The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1 - Wikidata - wikimedia - TriplyDB

The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1

The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1

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Multiple Export Mechanisms for mRNAs RNA Export through the NPC in Eukaryotes Postage for the messenger: designating routes for nuclear mRNA export Structure of a Yeast Dyn2-Nup159 Complex and Molecular Basis for Dynein Light Chain-Nuclear Pore Interaction Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1bulletNup98)Altered RNA processing and export lead to retention of mRNAs near transcription sites and nuclear pore complexes or within the nucleolus.The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1 Nuclear export of messenger RNA Nuclear export of single native mRNA molecules observed by light sheet fluorescence microscopy.Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex Regulation of mRNA trafficking by nuclear pore complexes.Insights into mRNP biogenesis provided by new genetic interactions among export and transcription factors An agent-based model for mRNA export through the nuclear pore complex.A single molecule view on Dbp5 and mRNA at the nuclear pore.RNA export factor Ddx19 is required for nuclear import of the SRF coactivator MKL1 Cytoplasmic hGle1A regulates stress granules by modulation of translation.Gle1 is a multifunctional DEAD-box protein regulator that modulates Ded1 in translation initiation A zebrafish model of lethal congenital contracture syndrome 1 reveals Gle1 function in spinal neural precursor survival and motor axon arborization.Nuclear 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.Cellular RNA helicases and HIV-1: insights from genome-wide, proteomic, and molecular studies P(I) Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivo Roles of helicases in translation initiation: a mechanistic view.Influenza A Virus Polymerase Recruits the RNA Helicase DDX19 to Promote the Nuclear Export of Viral mRNAs.Dbp5, Gle1-IP6 and Nup159: a working model for mRNP export.Multiscale dynamics in nucleocytoplasmic transport.To the pore and through the pore: a story of mRNA export kinetics.Insights into mRNA export-linked molecular mechanisms of human disease through a Gle1 structure-function analysis.Nuclear trafficking in health and disease.Emerging mechanisms of mRNP remodeling regulation.Control of mammalian gene expression by selective mRNA export.Temporal and spatial regulation of mRNA export: Single particle RNA-imaging provides new tools and insights.The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation.RNA helicase DDX19 stabilizes ribosomal elongation and termination complexes.Regulation of the Dbp5 ATPase cycle in mRNP remodeling at the nuclear pore: a lively new paradigm for DEAD-box proteins Size matters in RNA export.Nup42 and IP6 coordinate Gle1 stimulation of Dbp5/DDX19B for mRNA export in yeast and human cells.Gle1 regulates RNA binding of the DEAD-box helicase Ded1 in its complex role in translation initiation.An ATR-dependent function for the Ddx19 RNA helicase in nuclear R-loop metabolism.

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The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1

http://www.wikidata.org/entity/Q39541546

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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name

The Dbp5 cycle at the nuclear ...... key steps for Nup159 and Gle1

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The Dbp5 cycle at the nuclear ...... key steps for Nup159 and Gle1.

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type

label

The Dbp5 cycle at the nuclear ...... key steps for Nup159 and Gle1

@en

The Dbp5 cycle at the nuclear ...... key steps for Nup159 and Gle1.

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prefLabel

The Dbp5 cycle at the nuclear ...... key steps for Nup159 and Gle1

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The Dbp5 cycle at the nuclear ...... key steps for Nup159 and Gle1.

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Genes & Development

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The Dbp5 cycle at the nuclear ...... key steps for Nup159 and Gle1

@en

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Abel R Alcazar-Roman

http://www.w3.org/2001/XMLSchema#string

Andrew W Folkmann

http://www.w3.org/2001/XMLSchema#string

Charles N Cole

http://www.w3.org/2001/XMLSchema#string

Christine A Hodge

http://www.w3.org/2001/XMLSchema#string

John J Scarcelli

http://www.w3.org/2001/XMLSchema#string

Kristen N Noble

http://www.w3.org/2001/XMLSchema#string

Rakefet Ben-Yishay

http://www.w3.org/2001/XMLSchema#string

Susan R Wente

http://www.w3.org/2001/XMLSchema#string

Yaron Shav-Tal

http://www.w3.org/2001/XMLSchema#string

P2860

Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p

The human homologue of Saccharomyces cerevisiae Gle1p is required for poly(A)+ RNA export

The mRNA export factor Gle1 and inositol hexakisphosphate regulate distinct stages of translation

The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p

mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain

RNA helicases at work: binding and rearranging

SR proteins in vertical integration of gene expression from transcription to RNA processing to translation

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner

The DEXD/H-box RNA Helicase DDX19 Is Regulated by an -Helical Switch

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1052-1064

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scholarly article

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10.1101/GAD.2041611

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10

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25

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Elizabeth J. Tran

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2011-05-01T00:00:00Z

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51130602

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21576265

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3093121

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