Results 81 to 90 of about 7,200 (169)

Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.

open access: yesPLoS Pathogens, 2011
In contrast to most RNA viruses, influenza viruses replicate their genome in the nucleus of infected cells. As a result, newly-synthesized vRNA genomes, in the form of viral ribonucleoprotein complexes (vRNPs), must be exported to the cytoplasm for ...
Geoffrey P Chase   +7 more
doaj   +1 more source

Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A

open access: yeseLife, 2020
In the nucleus, the spatiotemporal regulation of the catalytic subunit of cAMP-dependent protein kinase A (PKA-C) is orchestrated by an intrinsically disordered protein kinase inhibitor, PKI, which recruits the CRM1/RanGTP nuclear exporting complex.
Cristina Olivieri   +13 more
doaj   +1 more source

Selective Inhibitor of Nuclear Export (SINE) Compounds Alter New World Alphavirus Capsid Localization and Reduce Viral Replication in Mammalian Cells.

open access: yesPLoS Neglected Tropical Diseases, 2016
The capsid structural protein of the New World alphavirus, Venezuelan equine encephalitis virus (VEEV), interacts with the host nuclear transport proteins importin α/β1 and CRM1.
Lindsay Lundberg   +8 more
doaj   +1 more source

Chromatin-prebound Crm1 recruits Nup98-HoxA9 fusion to induce aberrant expression of Hox cluster genes

open access: yeseLife, 2016
The nucleoporin Nup98 is frequently rearranged to form leukemogenic Nup98-fusion proteins with various partners. However, their function remains largely elusive. Here, we show that Nup98-HoxA9, a fusion between Nup98 and the homeobox transcription factor
Masahiro Oka   +10 more
doaj   +1 more source

Evolution of a species-specific determinant within human CRM1 that regulates the post-transcriptional phases of HIV-1 replication.

open access: yesPLoS Pathogens, 2011
The human immunodeficiency virus type-1 (HIV-1) Rev protein regulates the nuclear export of intron-containing viral RNAs by recruiting the CRM1 nuclear export receptor.
Nathan M Sherer   +5 more
doaj   +1 more source

CRM1/XPO1 is associated with clinical outcome in glioma and represents a therapeutic target by perturbing multiple core pathways

open access: yesJournal of Hematology & Oncology, 2016
Background Malignant gliomas are associated with a high mortality rate, and effective treatment options are limited. Thus, the development of novel targeted treatments to battle this deadly disease is imperative.
Xuejiao Liu   +11 more
doaj   +1 more source

Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore

open access: yeseLife, 2018
Non-centrosomal microtubule organizing centers (MTOCs) are important for microtubule organization in many cell types. In fission yeast Schizosaccharomyces pombe, the protein Mto1, together with partner protein Mto2 (Mto1/2 complex), recruits the γ ...
Xun X Bao   +7 more
doaj   +1 more source

Sphingosine kinase 1 serves as a pro-viral factor by regulating viral RNA synthesis and nuclear export of viral ribonucleoprotein complex upon influenza virus infection.

open access: yesPLoS ONE, 2013
Influenza continues to pose a threat to humans by causing significant morbidity and mortality. Thus, it is imperative to investigate mechanisms by which influenza virus manipulates the function of host factors and cellular signal pathways. In this study,
Young-Jin Seo   +6 more
doaj   +1 more source

Crm1 locks up replication factors

open access: yesThe Journal of Cell Biology, 2003
![Graphic][1] Crm1 in the cell cycle. Yamaguchi/Elsevier Limiting replication to a single round per division is critical for cells, but the proteins that control the process in metazoans have remained obscure.
openaire   +2 more sources

The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycle.

open access: yesPLoS ONE, 2015
Molecular traffic between the nucleus and the cytoplasm is regulated by the nuclear pore complex (NPC), which acts as a highly selective channel perforating the nuclear envelope in eukaryotic cells.
Seyed Hanif Mahboobi   +2 more
doaj   +1 more source

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