about
The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosisRanGTP and CLASP1 cooperate to position the mitotic spindle.Characterisation of the passive permeability barrier of nuclear pore complexesTopology of yeast Ndc1p: predictions for the human NDC1/NET3 homologueThe nuclear envelopeThe Nup107-160 nucleoporin complex is required for correct bipolar spindle assemblyRanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassemblyNDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexesCrosstalk between the actin cytoskeleton and Ran-mediated nuclear transport.The RanGTP Pathway: From Nucleo-Cytoplasmic Transport to Spindle Assembly and BeyondBuilding a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensationThe role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and functionER membrane-bending proteins are necessary for de novo nuclear pore formationFG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties.The nuclear GTPase Gsp1p can affect proper telomeric function through the Sir4 protein in Saccharomyces cerevisiae.The karyopherin Kap95 regulates nuclear pore complex assembly into intact nuclear envelopes in vivo.Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium.Inner/Outer nuclear membrane fusion in nuclear pore assembly: biochemical demonstration and molecular analysisOrigin of the nucleus and Ran-dependent transport to safeguard ribosome biogenesis in a chimeric cellMolecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells.Modulation of histone deposition by the karyopherin kap114Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1.Cdk1 and okadaic acid-sensitive phosphatases control assembly of nuclear pore complexes in Drosophila embryos.An in vitro nuclear disassembly system reveals a role for the RanGTPase system and microtubule-dependent steps in nuclear envelope breakdown.In vivo dynamics of Drosophila nuclear envelope components.Dynamic localisation of Ran GTPase during the cell cycle.Annulate lamellae play only a minor role in the storage of excess nucleoporins in Drosophila embryos.Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358.Xenopus importin beta validates human importin beta as a cell cycle negative regulatorNucleosomal regulation of chromatin composition and nuclear assembly revealed by histone depletion.Cell cycle-dependent differences in nuclear pore complex assembly in metazoaTransportin-1 and Transportin-2: protein nuclear import and beyond.Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphaseRequirement for lamin B receptor and its regulation by importin {beta} and phosphorylation in nuclear envelope assembly during mitotic exit.Nuclear envelope breakdown is coordinated by both Nup358/RanBP2 and Nup153, two nucleoporins with zinc finger modulesFunctional characterization of nuclear localization and export signals in hepatitis C virus proteins and their role in the membranous web.Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM.POM121 and Sun1 play a role in early steps of interphase NPC assemblyImportazole, a small molecule inhibitor of the transport receptor importin-βThe nuclear envelope: form and reformation.
P2860
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P2860
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
RanGTP mediates nuclear pore complex assembly.
@ast
RanGTP mediates nuclear pore complex assembly.
@en
RanGTP mediates nuclear pore complex assembly.
@en-gb
RanGTP mediates nuclear pore complex assembly.
@nl
type
label
RanGTP mediates nuclear pore complex assembly.
@ast
RanGTP mediates nuclear pore complex assembly.
@en
RanGTP mediates nuclear pore complex assembly.
@en-gb
RanGTP mediates nuclear pore complex assembly.
@nl
prefLabel
RanGTP mediates nuclear pore complex assembly.
@ast
RanGTP mediates nuclear pore complex assembly.
@en
RanGTP mediates nuclear pore complex assembly.
@en-gb
RanGTP mediates nuclear pore complex assembly.
@nl
P2093
P2860
P50
P356
P1433
P1476
RanGTP mediates nuclear pore complex assembly.
@en
P2093
Gareth Griffiths
Martin Hetzer
Tobias C Walther
P2860
P2888
P304
P356
10.1038/NATURE01898
P407
P577
2003-07-30T00:00:00Z
P6179
1016541026