The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore.
about
eEF1A is a novel component of the mammalian nuclear protein export machineryCrystal structure of the N-terminal domain of the human protooncogene Nup214/CANCrystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architectureStructural and Functional Studies of Nup107/Nup133 Interaction and Its Implications for the Architecture of the Nuclear Pore ComplexStructural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA exportStructure of a Yeast Dyn2-Nup159 Complex and Molecular Basis for Dynein Light Chain-Nuclear Pore InteractionMolecular Basis for the Anchoring of Proto-Oncoprotein Nup98 to the Cytoplasmic Face of the Nuclear Pore ComplexThe Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores.Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex.Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex.Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiaeThe yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexesThe mitogen-activated protein kinase Slt2 regulates nuclear retention of non-heat shock mRNAs during heat shock-induced stress.Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export.The splicing ATPase prp43p is a component of multiple preribosomal particles.Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export.Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance.Gonadotropin-regulated testicular RNA helicase (GRTH/Ddx25) is a transport protein involved in gene-specific mRNA export and protein translation during spermatogenesisHuman Nup98 regulates the localization and activity of DExH/D-box helicase DHX9Compositionally distinct nuclear pore complexes of functionally distinct dimorphic nuclei in the ciliate TetrahymenaIdentification and analysis of LNO1-like and AtGLE1-like nucleoporins in plantsNucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complexSimple fold composition and modular architecture of the nuclear pore complex.Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.Biology and biophysics of the nuclear pore complex and its componentsThe yeast nuclear pore complex and transport through itNuclear Export of Pre-Ribosomal Subunits Requires Dbp5, but Not as an RNA-Helicase as for mRNA Export.Interactome Mapping Reveals the Evolutionary History of the Nuclear Pore Complex.P(I) Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)Multiple recognition motifs in nucleoporin Nup159 provide a stable and rigid Nup159-Dyn2 assembly.In vivo analysis of human nucleoporin repeat domain interactions.Synthetic genetic array analysis in Saccharomyces cerevisiae provides evidence for an interaction between RAT8/DBP5 and genes encoding P-body components.Towards reconciling structure and function in the nuclear pore complex.Nuclear pore proteins and cancerThe nuclear pore complex has entered the atomic age.Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.mRNA nuclear export at a glance.
P2860
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P2860
The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@ast
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@en
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@nl
type
label
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@ast
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@en
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@nl
prefLabel
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@ast
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@en
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@nl
P2093
P1433
P1476
The N-terminal domain of Nup15 ...... case Dbp5 to the nuclear pore.
@en
P2093
Christine S Weirich
James M Berger
Jan P Erzberger
P304
P356
10.1016/J.MOLCEL.2004.10.032
P407
P50
P577
2004-12-03T00:00:00Z