Associated Papers
A scalable approach to resolving variants of uncertain significance.
Tejura M et al.
Biorxiv : the Preprint Server for Biology, 2026
The role of inner nuclear membrane protein emerin in myogenesis.
Marano N et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2025
Emerin interacts with histone methyltransferases to regulate repressive chromatin at the nuclear periphery.
Marano N et al.
Frontiers in Cell and Developmental Biology, 2022
The Role of Emerin in Cancer Progression and Metastasis.
Liddane AG et al.
International Journal of Molecular Sciences, 2021
EDMD-Causing Emerin Mutant Myogenic Progenitors Exhibit Impaired Differentiation Using Similar Mechanisms.
Iyer A et al.
Cells, 2020
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Fragoza R et al.
Nature Communications, 2019
An Emerin LEM-Domain Mutation Impairs Cell Response to Mechanical Stress.
Essawy N et al.
Cells, 2019
Capturing variation impact on molecular interactions in the IMEx Consortium mutations data set.
Del-Toro N et al.
Nature Communications, 2019
Emerin self-assembly mechanism: role of the LEM domain.
Samson C et al.
The Febs Journal, 2017
The nuclear lamina in health and disease.
Dobrzynska A et al.
Nucleus (austin, Tex.), 2016
Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties.
Herrada I et al.
Acs Chemical Biology, 2015
Role of structural flexibility in the evolution of emerin.
Yuan J et al.
Journal of Theoretical Biology, 2015
Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations.
Holehouse AS et al.
Plos One, 2015
The molecular basis of emerin-emerin and emerin-BAF interactions.
Berk JM et al.
Journal of Cell Science, 2014
Emerin in health and disease.
Koch AJ et al.
Seminars in Cell & Developmental Biology, 2014
O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
Berk JM et al.
The Journal of Biological Chemistry, 2013
The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity.
Demmerle J et al.
The Journal of Biological Chemistry, 2012
Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation.
Wheeler MA et al.
Cellular and Molecular Life Sciences : Cmls, 2010
The nuclear envelopathies and human diseases.
Chi YH et al.
Journal of Biomedical Science, 2009
Tyrosine phosphorylation of nuclear-membrane protein emerin by Src, Abl and other kinases.
Tifft KE et al.
Journal of Cell Science, 2009
Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases.
Ryu GM et al.
Nucleic Acids Research, 2009
Emerin and the nuclear lamina in muscle and cardiac disease.
Holaska JM
Circulation Research, 2008
Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy.
Wheeler MA et al.
Experimental Cell Research, 2007
Proteins that associate with lamins: many faces, many functions.
Schirmer EC et al.
Experimental Cell Research, 2007
Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes.
Holaska JM et al.
Human Molecular Genetics, 2006
The Emery-Dreifuss muscular dystrophy associated-protein emerin is phosphorylated on serine 49 by protein kinase A.
Roberts RC et al.
The Febs Journal, 2006
Identification of tyrosine-phosphorylation sites in the nuclear membrane protein emerin.
Schlosser A et al.
The Febs Journal, 2006
Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane.
Holaska JM et al.
Plos Biology, 2004
Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy.
Haraguchi T et al.
European Journal of Biochemistry, 2004
Multiple and surprising new functions for emerin, a nuclear membrane protein.
Bengtsson L et al.
Current Opinion in Cell Biology, 2004
Emerin interacts in vitro with the splicing-associated factor, YT521-B.
Wilkinson FL et al.
European Journal of Biochemistry, 2003
Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro.
Holaska JM et al.
The Journal of Biological Chemistry, 2003
The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype.
Fairley EA et al.
Journal of Cell Science, 2002
Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF.
Lee KK et al.
Journal of Cell Science, 2001
The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane.
Fairley EA et al.
Journal of Cell Science, 1999
Heart to heart: from nuclear proteins to Emery-Dreifuss muscular dystrophy.
Morris GE et al.
Human Molecular Genetics, 1999
The nuclear envelope LEM-domain protein emerin.
Berk JM et al.
Nucleus (austin, Tex.), 0