about
Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membraneEmerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophyIdentification of an NTF2-related factor that binds Ran-GTP and regulates nuclear protein export.Emerin interacts in vitro with the splicing-associated factor, YT521-BDNA binding domains in diverse nuclear receptors function as nuclear export signals.The use of permeabilized cell systems to study nuclear transport.Ca2+-dependent nuclear export mediated by calreticulin.A cytosolic activity distinct from crm1 mediates nuclear export of protein kinase inhibitor in permeabilized cells.An emerin "proteome": purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture.MAPK signaling pathways and HDAC3 activity are disrupted during differentiation of emerin-null myogenic progenitor cells.Loss of emerin alters myogenic signaling and miRNA expression in mouse myogenic progenitors.Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes.The nuclear envelope, lamins and nuclear assembly.Emerin in health and disease.Nuclear membrane protein emerin: roles in gene regulation, actin dynamics and human disease.Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis.Emerin and the nuclear lamina in muscle and cardiac disease.Disruption of nesprin-1 produces an Emery Dreifuss muscular dystrophy-like phenotype in mice.Diseases of the Nucleoskeleton.Emerin inhibits Lmo7 binding to the Pax3 and MyoD promoters and expression of myoblast proliferation genes.Disruption of the lamin A and matrin-3 interaction by myopathic LMNA mutations.Expression Profiling of Differentiating Emerin-Null Myogenic Progenitor Identifies Molecular Pathways Implicated in Their Impaired Differentiation.LMO7-null mice exhibit phenotypes consistent with emery-dreifuss muscular dystrophy.Histone acetyltransferase inhibition rescues differentiation of emerin-deficient myogenic progenitorsEDMD-Causing Emerin Mutant Myogenic Progenitors Exhibit Impaired Differentiation Using Similar Mechanisms
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Q24301949-752282AE-90BA-4F73-872D-C2E48CB604F2Q24315475-83429D4C-ED8C-453B-A16B-C3A0BA4E7588Q24554370-56A85847-FD53-4F9C-9FE0-8A2D0789E3AAQ28205048-3B4DF290-5936-41CF-A0F5-4A80B4B583CDQ30308287-FBCE0237-EB2D-4164-92A3-E67DAC26835FQ30309597-084B2018-7781-477D-B26D-E280EE0C966BQ30309755-2A9B1675-055D-4EB5-A68A-F67A46D70988Q30454343-AB957222-B152-49FF-8250-B50B9EB5FB7CQ33290327-F3EAF654-5533-4BE4-B9CD-3653EF1A7BA9Q33588122-08A91317-38D4-4D91-8A0B-EEAD84F74EDBQ34273959-8BA11E10-B83E-48B3-8B64-7B748466E93BQ34577033-364AB424-D835-4772-8A44-E61031068C38Q34688457-1213A2E7-AF30-4E10-AD03-819734E16335Q35259539-1D7E62AD-8E93-40C5-9759-D4377F240CCAQ36073086-B3D54524-74A3-4F38-A037-ECF898EF8FBCQ36791375-62EBCA5D-41A7-4B5D-98AF-45CF6B5F83F2Q37205487-6F70D9E4-7D48-4747-A07D-CE087177CCF7Q37292920-89F25167-22AE-4787-8AF4-3854F12E84A5Q38991463-C4EFFF63-F211-4702-ABB0-1BEF05C99DDCQ39551962-A71513B4-8614-4DB7-90B2-97A35E8F34C7Q41374034-7B7231BF-5271-453B-802D-0CB71372B370Q47170895-C44B4FE1-57B6-4048-9265-4FF586AE4A46Q54352897-E99954AD-EFCA-452F-9507-D135EA855678Q92029128-F211C5F6-2480-46E8-BD84-9AE3B8158749Q96438213-A1A99E84-AD9A-40F2-BAF0-60488970D923
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
James M Holaska
@ast
James M Holaska
@en
James M Holaska
@es
James M Holaska
@nl
type
label
James M Holaska
@ast
James M Holaska
@en
James M Holaska
@es
James M Holaska
@nl
prefLabel
James M Holaska
@ast
James M Holaska
@en
James M Holaska
@es
James M Holaska
@nl
P108
P106
P21
P31
P496
0000-0003-0273-9995