Results 11 to 20 of about 4,186 (177)

Emerin increase in regenerating muscle fibers

European Journal of Histochemistry, 2009
The fate of emerin during skeletal muscle regeneration was investigated in an animal model by means of crush injury. Immunofluorescence, immunoblotting and mRNA analysis demonstrated that emerin level is increased in regenerating rat muscle fibers with ...
S Squarzoni, P Sabatelli, C Capanni, G Lattanzi, C Rutigliano, M Columbaro   +5 more
doaj   +8 more sources

Emerin expression in tubular aggregates

Acta Neuropathologica, 2004
Emerin is an inner nuclear membrane protein that is mutated or not expressed in patients with X-linked Emery-Dreifuss muscular dystrophy (X-EDMD/EMD). Cytoplasmic localization of emerin in cultured cells or tissues has been reported, although this remains a controversial issue. Tubular aggregates (TAs) are pathological structures seen in the sarcoplasm
Manta, P., Terzis, G., Papadimitriou, C., Kontou, C., Vassilopoulos, D.   +4 more
core   +5 more sources

Emerin self‐assembly mechanism: role of the LEM domain [PDF]

The FEBS Journal, 2017
At the nuclear envelope, the inner nuclear membrane protein emerin contributes to the interface between the nucleoskeleton and the chromatin. Emerin is an essential actor of the nuclear response to a mechanical signal. Genetic defects in emerin cause Emery–Dreifuss muscular dystrophy. It was proposed that emerin oligomerization regulates nucleoskeleton
Samson, Camille, Celli, Florian, Hendriks, Kitty, Zinke, Maximilian, Essawy, Nada, Herrada, Isaline, Arteni, Ana‐andreea, Theillet, Francois-Xavier, Alpha‐bazin, Béatrice, Armengaud, J., Coirault, Catherine, Lange, Adam, Zinn‐Justin, Sophie   +12 more
openaire   +4 more sources

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

International Journal of Molecular Sciences, 2020
β-dystroglycan (β-DG) assembles with lamins A/C and B1 and emerin at the nuclear envelope (NE) to maintain proper nuclear architecture and function. To provide insight into the nuclear function of β-DG, we characterized the interaction between β-DG and emerin at the molecular level. Emerin is a major NE protein that regulates multiple nuclear processes
Gómez-Monsivais, Wendy Lilián, Monterrubio-Ledezma, Feliciano, Huerta-Cantillo, Jazmin, Mondragon-Gonzalez, Ricardo, Alamillo-Iniesta, Alma, García-Aguirre, Ian, Azuara-Medina, Paulina Margarita, Arguello-García, Raúl, Rivera-Monroy, Jhon Erick, Holaska, James M., Hernández-Méndez, Jesús Mauricio Ernesto, Garrido, Efraín, Magaña, Jonathan Javier, Winder, Steve J., Brancaccio, Andrea, Martínez-Vieyra, Ivette, Navarro-Garcia, Fernando, Cisneros, Bulmaro, Gómez-Monsivais, Wendy Lilián; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, wlgomez@cinvestav.mx, Monterrubio-Ledezma, Feliciano; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, eduardo.monterrubio@cinvestav.mx, Huerta-Cantillo, Jazmin; Cell Biology Department, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, jazmin.huerta@cinvestav.mx, Mondragon-Gonzalez, Ricardo; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, rmondragon90@gmail.com, Alamillo-Iniesta, Alma; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, aalamilloi@cinvestav.mx, García-Aguirre, Ian; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, ian.garcia@cinvestav.mx, Azuara-Medina, Paulina Margarita; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, pauazmd@gmail.com, Arguello-García, Raúl; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, rag@cinvestav.mx, Rivera-Monroy, Jhon Erick; Department of Molecular Biology, Faculty of Medicine, GZMB, Georg-August University, 37073 Göttingen, Germany, jhonriv@gmail.com Laboratorio Instrumental de Alta Complejidad, Universidad de La Salle, 111311 Bogotá, Colombia, jhonriv@gmail.com, Holaska, James M.; Department of Biomedical Sciences, Cooper Medical School of Rowan University, 401 S Broadway, Camden, NJ 08028, USA, holaska@rowan.edu, Hernández-Méndez, Jesús Mauricio Ernesto; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, mauriciohermen91@hotmail.com, Garrido, Efraín; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, egarrido@cinvestav.mx, Magaña, Jonathan Javier; Laboratory of Genomic Medicine, Department of Genetics, National Rehabilitation Institute-Luis Guillermo Ibarra Ibarra (INR-LGII), 14389 Mexico City, Mexico, magana.jj@tec.mx Departamento de Bioingeniería, Escuela de Ingeniería y Ciencias, Instituto Tecnológico y de Estudios Superiores de Monterrey-Campus Ciudad de México, 14380 Ciudad de México, Mexico, magana.jj@tec.mx, Winder, Steve J.; Department of Biomedical Science, University of Sheffield, Western Bank, Sheffield S10 2TN, UK, s.winder@sheffield.ac.uk, Brancaccio, Andrea; School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK, andrea.brancaccio@cnr.it Institute of Chemical Sciences and Technologies “Giulio Natta” (SCITEC), 00168 Roma, Italy, andrea.brancaccio@cnr.it, Martínez-Vieyra, Ivette; Laboratory of Hematobiology, Escuela Nacional de Medicina y Homeopatía, Instituto Politécnico Nacional, 07320 Ciudad de México, Mexico, ivette0381@yahoo.com.mx, Navarro-Garcia, Fernando; Cell Biology Department, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, enavarro@cinvestav.mx, Cisneros, Bulmaro; Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), 07360 Mexico City, Mexico, bcisnero@cinvestav.mx   +35 more
openaire   +11 more sources

Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope [PDF]

Physical Review Research
Emerin, a nuclear membrane protein with important biological roles in mechanotransduction and nuclear shape adaptation, self-assembles into nanometer-size domains at the inner nuclear membrane.
Carlos D. Alas, Liying Wu, Fabien Pinaud, Christoph A. Haselwandter   +3 more
doaj   +3 more sources

Development of Emerin mRNA Lipid Nanoparticles to Rescue Myogenic Differentiation. [PDF]

Int J Mol Sci
Emery–Dreifuss muscular dystrophy 1 (EDMD1) arises from mutations in EMD. Most EDMD1 patients lack detectable emerin expression. They experience symptoms such as skeletal muscle wasting, joint contractures, and cardiac conduction defects. Currently, physicians rely on treating patient symptoms without addressing the underlying cause—lack of functional ...
Marano N, Guner LE, Riley RS, Holaska JM.   +3 more
europepmc   +5 more sources

Temporal Stretch-Induced Nuclear Mechanosensing Coordinates Early Chromatin Accessibility and Genome Protection. [PDF]

Adv Sci (Weinh)
Cyclic stretching of fibroblasts triggers coordinated nuclear mechanosensing events, including calcium ion release, perinuclear actin assembly, emerin translocation, and H3K9me3 loss, increasing chromatin accessibility for specific genes related to mechanotransduction and repair.
Shim HW, Yoon JY, Lee H, Karunasagara S, Li CJ, Shin Y, Hong S, Lee DJ, Lee JH, Leong KW, Kim HW.   +10 more
europepmc   +2 more sources

ERM proteins support perinuclear actin rim formation [PDF]

Frontiers in Cell and Developmental Biology
The interaction of actin filaments with the nuclear envelope is essential for diverse cellular processes, including cell migration, nuclear positioning, and transcriptional control.
Yuval Hadad, Andrea Fracchia, Dagmawit Babele, Amit Ben Shushan, Gabi Gerlitz   +4 more
doaj   +2 more sources

Mechanical-biochemical signaling accelerates scleral remodeling in myopia via the LaminA/C-Emerin-MKL1 axis [PDF]

Cell Communication and Signaling
Scleral remodeling is the pathological basis of axial elongation during the progression of myopia. However, the mechanism underlying the onset and progression of scleral remodeling remains unclear.
Yuying Liu, Xin Liu, Mingming Liu, Xuetong Wang, Wenzhe Qian, Ting Zhao, Min Li, Bilian Ke   +7 more
doaj   +2 more sources

The Role of HOP in Emerin-Mediated Nuclear Structure [PDF]

, 2021
A vital component of the integral nuclear membrane is emerin, a Lamin Emerin and Man1 (LEM) domain protein whose concentration determines the levels of partner proteins that together constitute the structure of the nuclear envelope. Deficiencies in any of these proteins causes the failure of the structure and assembly and disassembly of the nuclear ...
Kituyi, Sarah Naulikha
openaire   +2 more sources