Results 21 to 30 of about 173,033 (291)

Relocation of Collapsed Forks to the Nuclear Pore Complex Depends on Sumoylation of DNA Repair Proteins and Permits Rad51 Association

open access: yesCell Reports, 2020
SUMMARY Expanded CAG repeats form stem-loop secondary structures that lead to fork stalling and collapse. Previous work has shown that these collapsed forks relocalize to nuclear pore complexes (NPCs) in late S phase in a manner dependent on replication,
J. Whalen   +4 more
semanticscholar   +1 more source

A complex of nuclear pore proteins required for pore function. [PDF]

open access: yesThe 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
openaire   +2 more sources

The Nuclear Pore Complex Is a Key Target of Viral Proteases to Promote Viral Replication

open access: yesViruses, 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]

open access: yesPLoS 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
doaj   +1 more source

Types of nuclear localization signals and mechanisms of protein import into the nucleus

open access: yesCell 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
doaj   +1 more source

On the nuclear pore complex and its emerging role in cellular mechanotransduction

open access: yesAPL Bioengineering, 2022
The nuclear pore complex (NPC) is a large protein assembly that perforates the nuclear envelope and provides a sole gateway for traffic between the cytoplasm and the nucleus.
A. Matsuda, M. Mofrad
semanticscholar   +1 more source

Deciphering Networks of Protein Interactions at the Nuclear Pore Complex [PDF]

open access: yesMolecular & 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
openaire   +2 more sources

Mitogen activated protein kinase at the nuclear pore complex [PDF]

open access: yesJournal 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
openaire   +2 more sources

Differential Mitotic Phosphorylation of Proteins of the Nuclear Pore Complex [PDF]

open access: yesJournal of Biological Chemistry, 1995
During each cell cycle, the nucleus of higher eukaryotes undergoes a dramatic assembly and disassembly. These events can be faithfully reproduced in vitro using cell-free extracts derived from Xenopus eggs. Such extracts contain three major N-acetylglucosaminylated proteins, p200, p97, and p60.
C, Macaulay, E, Meier, D J, Forbes
openaire   +2 more sources

Herpesvirus Nuclear Egress across the Outer Nuclear Membrane

open access: yesViruses, 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
doaj   +1 more source

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