Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication.
about
A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein exportNucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basketDirect interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complexProteomic analysis of the mammalian nuclear pore complexProtein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusionThe t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filamentsNup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assemblyNucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1 RevThe nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteinsSteady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domainsNup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexesIdentification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assayDisruption of the FG nucleoporin NUP98 causes selective changes in nuclear pore complex stoichiometry and functionThe nucleoporin nup153 plays a critical role in multiple types of nuclear exportGradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear importMajor binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein TprBinding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export.The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factorNup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p.Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene.Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p.Nup98 is a mobile nucleoporin with transcription-dependent dynamics.Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates.Intranuclear dynamics of the Nup107-160 complex.Xenopus importin beta validates human importin beta as a cell cycle negative regulatorO-GlcNAc-ylation in the Nuclear Pore Complex.Effects of the NUP98-DDX10 oncogene on primary human CD34+ cells: role of a conserved helicase motifInhibition of CRM1-mediated nuclear export of transcription factors by leukemogenic NUP98 fusion proteins.Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.RNA association defines a functionally conserved domain in the nuclear pore protein Nup153.Nuclear envelope breakdown is coordinated by both Nup358/RanBP2 and Nup153, two nucleoporins with zinc finger modulesCaspases target only two architectural components within the core structure of the nuclear pore complex.Nup98 regulates bipolar spindle assembly through association with microtubules and opposition of MCAK.The nucleoporin Nup98 associates with the intranuclear filamentous protein network of TPR.Amino-terminal enhancer of split (AES) interacts with the oncoprotein NUP98-HOXA9 and enhances its transforming abilityNUP98 gene fusions and hematopoietic malignancies: common themes and new biologic insightsAnalysis of nuclear reconstitution, nuclear envelope assembly, and nuclear pore assembly using Xenopus in vitro assays.
P2860
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P2860
Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Reconstituted nuclei depleted ...... uclear growth and replication.
@ast
Reconstituted nuclei depleted ...... uclear growth and replication.
@en
type
label
Reconstituted nuclei depleted ...... uclear growth and replication.
@ast
Reconstituted nuclei depleted ...... uclear growth and replication.
@en
prefLabel
Reconstituted nuclei depleted ...... uclear growth and replication.
@ast
Reconstituted nuclei depleted ...... uclear growth and replication.
@en
P2093
P2860
P356
P1476
Reconstituted nuclei depleted ...... uclear growth and replication.
@en
P2093
C Macaulay
D J Forbes
F R Masiarz
M A Powers
P2860
P304
P356
10.1083/JCB.128.5.721
P407
P577
1995-03-01T00:00:00Z