Results 31 to 40 of about 158,042 (243)
Structural Basis for Capsid Recruitment and Coat Formation during HSV-1 Nuclear Egress
Proceedings, 2020 During herpesvirus infection, nascent viral capsids egress the nucleus into the cytoplasm by an unusual mechanism whereby capsids bud at the inner nuclear membrane.
Elizabeth Draganova +3 more
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Viruses, 2015 Herpes simplex virus 1 (HSV-1) capsids are assembled in the nucleus bud at the inner nuclear membrane into the perinuclear space, acquiring envelope and tegument. In theory, these virions are de-enveloped by fusion of the envelope with the outer nuclear
Peter Wild +6 more
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Generating Membrane Curvature at the Nuclear Pore: A Lipid Point of View
Cells, 2022 In addition to its structural role in enclosing and protecting the genome, the nuclear envelope (NE) forms a highly adaptive communication interface between the cytoplasm and the nuclear interior in eukaryotic cells.
Bas W. A. Peeters +2 more
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A transmembrane inner nuclear membrane protein in the mitotic spindle [PDF]
Nucleus, 2010 We have recently characterized a novel transmembrane protein of the inner nuclear membrane of mammalian cells. The protein has two very interesting features. First, despite being an integral membrane protein it is able to concentrate in the membranes colocalizing with the mitotic spindle in metaphase and anaphase.
Ricardo, Figueroa +3 more
openaire +2 more sources
PLoS Genetics, 2014 Recent interest has focused on the importance of the nucleus and associated nucleoskeleton in regulating changes in cardiac gene expression in response to biomechanical load.
Indroneal Banerjee +11 more
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Targeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear Membrane. [PDF]
Int J Mol Sci, 2019 LRRC59 (leucine-rich repeat-containing protein 59) is a tail-anchored protein with a single transmembrane domain close to its C-terminal end that localizes to the endoplasmic reticulum (ER) and the nuclear envelope. Here, we investigate the mechanisms of membrane integration of LRRC59 and its targeting to the inner nuclear membrane (INM).
Blenski M, Kehlenbach RH.
europepmc +6 more sources
PLoS Biology, 2004 X-linked Emery-Dreifuss muscular dystrophy is caused by loss of emerin, a LEM-domain protein of the nuclear inner membrane. To better understand emerin function, we used affinity chromatography to purify emerin-binding proteins from nuclear extracts of ...
James M Holaska +2 more
doaj +1 more source
The SUN protein Mps3 is required for spindle pole body insertion into the nuclear membrane and nuclear envelope homeostasis. [PDF]
PLoS Genetics, 2011 The budding yeast spindle pole body (SPB) is anchored in the nuclear envelope so that it can simultaneously nucleate both nuclear and cytoplasmic microtubules. During SPB duplication, the newly formed SPB is inserted into the nuclear membrane.
Jennifer M Friederichs +9 more
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Sun2 Is a Novel Mammalian Inner Nuclear Membrane Protein [PDF]
Journal of Biological Chemistry, 2004 Sun protein (Sun1 and Sun2) cDNAs were previously cloned based on the homology of their C-terminal regions (SUN (Sad1 and UNC) domain) with the Caenorhabditis elegans protein UNC-84 whose mutation disrupts nuclear migration/positioning. In this study, we raised an anti-Sun2 serum and identified Sun2 in mammalian cells.
Didier M, Hodzic +4 more
openaire +2 more sources
STAR Protocols, 2021 Summary: Single-molecule fluorescence recovery after photobleaching (smFRAP) is a newly developed technique that combines single-molecule super-resolution microscopy and traditional FRAP microscopy.
Mark Tingey, Yichen Li, Weidong Yang
doaj +1 more source