Search Results - "Kehlenbach, Ralph H."
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CRM1-mediated nuclear export: to the pore and beyond
Published in Trends in cell biology (01-04-2007)“…CRM1 (chromosome region maintenance 1; also referred to as exportin1 or Xpo1) is a member of the importin β superfamily of nuclear transport receptors,…”
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The Part and the Whole: functions of nucleoporins in nucleocytoplasmic transport
Published in Trends in cell biology (01-08-2010)“…The nuclear pore complex (NPC) functions as a selective gate that allows passage of certain molecules into and out of the nucleus and restricts that of others…”
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Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1
Published in Scientific reports (04-05-2018)“…TDP-43 and FUS are nuclear proteins with multiple functions in mRNA processing. They play key roles in ALS (amyotrophic lateral sclerosis) and FTD…”
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4
Targeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear Membrane
Published in International journal of molecular sciences (15-01-2019)“…LRRC59 (leucine-rich repeat-containing protein 59) is a tail-anchored protein with a single transmembrane domain close to its C-terminal end that localizes to…”
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Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane
Published in The Journal of biological chemistry (01-11-2019)“…Vesicle-associated membrane protein–associated protein B (VAPB) is a tail-anchored protein that is present at several contact sites of the endoplasmic…”
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The Interactome of the VAP Family of Proteins: An Overview
Published in Cells (Basel, Switzerland) (14-07-2021)“…Membrane contact sites (MCS) are sites of close apposition of two organelles that help in lipid transport and synthesis, calcium homeostasis and several other…”
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Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export
Published in Cell reports (Cambridge) (27-10-2015)“…CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine…”
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Resolution doubling in fluorescence microscopy with confocal spinning-disk image scanning microscopy
Published in Proceedings of the National Academy of Sciences - PNAS (24-12-2013)“…We demonstrate how a conventional confocal spinning-disk (CSD) microscope can be converted into a doubly resolving image scanning microscopy (ISM) system…”
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Sequestosome 1 Is Part of the Interaction Network of VAPB
Published in International journal of molecular sciences (09-12-2021)“…VAPB (Vesicle-Associated-membrane Protein-associated protein B) is a tail-anchored membrane protein of the endoplasmic reticulum that can also be detected at…”
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Nup214 Is Required for CRM1-Dependent Nuclear Protein Export In Vivo
Published in Molecular and Cellular Biology (01-09-2006)“…Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Extensive Identification and In-depth Validation of Importin 13 Cargoes
Published in Molecular & cellular proteomics (01-07-2018)“…Importin 13 is a member of the importin β family of transport receptors. Unlike most family members, importin 13 mediates both, nuclear protein import and…”
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Defective nuclear import of Tpr in Progeria reflects the Ran sensitivity of large cargo transport
Published in The Journal of cell biology (13-05-2013)“…The RanGTPase acts as a master regulator of nucleocytoplasmic transport by controlling assembly and disassembly of nuclear transport complexes. RanGTP is…”
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Several Phenylalanine-Glycine Motives in the Nucleoporin Nup214 Are Essential for Binding of the Nuclear Export Receptor CRM1
Published in The Journal of biological chemistry (08-02-2013)“…Nucleoporins containing phenylalanine glycine (FG) repeats play an important role in nucleocytoplasmic transport as they bind to transport receptors and…”
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The Oncogenic Fusion Proteins SET-Nup214 and Sequestosome-1 (SQSTM1)-Nup214 Form Dynamic Nuclear Bodies and Differentially Affect Nuclear Protein and Poly(A)+ RNA Export
Published in The Journal of biological chemistry (28-10-2016)“…Genetic rearrangements are a hallmark of several forms of leukemia and can lead to oncogenic fusion proteins. One example of an affected chromosomal region is…”
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The SQSTM1-NUP214 fusion protein interacts with Crm1, activates Hoxa and Meis1 genes, and drives leukemogenesis in mice
Published in PloS one (28-04-2020)“…The NUP98 and NUP214 nucleoporins (NUPs) are recurrently fused to heterologous proteins in leukemia. The resulting chimeric oncoproteins retain the…”
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Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia deformation sequence
Published in PLoS genetics (13-12-2018)“…Nucleoporins build the nuclear pore complex (NPC), which, as sole gate for nuclear-cytoplasmic exchange, is of outmost importance for normal cell function…”
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The Nucleoporin Nup358/RanBP2 Promotes Nuclear Import in a Cargo‐ and Transport Receptor‐Specific Manner
Published in Traffic (Copenhagen, Denmark) (01-02-2012)“…In vertebrates, the nuclear pore complex (NPC), the gate for transport of macromolecules between the nucleus and the cytoplasm, consists of approximately 30…”
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MD Simulations and FRET Reveal an Environment-Sensitive Conformational Plasticity of Importin-β
Published in Biophysical journal (21-07-2015)“…The nuclear pore complex mediates nucleocytoplasmic transport of macromolecules in eukaryotic cells. Transport through the pore is restricted by a hydrophobic…”
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nuclear pore component Nup358 promotes transportin-dependent nuclear import
Published in Journal of cell science (15-04-2009)“…Nup358 (also known as RanBP2), a component of the cytoplasmic filaments of the nuclear pore complex, has been implicated in various nucleocytoplasmic transport…”
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Notch1 signaling is mediated by importins alpha 3, 4, and 7
Published in Cellular and molecular life sciences : CMLS (01-09-2010)“…The Notch signaling pathway is an important regulation system for the development and self-renewal of different tissues. A specific feature of this signaling…”
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