Results 121 to 130 of about 10,026 (221)

Molecular architecture of the Nup84–Nup145C–Sec13 edge element in the nuclear pore complex lattice [PDF]

open access: yes, 2009
Nuclear pore complexes (NPCs) facilitate all nucleocytoplasmic transport. These massive protein assemblies are modular, with a stable structural scaffold supporting more dynamically attached components.
A Fotin   +62 more
core   +1 more source

The Multiple Faces of Disordered Nucleoporins

open access: yesJournal of Molecular Biology, 2016
An evolutionary advantage of intrinsically disordered proteins (IDPs) is their ability to bind a variety of folded proteins-a paradigm that is central to the nucleocytoplasmic transport mechanism, in which nuclear transport receptors mediate the translocation of various cargo through the nuclear pore complex by binding disordered phenylalanine-glycine ...
openaire   +2 more sources

Nucleoporin 153 links nuclear pore complex to chromatin architecture by mediating CTCF and cohesin binding

open access: yesNature Communications, 2020
The nuclear pore complex components, nucleoporins, have been proposed to mediate spatial and temporal organization of chromatin. Here, the authors show that Nucleoporin 153 interacts with CTCF and cohesin, and mediates their binding across cis-regulatory
Shinichi Kadota   +5 more
doaj   +1 more source

A role for Gle1, a regulator of DEAD-box RNA helicases, at centrosomes and basal bodies. [PDF]

open access: yes, 2017
Control of organellar assembly and function is critical to eukaryotic homeostasis and survival. Gle1 is a highly conserved regulator of RNA-dependent DEAD-box ATPase proteins, with critical roles in both mRNA export and translation.
Akef, Abdalla   +2 more
core   +1 more source

D2P2: database of disordered protein predictions [PDF]

open access: yes, 2013
We present the Database of Disordered Protein Prediction (D2P2), available at http://d2p2.pro (including website source code). A battery of disorder predictors and their variants, VL-XT, VSL2b, PrDOS, PV2, Espritz and IUPred, were run on all protein ...
Dosztányi, Zsuzsanna   +3 more
core  

Nucleoporins and Transcription: New Connections, New Questions

open access: yesPLoS Genetics, 2010
It seems to make perfect sense that RNA, which must be exported from the nucleus to be translated, would be produced near or in association with nuclear pores. Indeed, recent reports proposed that Saccharomyces cerevisiae genes located close to the nuclear pore complex (NPC) tend to be highly transcribed [1],[2] and that, upon activation, some genes ...
Kohta Ikegami, Jason D Lieb
openaire   +3 more sources

Nucleoporin 107, 62 and 153 mediate Kcnq1ot1 imprinted domain regulation in extraembryonic endoderm stem cells

open access: yesNature Communications, 2018
Genomic imprinting restricts transcription to predominantly one parental allele. Here the authors perform a screen for epigenetic factors involved in paternal allelic silencing at the Kcnq1ot1 imprinted domain in mouse extraembryonic endoderm stem cells ...
Saqib S. Sachani   +6 more
doaj   +1 more source

Newly found Tetrahymena nucleoporins, Nup214, Nup153 and Pom121/Pom82, differentiate nuclear pore complexes of functionally distinct nuclei

open access: yesCommunicative & Integrative Biology, 2018
The nuclear pore complex (NPC) is the sole gateway for molecular transport between the nucleus and the cytoplasm in eukaryotes. The NPC is composed of approximately 30 different kinds of protein components called nucleoporins. The functional structure of
Masaaki Iwamoto   +2 more
doaj   +1 more source

Mitotic Phosphorylation of Nucleoporins: Dismantling NPCs and Beyond [PDF]

open access: yesDevelopmental Cell, 2011
Recently reporting in Cell, Laurell et al. (2011) demonstrate that the hyperphosphorylation of vertebrate Nup98 by distinct mitotic kinases contributes to its release from nuclear pores, drives nuclear envelope permeabilization, and may provide a molecular switch coordinating nuclear envelope breakdown and spindle formation.
openaire   +2 more sources

From the trap to the basket: getting to the bottom of the nuclear pore complex [PDF]

open access: yes, 2018
Nuclear pore complexes (NPCs) are large supramolecular assemblies that perforate the double-membraned nuclear envelope and serve as the sole gateways of molecular exchange between the cytoplasm and the nucleus in interphase cells.
Aebi, Ueli   +2 more
core  

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