Results 41 to 50 of about 173,033 (291)

Silencing nuclear pore protein Tpr elicits a senescent-like phenotype in cancer cells.

PLoS ONE, 2011
BackgroundTpr is a large coiled-coil protein located in the nuclear basket of the nuclear pore complex for which many different functions were proposed from yeast to human.Methodology/principal findingsHere we show that depletion of Tpr by RNA ...
Brigitte David-Watine
doaj   +1 more source

The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome [PDF]

Proceedings of the National Academy of Sciences, 2003
Triple A syndrome is a human autosomal recessive disorder characterized by an unusual array of tissue-specific defects. Triple A syndrome arises from mutations in a WD-repeat protein of unknown function called ALADIN (also termed Adracalin or AAAS).
Janet M, Cronshaw, Michael J, Matunis
openaire   +2 more sources

The NAE Pathway: Autobahn to the Nucleus for Cell Surface Receptors

Cells, 2019
Various growth factors and full-length cell surface receptors such as EGFR are translocated from the cell surface to the nucleoplasm, baffling cell biologists to the mechanisms and functions of this process. Elevated levels of nuclear EGFR correlate with
Poonam Shah, Alexandre Chaumet, Stephen J. Royle, Frederic A. Bard   +3 more
doaj   +1 more source

The transport of integral membrane proteins across the nuclear pore complex [PDF]

Nucleus, 2012
The nuclear envelope protects and organizes the genome. The nuclear pore complexes embedded in the nuclear envelope allow selective transport of macromolecules between the cytosol and nucleoplasm, and as such help to control the flow of information from DNA to RNA to proteins.
Meinema, Anne C., Poolman, Bert, Veenhoff, Liesbeth M.   +2 more
openaire   +2 more sources

The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex

Viruses, 2021
Herpes simplex virus type 1 nucleocapsids are released from the host nucleus by a budding process through the nuclear envelope called nuclear egress. Two viral proteins, the integral membrane proteins pUL34 and pUL31, form the nuclear egress complex at ...
Christina Funk, Débora Marques da Silveira e Santos, Melanie Ott, Verena Raschbichler, Susanne M. Bailer   +4 more
doaj   +1 more source

Biochemical characterization of nuclear pore complex protein gp210 oligomers [PDF]

European Journal of Biochemistry, 2001
The membrane‐spanning glycoprotein gp210 is a major component of the nuclear pore complex. This nucleoporin contains a large cisternal N‐terminal domain, a short C‐terminal cytoplasmic tail, and a single transmembrane segment. We show here that dimers of native gp210 can be isolated from cell extracts by immunoprecipitation, and from purified rat liver
C, Favreau, R, Bastos, J, Cartaud, J C, Courvalin, P, Mustonen   +4 more
openaire   +2 more sources

Nuclear envelope budding and its cellular functions

Nucleus, 2023
The nuclear pore complex (NPC) has long been assumed to be the sole route across the nuclear envelope, and under normal homeostatic conditions it is indeed the main mechanism of nucleo-cytoplasmic transport.
Katharina S. Keuenhof, Verena Kohler, Filomena Broeskamp, Dimitra Panagaki, Sean D. Speese, Sabrina Büttner, Johanna L. Höög   +6 more
doaj   +1 more source

Assembly of nuclear pore complexes mediated by major vault protein [PDF]

Journal of Cell Science, 2009
During interphase growth of eukaryotic cells, nuclear pore complexes (NPCs) are continuously incorporated into the intact nuclear envelope (NE) by mechanisms that are largely unknown. De novo formation of NPCs involves local fusion events between the inner and outer nuclear membrane, formation of a transcisternal membranous channel of defined diameter ...
Friederike, Vollmar, Christian, Hacker, René-Peiman, Zahedi, Albert, Sickmann, Andrea, Ewald, Ulrich, Scheer, Marie-Christine, Dabauvalle   +6 more
openaire   +2 more sources

Higher nucleoporin-Importinβ affinity at the nuclear basket increases nucleocytoplasmic import.

PLoS ONE, 2013
Several in vitro studies have shown the presence of an affinity gradient in nuclear pore complex proteins for the import receptor Importinβ, at least partially contributing to nucleocytoplasmic transport, while others have historically argued against the
Mohammad Azimi, Mohammad R K Mofrad
doaj   +1 more source

hnRNPA3 regulates hESCs pluripotency through modulating mRNA export [PDF]

Jichu yixue yu linchuang, 2021
Objective To explore the biological function of RNA binding protein heterogeneous nuclear ribonucleoprotein A3(hnRNPA3) in the maintenance of pluripotency of human embryonic stem cells(hESCs) and to reveal its new mechanism in RNA transport.
YANG Jia-bin, CHEN Zhong-yang, ZHOU Fan-qi, YU Jia, MA Yan-ni
doaj