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Imaging Fluorescent Nuclear Pore Complex Proteins in C. elegans
2022C. elegans is a well-characterized and relatively simple model organism, making it attractive for studying nuclear pore complex proteins in cell and developmental biology. C. elegans is transparent and highly amendable to genetic manipulation. Therefore, it is possible to generate fluorescently tagged proteins and combine this with various light ...
Courtney, Lancaster +7 more
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1996
The nuclear envelope forms the boundary between the nucleus and the cytoplasm and as such regulates the exchange of macromolecules between the two compartments. The channels through the nuclear envelop that actually mediate this macromolecular traffic are the nuclear pore complexes.
R, Bastos, N, Panté, B, Burke
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The nuclear envelope forms the boundary between the nucleus and the cytoplasm and as such regulates the exchange of macromolecules between the two compartments. The channels through the nuclear envelop that actually mediate this macromolecular traffic are the nuclear pore complexes.
R, Bastos, N, Panté, B, Burke
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The functional versatility of the nuclear pore complex proteins
Seminars in Cell & Developmental Biology, 2017Over the past few decades, it is increasingly evident that nucleoporins are multi-functional proteins that are not only pivotal for the formation of the nuclear pore complex. They also have key roles in mitosis, gene expression, development and disease. In this review, the versatility and functions of nucleoporins outside the NPC will be discussed.
Mohammed, Hezwani, Birthe, Fahrenkrog
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Identification and characterization of a nuclear pore complex protein
Cell, 1986We describe studies using a monoclonal antibody that recognizes a 62 kd protein (p62) of rat liver nuclei. This protein remains associated with the nuclear pore complex-lamina fraction resulting from treatment of nuclei with DNAase, RNAase, and nonionic detergent. Immunofluorescence revealed a strikingly punctate pattern of nuclear rim staining.
L I, Davis, G, Blobel
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Specific Monoclonal Antibody Against the Nuclear Pore Complex Protein, Nup96
Hybridoma, 2010Nup96 is a component of the Nup107-160 complex, the largest subunit of the nuclear pore complex. Nup96 is generated as a precursor protein with Nup98. However, the mechanism by which Nup96 contributes to cell function is not clear. We report here on the preparation of a monoclonal antibody (MAb) directed against mouse Nup96.
Chiaki, Mizuguchi +4 more
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Specific Monoclonal Antibody Against the Nuclear Pore Complex Protein, Nup98
Hybridoma, 2005Nup98 is a component of nuclear pore complexes, which are large protein assemblies embedded in the nuclear envelope. Previous studies have shown that Nup98 interacts with several transport factors and plays a critical part in nuclear trafficking. However, the mechanism by which Nup98 contributes to nuclear trafficking is not clear.
Takaomi, Fukuhara +6 more
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Chemically Induced Nuclear Pore Complex Protein Degradation via TRIM21
ACS Chemical BiologyDespite the exciting progress of bifunctional degrader molecules, also known as proteolysis-targeting chimeras (PROTACs), the rapidly expanding field is still significantly hampered by the lack of available E3 ligase ligands. Our research bridges this gap by uncovering a series of small-molecule ligands to the E3 ligase TRIM21 through DNA-Encoded ...
Xiaomei Li +23 more
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Characterisation of nuclear pore complex oxalate binding protein from human kidney
Molecular and Cellular Biochemistry, 2003Both rat and human kidney nuclei exhibited time and pH dependent oxalate or histone-oxalate uptake which was inhibited by anion transport inhibitor, 4,4'-dithiocyanostilbene-2,2'-disulphonic acid. Sodium chloride had no effect. Nuclear membrane had oxalate binding at pH 7.4.
R, Selvam, R, Vijaya, P, Sivakamasundari
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Analysis of Ubiquitylation and SUMOylation of Yeast Nuclear Pore Complex Proteins
2022Posttranslational modifications and in particular ubiquitylation and SUMOylation of the nuclear pore complex (NPC), have been shown to regulate some of its functions, particularly in response to diverse stress signals.Although proteomic approaches are extremely powerful to identify substrates and modification sites, dissecting specific mechanisms and ...
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Protein phase separation of plant nuclear pore complex
Molecular Plant, 2023Kentaro, Tamura, Masaya, Koide
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