PeerJ · doi:10.7717/peerj.134 · Cited by 29

The Drosophila Nuclear Lamina Protein Otefin Is Required for Germline Stem Cell Survival

Barton, L. J., Pinto, B. S., Wallrath, L. L., & Geyer, P. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.023 · Cited by 29

Alterations in the Nuclear Architecture Produced by the Overexpression of Tau Protein in Neuroblastoma Cells

Monroy-Ramírez, H. C., Basurto‐Islas, G., Mena, R., Cisneros, B., Binder, L. I., Ávila, J., & García‐Sierra, F. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122401 · Cited by 32

Involvement of an inner nuclear membrane protein, Nemp1, in Xenopus neural development through an interaction with the chromatin protein BAF

Mamada, H., Takahashi, N., & Taira, M. (2009) · Developmental Biology · doi:10.1016/j.ydbio.2008.12.038 · Cited by 28

Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome–nucleus association and transcriptional signaling

Meyer, A. J., Almendrala, D. K., Go, M. M., & Krauss, S. W. (2011) · Journal of Cell Science · doi:10.1242/jcs.077883 · Cited by 27

The Inner Nuclear Membrane Protein Nemp1 Is a New Type of RanGTP-Binding Protein in Eukaryotes

Shibano, T., Mamada, H., Hakuno, F., Takahashi, S.-I., & Taira, M. (2015) · PLOS ONE · doi:10.1371/journal.pone.0127271 · Cited by 27

Nucleoskeletal regulation of transcription: Actin on MRTF

Sidorenko, E., & Vartiainen, M. K. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219854669 · Cited by 32

LINCing Nuclear Mechanobiology With Skeletal Muscle Mass and Function

van Ingen, M. J. A., & Kirby, T. J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.690577 · Cited by 26

Emerin suppresses Notch signaling by restricting the Notch intracellular domain to the nuclear membrane

Lee, B., Lee, T.-H., & Shim, J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.11.013 · Cited by 27

MAPK signaling pathways and HDAC3 activity are disrupted during emerin-null myogenic progenitor differentiation

Collins, C. M., Ellis, J. A., & Holaska, J. M. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028787 · Cited by 26

Organization of nuclear architecture during adipocyte differentiation

Charó, N. L., Ceschan, M. I. R., Galigniana, N. M., Toneatto, J., & Piwien‐Pilipuk, G. (2016) · Nucleus · doi:10.1080/19491034.2016.1197442 · Cited by 27

Increased expression of Syne1/nesprin‐1 facilitates nuclear envelope structure changes in embryonic stem cell differentiation

Smith, E. R., Zhang, X., Capo‐chichi, C. D., Chen, X., & Xu, X. (2011) · Developmental Dynamics · doi:10.1002/dvdy.22717 · Cited by 25

A Flow Cytometry-Based Screen of Nuclear Envelope Transmembrane Proteins Identifies NET4/Tmem53 as Involved in Stress-Dependent Cell Cycle Withdrawal

Korfali, N., Sršeň, V., Waterfall, M., Batrakou, D. G., Pekovic‐Vaughan, V., Hutchison, C. J., & Schirmer, E. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018762 · Cited by 24

Control of nuclear organization by F-actin binding proteins

Pfisterer, K., Jayo, A., & Parsons, M. (2017) · Nucleus · doi:10.1080/19491034.2016.1267093 · Cited by 24

Cytoskeleton and nuclear lamina affection in recessive osteogenesis imperfecta: A functional proteomics perspective

Gagliardi, A., Besio, R., Carnemolla, C., Landi, C., Armini, A., Aglan, M., Otaify, G. A., Temtamy, S. A., Forlino, A., Bini, L., et al. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.08.007 · Cited by 25

Nucleus Mechanosensing in Cardiomyocytes

Coscarella, I. L., Landim-Vieira, M., Rastegarpouyani, H., Chase, P. B., Irianto, J., & Pinto, J. R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713341 · Cited by 25

At the nuclear envelope of bone mechanobiology

Birks, S., & Uzer, G. (2021) · Bone · doi:10.1016/j.bone.2021.116023 · Cited by 22

Comparative proteomic analyses of the nuclear envelope and pore complex suggests a wide range of heretofore unexpected functions

Batrakou, D. G., Kerr, A. R. W., & Schirmer, E. C. (2008) · Journal of Proteomics · doi:10.1016/j.jprot.2008.09.004 · Cited by 24

Feeling the force from within – new tools and insights into nuclear mechanotransduction

Morival, J. L. P., Hazelwood, A., & Lammerding, J. (2025) · Journal of Cell Science · doi:10.1242/jcs.263615 · Cited by 26

Proteomic Analysis of Proton Beam Irradiated Human Melanoma Cells

Kędracka–Krok, S., Jankowska, U., Elas, M., Sowa, U., Swakoń, J., Cierniak, A., Olko, P., Romanowska‐Dixon, B., & Urbańska, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084621 · Cited by 23

Karyopherin Alpha 1 Regulates Satellite Cell Proliferation and Survival by Modulating Nuclear Import

Choo, H. J., Cutler, A. A., Rother, F., Bäder, M., & Pavlath, G. K. (2016) · Stem Cells · doi:10.1002/stem.2467 · Cited by 23

Nesprin proteins: bridging nuclear envelope dynamics to muscular dysfunction

Zi-yi, Z., Qin, Q., Fei, Z., Cun-Yu, C., & Lin, T. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01593-y · Cited by 23

Barrier-to-Autointegration Factor 1 (BAF/BANF1) Promotes Association of the SETD1A Histone Methyltransferase with Herpes Simplex Virus Immediate-Early Gene Promoters

Oh, H. S., Traktman, P., & Knipe, D. M. (2015) · mBio · doi:10.1128/mbio.00345-15 · Cited by 22

Emerin Is Required for Proper Nucleus Reassembly after Mitosis: Implications for New Pathogenetic Mechanisms for Laminopathies Detected in EDMD1 Patients

Dubińska–Magiera, M., Kozioł, K., Machowska, M., Piekarowicz, K., Filipczak, D., & Rzepecki, R. (2019) · Cells · doi:10.3390/cells8030240 · Cited by 22

Molecular signatures of Emery–Dreifuss muscular dystrophy

Wheeler, M., & Ellis, J. A. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361354 · Cited by 22

Absence of Nuclear p16 Is a Diagnostic and Independent Prognostic Biomarker in Squamous Cell Carcinoma of the Cervix

Mendaza, S., Fernández‐Irigoyen, J., Santamaría, E., Zudaire, T., Guarch, R., Guerrero‐Setas, D., Vidal, A., Santos-Salas, J., Matías‐Guiu, X., Ausín, K., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062125 · Cited by 21

Molecular Mechanisms for the Regulation of Nuclear Membrane Integrity

Lee, G.-E., Byun, J., Lee, C., & Cho, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015497 · Cited by 22

N-terminal nesprin-2 variants regulate β-catenin signalling

Zhang, Q., Minaisah, R.-M., Ferraro, E., Li, C., Porter, L. J., Zhou, C., Gao, F., Zhang, J., Rajgor, D., Autore, F., et al. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.06.008 · Cited by 21

The increasing relevance of nuclear envelope myopathies

Meinke, P., & Schirmer, E. C. (2016) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000359 · Cited by 20

LINCing Senescence and Nuclear Envelope Changes

Meqbel, B. R. M., Gomes, M., Omer, A., Gallouzi, I., & Horn, H. F. (2022) · Cells · doi:10.3390/cells11111787 · Cited by 23

Expression Profiling of Differentiating Emerin-Null Myogenic Progenitor Identifies Molecular Pathways Implicated in Their Impaired Differentiation

Iyer, A., Koch, A. J., & Holaska, J. M. (2017) · Cells · doi:10.3390/cells6040038 · Cited by 20

Comparative Interactome Analysis of Emerin, MAN1 and LEM2 Reveals a Unique Role for LEM2 in Nucleotide Excision Repair

Moser, B., Basílio, J., Gotzmann, J., Brachner, A., & Foisner, R. (2020) · Cells · doi:10.3390/cells9020463 · Cited by 20

Abnormal proliferation and spontaneous differentiation of myoblasts from a symptomatic female carrier of X-linked Emery–Dreifuss muscular dystrophy

Meinke, P., Schneiderat, P., Sršeň, V., Korfali, N., Thanh, P. L., Cowan, G. J. M., Cavanagh, D. R., Wehnert, M. S., Schirmer, E. C., & Walter, M. C. (2014) · Neuromuscular Disorders · doi:10.1016/j.nmd.2014.09.012 · Cited by 19

Accumulation of Progerin Affects the Symmetry of Cell Division and Is Associated with Impaired Wnt Signaling and the Mislocalization of Nuclear Envelope Proteins

Sola-Carvajal, A., Revêchon, G., Helgadottir, H. T., Whisenant, D., Hagblom, R., Döhla, J., Katajisto, P., Brodin, D., Fagerström‐Billai, F., Viceconte, N., et al. (2019) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2019.05.005 · Cited by 19

An Emerin LEM-Domain Mutation Impairs Cell Response to Mechanical Stress

Essawy, N. O. E., Samson, C., Petitalot, A., Moog, S., Bigot, A., Herrada, I., Marcelot, A., Arteni, A., Coirault, C., & Zinn‐Justin, S. (2019) · Cells · doi:10.3390/cells8060570 · Cited by 19

Using nuclear envelope mutations to explore age-related skeletal muscle weakness

Battey, E., Stroud, M. J., & Ochala, J. (2020) · Clinical Science · doi:10.1042/cs20190066 · Cited by 17

Feeling the force: Multiscale force sensing and transduction at the cell-cell interface

Inman, A., & Smutny, M. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.06.006 · Cited by 20

The scaffolding protein IQGAP1 co-localizes with actin at the cytoplasmic face of the nuclear envelope: implications for cytoskeletal regulation

Johnson, M. A., & Henderson, B. R. (2012) · BioArchitecture · doi:10.4161/bioa.21182 · Cited by 17

Matrix Remodeling Controls a Nuclear Lamin A/C-Emerin Network that Directs Wnt-Regulated Stem Cell Fate

Tang, Y., Zhu, L.-X., Cho, J., Li, X.-Y., & Weiss, S. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.01.015 · Cited by 13

The role of inner nuclear membrane proteins in tumourigenesis and as potential targets for cancer therapy

Rose, M., Burgess, J. T., O'Byrne, K. J., Richard, D. J., & Bolderson, E. (2022) · Cancer and Metastasis Reviews · doi:10.1007/s10555-022-10065-z · Cited by 15

Breaking the scale: how disrupting the karyoplasmic ratio gives cancer cells an advantage for metastatic invasion

Rizzotto, A., & Schirmer, E. C. (2017) · Biochemical Society Transactions · doi:10.1042/bst20170153 · Cited by 14

Control of nuclear β-dystroglycan content is crucial for the maintenance of nuclear envelope integrity and function

Vélez‐Aguilera, G., Gómez-López, J. D. D., Jiménez-Gutiérrez, G. E., Vásquez‐Limeta, A., Laredo-Cisneros, M. S., Gómez, P., Winder, S. J., & Cisneros, B. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.11.013 · Cited by 14

Chapter 7 Fraying at the Edge

Cohen, T. V., & Stewart, C. L. (2008) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)00607-8 · Cited by 14

Essential roles of LEM-domain protein MAN1 during organogenesis in Xenopus laevis and overlapping functions of emerin

Reil, M., & Dabauvalle, M. (2013) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2013.10.008 · Cited by 14

The epigenetics of nuclear envelope organization and disease

Schirmer, E. C. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.07.012 · Cited by 13

ISGylation of EMD promotes its interaction with PDHA to inhibit aerobic oxidation in lung adenocarcinoma

Zhang, C., Cui, J., Cao, L., Tian, X., Miao, Y., Wang, Y., Qiu, S., Guo, W., Ma, L., Xia, J., et al. (2022) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17536 · Cited by 13

Custos controls β-catenin to regulate head development during vertebrate embryogenesis

Komiya, Y., Mandrekar, N., Sato, A., Dawid, I. B., & Habas, R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414437111 · Cited by 13

The role of nesprins as multifunctional organizers in the nucleus and the cytoskeleton

Noegel, A. A., & Neumann, S. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110668 · Cited by 13

Mechanobiological Dynamics‐Inspired Mechanomodulatory Biomaterials

Yang, L., Jiang, P., Stein, J. B., Hou, Y., Zhou, C. W., Kang, H., & Lee, K. (2025) · Advanced Science · doi:10.1002/advs.202416992 · Cited by 14

Emerin interacts with histone methyltransferases to regulate repressive chromatin at the nuclear periphery

Marano, N., & Holaska, J. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1007120 · Cited by 12

Emerin deficiency drives MCF7 cells to an invasive phenotype

Hansen, E., Rolling, C., Wang, M., & Holaska, J. M. (2024) · Scientific Reports · doi:10.1038/s41598-024-70752-5 · Cited by 12

EDMD-Causing Emerin Mutant Myogenic Progenitors Exhibit Impaired Differentiation Using Similar Mechanisms

Iyer, A., & Holaska, J. M. (2020) · Cells · doi:10.3390/cells9061463 · Cited by 12

Trafficking of Adhesion and Growth Factor Receptors and Their Effector Kinases

Schoenherr, C., Frame, M. C., & Byron, A. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062559 · Cited by 11

The E3 SUMO ligase PIASγ is a novel interaction partner regulating the activity of diabetes associated hepatocyte nuclear factor-1α

Kaci, A., Keindl, M., Solheim, M. H., Njølstad, P. R., Bjørkhaug, L., & Aukrust, I. (2018) · Scientific Reports · doi:10.1038/s41598-018-29448-w · Cited by 12

The LINC Complex Assists the Nuclear Import of Mechanosensitive Transcriptional Regulators

Takata, T., & Matsumura, M. (2022) · Results and problems in cell differentiation · doi:10.1007/978-3-031-06573-6_11 · Cited by 11

Adipogenesis is under surveillance of Hsp90 and the high molecular weight Immunophilin FKBP51

Toneatto, J., Charó, N. L., Galigniana, N. M., & Piwien‐Pilipuk, G. (2015) · Adipocyte · doi:10.1080/21623945.2015.1049401 · Cited by 11

Laminopathies and A-type lamin-associated signalling pathways

Maraldi, N. M., Lattanzi, G., Cenni, V., Bavelloni, A., Marmiroli, S., & Manzoli, F. A. (2009) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2009.10.019 · Cited by 10

The Sky's the LEMit: New insights into nuclear structure regulation of transcription factor activity

Mirza, A., Gonzalez, F., Ha, S. K., & Oro, A. E. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.10.006 · Cited by 10

Proteogenomic Analysis Reveals Proteins Involved in the First Step of Adipogenesis in Human Adipose-Derived Stem Cells

Bonilauri, B., Camillo-Andrade, A. C., Santos, M. D. M., Fischer, J. D. S. D. G., Carvalho, P. C., & Dallagiovanna, B. (2021) · Stem Cells International · doi:10.1155/2021/3168428 · Cited by 10

Activation of the wnt/β-Catenin Signaling Pathway in Polymyositis, Dermatomyositis and Duchenne Muscular Dystrophy

Liu, F., Liang, Z., Xu, J., Li, W., Zhao, D., Zhao, Y., & Yan, C. (2016) · Journal of Clinical Neurology · doi:10.3988/jcn.2016.12.3.351 · Cited by 10

Emerin Represses STAT3 Signaling through Nuclear Membrane-Based Spatial Control

Lee, B., Lee, S., Lee, Y., Park, Y., & Shim, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136669 · Cited by 12

The role of inner nuclear membrane protein emerin in myogenesis

Marano, N., & Holaska, J. M. (2025) · The FASEB Journal · doi:10.1096/fj.202500323 · Cited by 9

Molecular and Mechanobiological Pathways Related to the Physiopathology of FPLD2

Varlet, A., Helfer, E., & Badens, C. (2020) · Cells · doi:10.3390/cells9091947 · Cited by 9

BCAP31 is involved in modulating colorectal cancer cell proliferation via the Emerin/β-catenin axis

Han, L., Shi, J., Zhao, L., Deng, J., Li, Y., Zhao, H., Wang, H., Yan, Y., & Zou, F. (2022) · Experimental Cell Research · doi:10.1016/j.yexcr.2022.113265 · Cited by 9

Semaphorin 3A promotes activation of Pax7, Myf5, and MyoD through inhibition of emerin expression in activated satellite cells

Qahar, M., Takuma, Y., Mizunoya, W., Tatsumi, R., Ikeuchi, Y., & Nakamura, M. (2016) · FEBS Open Bio · doi:10.1002/2211-5463.12050 · Cited by 9

The Integral Nuclear Membrane Protein Nurim Plays a Role in the Suppression of Apoptosis

Chen, H., Chen, K., Chen, J., Cheng, H., & Zhou, R. (2012) · Current Molecular Medicine · doi:10.2174/156652412803833571 · Cited by 9

Nuclear envelope influences on genome organization

Malik, P. R., Zuleger, N., & Schirmer, E. C. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380268 · Cited by 8

Nucleoskeleton dynamics and functions in health and disease

Schirmer, E. C., Meinke, P., Makarov, A. A., Thanh, P. L., & Sadurska, D. (2015) · Cell Health and Cytoskeleton · doi:10.2147/chc.s53821 · Cited by 8

Nucleo-cytoplasmic shuttling of the endonuclease ankyrin repeats and LEM domain-containing protein 1 (Ankle1) is mediated by canonical nuclear export- and nuclear import signals

Zlopaša, L., Brachner, A., & Foisner, R. (2016) · BMC Cell Biology · doi:10.1186/s12860-016-0102-z · Cited by 8

The Molecular Basis and Biologic Significance of the β-Dystroglycan-Emerin Interaction

Gómez-Monsivais, W. L., Monterrubio-Ledezma, F., Huerta-Cantillo, J., Mondragón-González, R., Alamillo‐Iniesta, A., García‐Aguirre, I., Azuara-Medina, P. M., Argüello-García, R., Rivera‐Monroy, J. E., Holaska, J. M., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21175944 · Cited by 7

Nuclear stiffness through lamin A/C overexpression differentially modulates chromosomal instability biomarkers

Bosch‐Calvet, M., Pérez‐Venteo, A., Cebria‐Xart, A., Garcia‐Cajide, M., & Mauvezin, C. (2025) · Biology of the Cell · doi:10.1111/boc.12001 · Cited by 6

Lamin regulates the dietary restriction response via the mTOR pathway in Caenorhabditis elegans

Charar, C., Metsuyanim-Cohen, S., Gruenbaum, Y., & Bar, D. Z. (2021) · Journal of Cell Science · doi:10.1242/jcs.258428 · Cited by 5

Regulation of Nucleocytoplasmic Transport in Skeletal Muscle

Hall, M. N., Corbett, A. H., & Pavlath, G. K. (2011) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/b978-0-12-385940-2.00010-3 · Cited by 6

Role of structural flexibility in the evolution of emerin

Jia, Y., & Xue, B. (2015) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2015.08.009 · Cited by 6

Nuclear envelope influences on cell-cycle progression

Sršeň, V., Korfali, N., & Schirmer, E. C. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110656 · Cited by 6

Nuclear–Centrosome Relationships During Fertilization, Cell Division, Embryo Development, and in Somatic Cell Nuclear Transfer Embryos

Schatten, H., & Sun, Q. (2012) · Humana Press eBooks · doi:10.1007/978-1-62703-035-9_4 · Cited by 6

Emerin induces nuclear breakage inXenopusextract and early embryos

Dilsaver, M. R., Chen, P., Thompson, T. A., Reusser, T., Mukherjee, R. N., Oakey, J. S., & Levy, D. L. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-05-0277 · Cited by 6

Molecular Genetics of Emery–Dreifuss Muscular Dystrophy

Morris, G. E., Sewry, C. A., & Wehnert, M. S. (2010) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0022438 · Cited by 6

Lamin A K97E leads to NF‐κB‐mediated dysfunction of inflammatory responses in dilated cardiomyopathy

Sengupta, D., & Sengupta, K. (2024) · Biology of the Cell · doi:10.1111/boc.202300094 · Cited by 5

Emery-Dreifuss Muscular Dystrophy

Merlini, L., & Maraldi, N. M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6567-6_61 · Cited by 5

Workshop on the nuclear envelope and Emery–Dreifuss muscular dystrophy 29th March 2006, Oswestry, UK

Randles, K. N., & Morris, G. E. (2006) · Neuromuscular Disorders · doi:10.1016/j.nmd.2006.07.016 · Cited by 5

Diseases of the Nucleoskeleton

Holaska, J. M. (2016) · Comprehensive physiology · doi:10.1002/cphy.c150039 · Cited by 5

Diseases of the Nucleoskeleton

Holaska, J. M. (2016) · Comprehensive physiology · doi:10.1002/j.2040-4603.2016.tb00721.x · Cited by 4

The inner nuclear membrane protein, Banf1, has an essential role in triple negative breast cancer cell proliferation and survival

Rose, M., Burgess, J. T., Cheong, C. M., Richard, I. A., Suraweera, A., Adams, M. N., Duijf, P. H. G., O'Byrne, K. J., Richard, D. J., & Bolderson, E. (2025) · Scientific Reports · doi:10.1038/s41598-025-10346-x · Cited by 3

Nuclear β-catenin: molecular regulation, challenges and therapeutic opportunities

Xie, B., Cao, Y., Li, W., Chen, R., Zhou, Q., & Xie, X. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02600-6 · Cited by 4

The Nuclear Envelope in Cardiac Health and Disease

Brayson, D., & Shanahan, C. M. (2015) · Springer eBooks · doi:10.1007/978-3-319-15263-9_9 · Cited by 3

NETs and Cell Cycle Regulation

Robson, M. I., Thanh, P. L., & Schirmer, E. C. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-8032-8_8 · Cited by 3

Molecular simulation investigation on the interaction between barrier-to-autointegration factor dimer or its Gly25Glu mutant and LEM domain of emerin

Shang, Y., Zhang, J., Wang, Y., Zhang, H., & Zheng, Q. (2014) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2014.09.007 · Cited by 3

Multiple and surprising new functions for emerin, a nuclear membrane protein

Bengtsson, L., & Wilson, K. L. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.11.012 · Cited by 132

The nuclear envelope LEM-domain protein emerin

Berk, J. M., Tifft, K. E., & Wilson, K. L. (2013) · Nucleus · doi:10.4161/nucl.25751 · Cited by 186

Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PLoS Biol

Holaska, J. M., Kowalski, A. K., & Wilson, K. L. (2004)

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

A-type lamins anchor emerin at the inner nuclear membrane via two independent binding sites

Odell, J., Nedza, K., & Lammerding, J. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111192 · Cited by 2