Differential mitotic phosphorylation of proteins of the nuclear pore complex. - Wikidata - awgldk - TriplyDB

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

http://www.wikidata.org/entity/Q46190811

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A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96 Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex Proteomic analysis of the mammalian nuclear pore complex Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay Mitosis, not just open or closed Nup358 integrates nuclear envelope breakdown with kinetochore assembly Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr Building a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p.Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p.Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexes Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p.A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis Nup98 is a mobile nucleoporin with transcription-dependent dynamics.Cdk1 and okadaic acid-sensitive phosphatases control assembly of nuclear pore complexes in Drosophila embryos.Systematic deletion and mitotic localization of the nuclear pore complex proteins of Aspergillus nidulans.An in vitro nuclear disassembly system reveals a role for the RanGTPase system and microtubule-dependent steps in nuclear envelope breakdown.Localization and dynamics of Cdc2-cyclin B during meiotic reinitiation in starfish oocytes A new model for nuclear envelope breakdown.Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor.Annulate lamellae play only a minor role in the storage of excess nucleoporins in Drosophila embryos.Function and assembly of nuclear pore complex proteins.Probing nuclear pore complex architecture with proximity-dependent biotinylation.Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid levels and interacts with the nucleoporin Nup62 RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.Phosphorylation of nucleoporin Tpr governs its differential localization and is required for its mitotic function RanGTP mediates nuclear pore complex assembly.A microtubule-independent role for centrosomes and aurora a in nuclear envelope breakdown Nuclear pore complexes: dynamics in unexpected places.Nucleoporin phosphorylation triggered by the encephalomyocarditis virus leader protein is mediated by mitogen-activated protein kinases

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P2860

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

http://www.wikidata.org/entity/Q46190811

description

1995 nî lūn-bûn

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1995年の論文

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年學術文章

@yue

1995年學術文章

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1995年學術文章

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name

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

@en

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

@nl

type

label

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

@en

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

@nl

prefLabel

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

@en

Differential mitotic phosphorylation of proteins of the nuclear pore complex.

@nl

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Journal of Biological Chemistry

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Differential mitotic phosphorylation of proteins of the nuclear pore complex

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D J Forbes

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E Meier

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P2860

Pathway of incorporation of microinjected lamin A into the nuclear envelope

O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation

Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway

A complex of nuclear pore proteins required for pore function

Steps in the assembly of replication-competent nuclei in a cell-free system from Xenopus eggs

Cyclin is degraded by the ubiquitin pathway

Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation

In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase

Identification and characterization of a nuclear pore complex protein

A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant.

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