Results 231 to 240 of about 97,972 (258)
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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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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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The nuclear pore complex: a protein machine bridging the nucleus and cytoplasm
Current Opinion in Cell Biology, 2000Compositional analysis of nuclear pore complexes (NPCs) is nearing completion, and efforts are now focused on understanding how these protein machines work. Recent analysis of soluble transport factor interactions with NPC proteins reveals distinct and overlapping pathways for movement between the nucleus and cytoplasm. New fluorescence- and microscopy-
K J, Ryan, S R, Wente
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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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Experimental Cell Research, 1998
Tpr is a 267-kDa protein of unknown function recently identified as a constitutive component of the nuclear pore complex (NPC2)-attached intranuclear filaments. Secondary structure predictions suggest that the protein is divided into a large, coiled-coil forming aminoterminal domain and a shorter, highly acidic carboxyterminal domain. To identify which
V C, Cordes, M E, Hase, L, Müller
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Tpr is a 267-kDa protein of unknown function recently identified as a constitutive component of the nuclear pore complex (NPC2)-attached intranuclear filaments. Secondary structure predictions suggest that the protein is divided into a large, coiled-coil forming aminoterminal domain and a shorter, highly acidic carboxyterminal domain. To identify which
V C, Cordes, M E, Hase, L, Müller
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Immunolocalization of lamins and nuclear pore complex proteins by atomic force microscopy
Pfl�gers Archiv European Journal of Physiology, 1995The nuclear envelope functions as a selective barrier separating the nuclear from the cytosolic compartment. Nuclear pore complexes (NPCs) mediate nuclear import and export of macromolecules and, therefore, are potential regulators of gene expression.
S, Schneider +3 more
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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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Protein phase separation of plant nuclear pore complex
Molecular Plant, 2023Kentaro, Tamura, Masaya, Koide
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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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