Results 121 to 130 of about 19,822 (225)
The Multiple Faces of Disordered Nucleoporins
Journal 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 ...
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Compensation for chronic oxidative stress in ALADIN null mice
Biology Open, 2018 Mutations in the AAAS gene coding for the nuclear pore complex protein ALADIN lead to the autosomal recessive disorder triple A syndrome. Triple A patients present with a characteristic phenotype including alacrima, achalasia and adrenal insufficiency ...
Ramona Jühlen +6 more
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Targeting self-renewal pathways in myeloid malignancies [PDF]
, 2013 A fundamental property of hematopoietic stem cells (HSCs) is the ability to self-renew. This is a complex process involving multiple signal transduction cascades which control the fine balance between self-renewal and differentiation through ...
Copland, M., Sands, W.A., Wheadon, H.
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Cell Division, 2018 Background Membrane-associated progesterone receptors are restricted to the endoplasmic reticulum and are shown to regulate the activity of cytochrome P450 enzymes which are involved in steroidogenesis or drug detoxification.
Ramona Jühlen +3 more
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Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: Commonalities, differences, challenges [PDF]
, 2011 The nuclear pore complex (NPC) regulates all traffic between the cytoplasm and the nucleus. It is a large protein assembly composed of multiple copies of ~30 nucleoporins (nups).
Leksa, Nina Carolina, Schwartz, Thomas
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Architecture of the nuclear pore complex coat [PDF]
, 2015 The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. Despite half a century of structural characterization, the architecture of the NPC remains unknown.
Correia, Ana R. +6 more
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eLife, 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
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Nucleoporins and Transcription: New Connections, New Questions
PLoS 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
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Deciphering the 'fuzzy' interaction of FG nucleoporins and transport factors using SANS
, 2018 The largely intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG Nups) underline a selectivity mechanism, which enables the rapid translocation of transport factors (TFs) through the nuclear pore complexes (NPCs).
Cowburn, David +3 more
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Mitotic Phosphorylation of Nucleoporins: Dismantling NPCs and Beyond [PDF]
Developmental 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.
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