Autoantibodies to Nuclear Envelope Proteins: Characterization and Clinical Significance

1989 ◽  
pp. 5-7
Author(s):  
J. C. Courvalin ◽  
M.-N. Guilly ◽  
F. Danon ◽  
Ch. André ◽  
J.-C. Brouet ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Clinical Significance ◽  
Envelope Proteins

Nuclear envelope proteins from Spisula solidissima germinal vesicles

1980 ◽  
Vol 130 (1) ◽  
pp. 229-240 ◽  
Author(s):  
Gerd G. Maul ◽  
Nebojŝa Avdalović
Keyword(s):  
Nuclear Envelope ◽  
Envelope Proteins ◽  
Spisula Solidissima ◽  
Germinal Vesicles

scholarly journals Challenges and Opportunities for Characterizing the Assembly of Nuclear Envelope Proteins by Fluorescence Fluctuation Spectroscopy

2019 ◽  
Vol 116 (3) ◽  
pp. 279a
Author(s):  
Jared Hennen ◽  
Kwang Ho Hur ◽  
John Kohler ◽  
G.W. Gant Luxton ◽  
Joachim D. Mueller
Keyword(s):  
Nuclear Envelope ◽  
Envelope Proteins ◽  
Fluorescence Fluctuation Spectroscopy ◽  
Challenges And Opportunities

scholarly journals Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins

2012 ◽  
Vol 24 (6) ◽  
pp. 775-783 ◽  
Author(s):  
J Sebastian Gomez-Cavazos ◽  
Martin W Hetzer
Keyword(s):  
Nuclear Envelope ◽  
Envelope Proteins ◽  
Tissue Specific

scholarly journals Homozygous Defects in LMNA, Encoding Lamin A/C Nuclear-Envelope Proteins, Cause Autosomal Recessive Axonal Neuropathy in Human (Charcot-Marie-Tooth Disorder Type 2) and Mouse

2002 ◽  
Vol 70 (3) ◽  
pp. 726-736 ◽  
Author(s):  
Annachiara De Sandre-Giovannoli ◽  
Malika Chaouch ◽  
Serguei Kozlov ◽  
Jean-Michel Vallat ◽  
Meriem Tazir ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Autosomal Recessive ◽  
Axonal Neuropathy ◽  
Envelope Proteins ◽  
Lamin A ◽  
Charcot Marie Tooth ◽  
Disorder Type

scholarly journals Analysis of RNA-Seq datasets reveals enrichment of tissue-specific splice variants for nuclear envelope proteins

Nucleus ◽  
2018 ◽  
Vol 9 (1) ◽  
pp. 410-430 ◽  
Author(s):  
Charlotte Capitanchik ◽  
Charles R. Dixon ◽  
Selene K. Swanson ◽  
Laurence Florens ◽  
Alastair R. W. Kerr ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Splice Variants ◽  
Envelope Proteins ◽  
Rna Seq ◽  
Tissue Specific

scholarly journals A network of nuclear envelope proteins and cytoskeletal force generators mediates movements of and within nuclei throughout Caenorhabditis elegans development

2019 ◽  
Vol 244 (15) ◽  
pp. 1323-1332 ◽  
Author(s):  
Daniel A Starr
Keyword(s):  
Dna Damage ◽  
Caenorhabditis Elegans ◽  
Nuclear Envelope ◽  
Nuclear Membrane ◽  
Dna Damage Repair ◽  
Nuclear Migration ◽  
Envelope Proteins ◽  
Nuclear Positioning ◽  
C Elegans ◽  
Damage Repair

Nuclear migration and anchorage, together referred to as nuclear positioning, are central to many cellular and developmental events. Nuclear positioning is mediated by a conserved network of nuclear envelope proteins that interacts with force generators in the cytoskeleton. At the heart of this network are linker of nucleoskeleton and cytoskeleton (LINC) complexes made of Sad1 and UNC-84 (SUN) proteins at the inner nuclear membrane and Klarsicht, ANC-1, and Syne homology (KASH) proteins in the outer nuclear membrane. LINC complexes span the nuclear envelope, maintain nuclear envelope architecture, designate the surface of nuclei distinctly from the contiguous endoplasmic reticulum, and were instrumental in the early evolution of eukaryotes. LINC complexes interact with lamins in the nucleus and with various cytoplasmic KASH effectors from the surface of nuclei. These effectors regulate the cytoskeleton, leading to a variety of cellular outputs including pronuclear migration, nuclear migration through constricted spaces, nuclear anchorage, centrosome attachment to nuclei, meiotic chromosome movements, and DNA damage repair. How LINC complexes are regulated and how they function are reviewed here. The focus is on recent studies elucidating the best-understood network of LINC complexes, those used throughout Caenorhabditis elegans development. Impact statement Defects in nuclear positioning disrupt development in many mammalian tissues. In human development, LINC complexes play important cellular functions including nuclear positioning, homolog pairing in meiosis, DNA damage repair, wound healing, and gonadogenesis. The topics reviewed here are relevant to public health because defects in nuclear positioning and mutations in LINC components are associated with a wide variety of human diseases including muscular dystrophies, neurological disorders, progeria, aneurysms, hearing loss, blindness, sterility, and multiple cancers. Although this review focuses on findings in the model nematode Caenorhabditis elegans, the studies are relevant because almost all the findings originally made in C. elegans are conserved to humans. Furthermore, C. elegans remains the best described network for how LINC complexes are regulated and function.

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