Results 41 to 50 of about 2,343,531 (340)

The Nuclear Pore Complex and Nuclear Transport [PDF]

open access: yesCold Spring Harbor Perspectives in Biology, 2010
Internal membrane bound structures sequester all genetic material in eukaryotic cells. The most prominent of these structures is the nucleus, which is bounded by a double membrane termed the nuclear envelope (NE). Though this NE separates the nucleoplasm and genetic material within the nucleus from the surrounding cytoplasm, it is studded throughout ...
Susan R. Wente, Michael P. Rout
openaire   +3 more sources

Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through NUP62, inhibiting host nucleocytoplasmic transport pathways [PDF]

open access: yes, 2012
The herpes simplex virus ICP27 protein is important for the expression and nuclear export of viral mRNAs. Although several binding sites have been mapped along the ICP27 sequence for various RNA and protein partners including the transport receptor TAP ...
Arnold   +83 more
core   +3 more sources

Construction of nuclear envelope shape by a high-genus vesicle with pore-size constraint [PDF]

open access: yesBiophys. J. 111, 824-831 (2016), 2016
Nuclear pores have an approximately uniform distribution in the nuclear envelope of most living cells. Hence, the morphology of the nuclear envelope is a spherical stomatocyte with a high genus. We have investigated the morphology of high-genus vesicles under pore-size constraint using dynamically triangulated membrane simulations.
arxiv   +1 more source

Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2

open access: yesJournal of Cell Biology, 2020
Rampello et al. demonstrate that Torsin ATPases play a critical role in nuclear pore assembly and thus present mechanistic insight into DYT1 dystonia etiology.
Anthony J. Rampello   +7 more
semanticscholar   +1 more source

The cAMP sensors, EPAC1 and EPAC2, display distinct subcellular distributions despite sharing a common nuclear pore localisation signal [PDF]

open access: yes, 2015
We have identified a conserved nuclear pore localisation signal (NPLS; amino acids 764–838 of EPAC1) in the catalytic domains of the cAMP-sensors, EPAC1 and EPAC2A.
Parnell, Euan   +2 more
core   +1 more source

Baculovirus Nuclear Import: Open, Nuclear Pore Complex (NPC) Sesame

open access: yesViruses, 2013
Baculoviruses are one of the largest viruses that replicate in the nucleus of their host cells. During infection, the rod-shape, 250-nm long nucleocapsid delivers its genome into the nucleus.
Wei Wu, Shelly Au, Nelly Panté
doaj   +1 more source

Nuclear magnetic resonance cryoporometry [PDF]

open access: yes, 2008
Nuclear Magnetic Resonance (NMR) cryoporometry is a technique for non-destructively determining pore size distributions in porous media through the observation of the depressed melting point of a confined liquid.
Mitchell, J.   +2 more
core   +1 more source

Interdependent changes of nuclear lamins, nuclear pore complexes, and ploidy regulate cellular regeneration and stress response in the heart

open access: yesNucleus, 2023
In adult mammals, many heart muscle cells (cardiomyocytes) are polyploid, do not proliferate (post-mitotic), and, consequently, cannot contribute to heart regeneration.
Yao Li   +3 more
doaj   +1 more source

Permeability of Single Nuclear Pores [PDF]

open access: yesBiophysical Journal, 1999
In this first application of optical single transporter recording (OSTR), a recently established technique for optically monitoring the activity of single transporters in membrane patches (Tschödrich-Rotter and Peters. 1998. J. Microsc. 192:114-125), the passive permeability of the nuclear pore complex (NPC) was measured for a homologous series of ...
Oliver Keminer, Reiner Peters
openaire   +3 more sources

Exo70-Mediated Recruitment of Nucleoporin Nup62 at the Leading Edge of Migrating Cells is Required for Cell Migration [PDF]

open access: yes, 2009
Nucleoporin Nup62 localizes at the central channel of the nuclear pore complex and is essential for nucleocytoplasmic transport. Through its FG-repeat domain, Nup62 regulates nuclear pore permeability and binds nuclear transport receptors.
Bayliss   +61 more
core   +1 more source

Home - About - Disclaimer - Privacy