Results 121 to 130 of about 18,104 (240)

MicroRNA-Mediated mRNA Translation Activation in Quiescent Cells and Oocytes Involves Recruitment of a Nuclear microRNP [PDF]

open access: yes, 2012
MicroRNAs can promote translation of specific mRNAs in quiescent (G0) mammalian cells and immature Xenopus laevis oocytes. We report that microRNA-mediated upregulation of target mRNAs in oocytes is dependent on nuclear entry of the microRNA ...
Lee, J. H.   +6 more
core   +1 more source

Using a Simple Cellular Assay to Map NES Motifs in Cancer-Related Proteins, Gain Insight into CRM1-Mediated NES Export, and Search for NES-Harboring Micropeptides

open access: yesInternational Journal of Molecular Sciences, 2020
The nuclear export receptor CRM1 (XPO1) recognizes and binds specific sequence motifs termed nuclear export signals (NESs) in cargo proteins. About 200 NES motifs have been identified, but over a thousand human proteins are potential CRM1 cargos, and ...
M. Sendino   +3 more
semanticscholar   +1 more source

SIRT6 Lysine‐Demyristoylates ATF2 to Ameliorate Vascular Injury via PRKCD/VE‐Cadherin Pathway Regulating Vascular Endothelial Barrier

open access: yesAdvanced Science, Volume 12, Issue 41, November 6, 2025.
A novel modified SIRT6 variant (dSIRT6) H133Y‐mediated enrichment technique unmasks 15 new human lysine‐myristoylated proteins. Notably, Sirtuin 6 (SIRT6) demyristoylation of activating transcription factor 2 (ATF2) at K296 orchestrates its nucleoplasmic translocation.
Runyang Feng   +40 more
wiley   +1 more source

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

Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex [PDF]

open access: yes, 2014
BACKGROUND: Box C/D snoRNPs, which are typically composed of box C/D snoRNA and the four core protein components Nop1, Nop56, Nop58, and Snu13, play an essential role in the modification and processing of pre-ribosomal RNA.
Liang Zhao   +4 more
core   +1 more source

Structural prerequisites for CRM1-dependent nuclear export signaling peptides: accessibility, adapting conformation, and the stability at the binding site

open access: yesScientific Reports, 2019
Nuclear export signal (NES) motifs function as essential regulators of the subcellular location of proteins by interacting with the major nuclear exporter protein, CRM1. Prediction of NES is of great interest in many aspects of research including cancer,
Yoonji Lee   +4 more
semanticscholar   +1 more source

Mixed Messages: Dynamic and Compositional Heterogeneity of Nuclear Messenger Ribonucleoprotein (mRNP) Complexes

open access: yesWIREs RNA, Volume 16, Issue 6, November/December 2025.
RNA‐protein (RNP) complexes formed by a network of RNA–RNA, RNA–protein, and protein–protein interactions are central to gene expression. mRNP compositional heterogeneity underlies precise regulation (e.g., export, storage, translation, and decay), enabling cells to adapt to changing conditions, with changes in composition further linked to stress ...
Theresa Wechsler   +2 more
wiley   +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

Tubulin is actively exported from the nucleus through the Exportin1/CRM1 pathway

open access: yesScientific Reports, 2019
Microtubules of all eukaryotic cells are formed by α- and β-tubulin heterodimers. In addition to the well known cytoplasmic tubulins, a subpopulation of tubulin can occur in the nucleus.
K. Schwarzerová   +9 more
semanticscholar   +1 more source

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