Results 81 to 90 of about 7,164,132 (254)

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

open access: yesPLoS 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

Emerging experimental and computational methods for studying redox‐regulated structural transitions

open access: yesFEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass   +2 more
wiley   +1 more source

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 ...
Graham, Sheila   +10 more
core   +1 more source

The coordination of nuclear envelope assembly and chromosome segregation in metazoans

open access: yesNucleus, 2020
The nuclear envelope (NE) is composed of two lipid bilayer membranes that enclose the eukaryotic genome. In interphase, the NE is perforated by thousands of nuclear pore complexes (NPCs), which allow transport in and out of the nucleus. During mitosis in
Shiwei Liu, David Pellman
doaj   +1 more source

Synergistic perspectives—How single‐molecule biophysics complement biochemical understanding

open access: yesFEBS Letters, EarlyView.
In this review, we discuss how ensemble biochemistry and single‐molecule approaches are complementary, outline commonly used single‐molecule techniques, and illustrate their relevance through two representative case studies: chromatin organization by SMC complexes and pathway choice during DNA double‐strand break repair.
Sara De Bragança   +2 more
wiley   +1 more source

NUP-1 is a large coiled-coil nucleoskeletal protein in Trypanosomes with lamin-like functions [PDF]

open access: yes, 2012
A unifying feature of eukaryotic nuclear organization is genome segregation into transcriptionally active euchromatin and transcriptionally repressed heterochromatin.
Wan, Yakun   +91 more
core   +2 more sources

Functional comparison of EncB and EncC cargo proteins in iron storage within the Myxococcus xanthus encapsulin

open access: yesFEBS Letters, EarlyView.
Encapsulins are protein nanocompartments that play an important role in iron storage. In the Myxococcus xanthus encapsulin system, two cargo proteins called EncB and EncC contribute to iron mineralization. Here, we show that EncB and EncC generate iron‐containing minerals with distinct chemical compositions, suggesting that the composition of stored ...
Harry B. McDowell   +2 more
wiley   +1 more source

Dissecting the structural dynamics of the nuclear pore complex

open access: yes, 2020
<p>Raw mass spectrometry data files for the experiments included in the manuscript "Dissecting the structural dynamics of the nuclear pore complex" by Hakhverdyan et al.</p ...
Zhanna Hakhverdyan   +2 more
core   +1 more source

Electron tomography reveals posttranscriptional binding of pre-mRNPs to specific fibers in the nucleoplasm [PDF]

open access: yes, 2000
International audienceUsing electron tomography, we have analyzed whether the Balbiani ring (BR) pre-mRNP particles in transit from the gene to the nuclear pore complex (NPC) are bound to any structure that could impair free diffusion through the ...
Sabri, N   +21 more
core   +1 more source

Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.

open access: yesPLoS Biology
Nuclear export of mRNAs requires loading the mRNP to the transporter Mex67/Mtr2 in the nucleoplasm, controlled access to the pore by the basket-localised TREX-2 complex and mRNA release at the cytoplasmic site by the DEAD-box RNA helicase Dbp5 ...
Bernardo Papini Gabiatti   +5 more
doaj   +1 more source

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