Results 21 to 30 of about 97,972 (258)

Characterization of a nuclear pore protein sheds light on the roles and composition of the Toxoplasma gondii nuclear pore complex [PDF]

open access: yesCellular and Molecular Life Sciences, 2017
The nuclear pore is a key structure in eukaryotes regulating nuclear-cytoplasmic transport as well as a wide range of cellular processes. Here, we report the characterization of the first Toxoplasma gondii nuclear pore protein, named TgNup302, which appears to be the orthologue of the mammalian Nup98-96 protein.
Courjol, Flavie   +9 more
openaire   +2 more sources

Nuclear Envelope Regulation of Oncogenic Processes: Roles in Pancreatic Cancer

open access: yesEpigenomes, 2018
Pancreatic cancer is an aggressive and intractable malignancy with high mortality. This is due in part to a high resistance to chemotherapeutics and radiation treatment conferred by diverse regulatory mechanisms.
Claudia C. Preston   +1 more
doaj   +1 more source

Components of coated vesicles and nuclear pore complexes share a common molecular architecture.

open access: yesPLoS Biology, 2004
Numerous features distinguish prokaryotes from eukaryotes, chief among which are the distinctive internal membrane systems of eukaryotic cells. These membrane systems form elaborate compartments and vesicular trafficking pathways, and sequester the ...
Damien Devos   +6 more
doaj   +1 more source

The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import [PDF]

open access: yesThe Journal of Cell Biology, 2002
The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells. Eight filaments project from the NPC into the cytoplasm and are proposed to function in nuclear import. We investigated the localization and function of two nucleoporins on the cytoplasmic face of the NPC, CAN/Nup214 and ...
Walther, T. C.   +6 more
openaire   +5 more sources

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

open access: yesPLoS 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]

open access: yesProceedings 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

open access: yesCells, 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   +3 more
doaj   +1 more source

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

open access: yesNucleus, 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.   +2 more
openaire   +2 more sources

Nuclear envelope budding and its cellular functions

open access: yesNucleus, 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   +6 more
doaj   +1 more source

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

open access: yesEuropean 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   +4 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy