Results 21 to 30 of about 6,268 (192)
Mutations in the gene encoding emerin (EMD) cause Emery–Dreifuss muscular dystrophy (EDMD1), an inherited disorder characterized by progressive skeletal muscle wasting, irregular heart rhythms and contractures of major tendons.
Ashvin Iyer, James M. Holaska
doaj +1 more source
Emerin—prelamin A interplay in human fibroblasts [PDF]
Background information. Emerin is a nuclear envelope protein that contributes to nuclear architecture, chromatin structure, and gene expression through its interaction with various nuclear proteins. In particular, emerin is molecularly connected with the nuclear lamina, a protein meshwork composed of lamins and lamin‐binding proteins underlying the ...
Capanni C +9 more
openaire +3 more sources
Chromosome positioning is largely unaffected in lymphoblastoid cell lines containing emerin or A-type lamin mutations [PDF]
Gene-poor human chromosomes are reproducibly found at the nuclear periphery in proliferating cells. There are a number of inner nuclear envelope proteins that may have roles in chromosome location and anchorage, e.g. emerin and A-type lamins.
Bridger, JM +3 more
core +1 more source
Emerin is an essential LEM (LAP2, Emerin, MAN1) domain protein in metazoans and an integral membrane protein associated with inner and outer nuclear membranes.
Magda Dubińska-Magiera +5 more
doaj +1 more source
Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes [PDF]
X-linked Emery-Dreifuss muscular dystrophy (X-EDMD) is inherited through mutations in emerin, a nuclear membrane protein. Emerin has proposed roles in nuclear architecture and gene regulation, but direct molecular links to disease were unknown. We report that Lim-domain only 7 (Lmo7) binds emerin directly with 125 nM affinity; the C-terminal half of ...
James M, Holaska +2 more
openaire +2 more sources
Emerin Deregulation Links Nuclear Shape Instability to Metastatic Potential [PDF]
Abstract Abnormalities in nuclear shape are a well-known feature of cancer, but their contribution to malignant progression remains poorly understood. Here, we show that depletion of the cytoskeletal regulator, Diaphanous-related formin 3 (DIAPH3), or the nuclear membrane–associated proteins, lamin A/C, in prostate and breast cancer ...
Mariana Reis-Sobreiro +19 more
openaire +3 more sources
An Emerin LEM-Domain Mutation Impairs Cell Response to Mechanical Stress
Emerin is a nuclear envelope protein that contributes to genome organization and cell mechanics. Through its N-terminal LAP2-emerin-MAN1 (LEM)-domain, emerin interacts with the DNA-binding protein barrier-to-autointegration (BAF).
Nada Essawy +9 more
doaj +1 more source
LAP2-Emerin-MAN1 (LEM) domain-containing proteins represent an abundant group of inner nuclear membrane proteins involved in diverse nuclear functions, but their functional redundancies remain unclear.
Bernhard Moser +4 more
doaj +1 more source
Background: The nuclear laminar protein Lamin A and inner nuclear membrane protein Emerin plays important role in sustaining nuclear structure. However, They have not investigated the significance of these proteins for development of pancreatic ...
Tamaki Hiroe +8 more
doaj +1 more source
Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly [PDF]
During mitosis, the nuclear envelope merges with the endoplasmic reticulum (ER), and nuclear pore complexes are disassembled. In a current model for reassembly after mitosis, the nuclear envelope forms by a reshaping of ER tubules.
Anderson +48 more
core +4 more sources

