Results 21 to 30 of about 7,200 (169)
Targeting CRM1 for Progeria Syndrome Therapy. [PDF]
Aging CellABSTRACTHutchinson‐Gilford progeria syndrome (HGPS) is a premature aging disease caused by progerin, a mutant variant of lamin A. Progerin anchors aberrantly to the nuclear envelope disrupting a plethora of cellular processes, which in turn elicits senescence.
Soto-Ponce A +14 more
europepmc +3 more sources
Cell Reports, 2015 CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tightly
Sarah A. Port +7 more
doaj +1 more source
CRM1-spike-mediated nuclear export of hepatitis B virus encapsidated viral RNA
Cell Reports, 2022 Summary: Hepatitis B virus (HBV) is a global pathogen. We report here that the cellular CRM1 machinery can mediate nuclear export of entire HBV core (HBc) particles containing encapsidated viral RNAs.
Ching-Chun Yang +10 more
doaj +1 more source
The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA
eLife, 2014 The HIV Rev protein routes viral RNAs containing the Rev Response Element (RRE) through the Crm1 nuclear export pathway to the cytoplasm where viral proteins are expressed and genomic RNA is delivered to assembling virions.
David S Booth +2 more
doaj +1 more source
CRM1-mediated Recycling of Snurportin 1 to the Cytoplasm [PDF]
The Journal of Cell Biology, 1999 Importin β is a major mediator of import into the cell nucleus. Importin β binds cargo molecules either directly or via two types of adapter molecules, importin α, for import of proteins with a classical nuclear localization signal (NLS), or snurportin 1, for import of m3G-capped U snRNPs.
Paraskeva, E. +7 more
openaire +5 more sources
Structural determinants of nuclear export signal orientation in binding to exportin CRM1
eLife, 2015 The Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of hundreds of proteins through recognition of their nuclear export signals (NESs), which are highly variable in sequence and structure.
Ho Yee Joyce Fung +3 more
doaj +1 more source
CRM1- and Ran-independent nuclear export of β-catenin [PDF]
Current Biology, 2001 Activation of the Wnt pathway induces beta-catenin to localize inside the nucleus, where it interacts with transcription factors such as TCF/LEF-1. Regulation of the pathway occurs through a beta-catenin-degrading complex based on Axin and the tumor suppressor APC. We have previously found that beta-catenin import occurs independently of nuclear import
Wiechens, N. +1 more
openaire +3 more sources
eLife, 2019 We previously demonstrated that CRM1, a major nuclear export factor, accumulates at Hox cluster regions to recruit nucleoporin-fusion protein Nup98HoxA9, resulting in robust activation of Hox genes (Oka et al., 2016).
Masahiro Oka +9 more
doaj +1 more source
Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals
eLife, 2017 Nuclear export receptor CRM1 binds highly variable nuclear export signals (NESs) in hundreds of different cargoes. Previously we have shown that CRM1 binds NESs in both polypeptide orientations (Fung et al., 2015).
Ho Yee Joyce Fung +2 more
doaj +1 more source
Nucleus, 2020 Xenopus egg extracts are a powerful in vitro tool for studying complex biological processes, including nuclear reconstitution, nuclear membrane and pore assembly, and spindle assembly.
Matthew S. Nord +5 more
doaj +1 more source