Nuclear Pore Complex Proteins in Alzheimer Disease [PDF]
Journal of Neuropathology and Experimental Neurology, 2006 Ultrastructural studies of neurofibrillary tangles in Alzheimer disease (AD) have demonstrated a close relationship between nuclear pores and the cytoplasmic paired helical filaments comprising the tangles, as well as nuclear irregularity in many tangle-bearing neurons; nuclear pore aggregation has been observed in nearby neurons.
Lynette G, Sheffield +3 more
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Weaving a pattern from disparate threads: lamin function in nuclear assembly and DNA replication [PDF]
, 1994 The major residual structure that remains associated with the nuclear envelope following extraction of isolated nuclei or oocyte germinal vesicles with non-ionic detergents, nucleases and high salt is the lamina (Fawcett, 1966; Aaronson and Blobel ...
Hutchison, CJ +3 more
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A complex of nuclear pore proteins required for pore function. [PDF]
The Journal of cell biology, 1991 A family of proteins bearing novel N-acetylglucosamine residues has previously been found to be required to form functional nuclear pores. To begin to determine which of the proteins in this family are essential for pore function, antisera were raised to each of three members of the family, p62, p58, and p54.
D R, Finlay +4 more
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The Nuclear Pore Complex Is a Key Target of Viral Proteases to Promote Viral Replication
Viruses, 2021 Various viruses alter nuclear pore complex (NPC) integrity to access the nuclear content favoring their replication. Alteration of the nuclear pore complex has been observed not only in viruses that replicate in the nucleus but also in viruses with a ...
Luis Adrián De Jesús-González +7 more
doaj +1 more source
Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure. [PDF]
PLoS ONE, 2014 DNAJB12 and DNAJB14 are transmembrane proteins in the endoplasmic reticulum (ER) that serve as co-chaperones for Hsc70/Hsp70 heat shock proteins. We demonstrate that over-expression of DNAJB12 or DNAJB14 causes the formation of elaborate membranous ...
Edward C Goodwin +4 more
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Types of nuclear localization signals and mechanisms of protein import into the nucleus
Cell Communication and Signaling, 2021 Nuclear localization signals (NLS) are generally short peptides that act as a signal fragment that mediates the transport of proteins from the cytoplasm into the nucleus.
Juane Lu +6 more
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Deciphering Networks of Protein Interactions at the Nuclear Pore Complex [PDF]
Molecular & Cellular Proteomics, 2002 The nuclear pore complex (NPC) gates the only known conduit for molecular exchange between the nucleus and cytoplasm of eukaryotic cells. Macromolecular transport across the NPC is mediated by nucleocytoplasmic shuttling receptors termed karyopherins (Kaps).
Nadia P C, Allen +7 more
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Mitogen activated protein kinase at the nuclear pore complex [PDF]
Journal of Cellular and Molecular Medicine, 2011 Mitogen activated protein (MAP) kinases control eukaryotic proliferation, and import of kinases into the nucleus through the nuclear pore complex (NPC) can influence gene expression to affect cellular growth, cell viability and homeostatic function. The NPC is a critical regulatory checkpoint for nucleocytoplasmic traffic that regulates gene expression
Faustino, Randolph S +2 more
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Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore [PDF]
, 2004 Resident integral proteins of the inner nuclear membrane (INM) are synthesized as membrane-integrated proteins on the peripheral endoplasmic reticulum (ER) and are transported to the INM throughout interphase using an unknown trafficking mechanism.
Gerace, Larry +7 more
core +1 more source
Herpesvirus Nuclear Egress across the Outer Nuclear Membrane
Viruses, 2021 Herpesvirus capsids are assembled in the nucleus and undergo a two-step process to cross the nuclear envelope. Capsids bud into the inner nuclear membrane (INM) aided by the nuclear egress complex (NEC) proteins UL31/34.
Richard J. Roller, David C. Johnson
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