Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly(A) RNA-binding protein 2 (Nab2) is required for correct mRNA 3'-end formation. - Wikidata - awgldk - TriplyDB

Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly(A) RNA-binding protein 2 (Nab2) is required for correct mRNA 3'-end formation.

Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly(A) RNA-binding protein 2 (Nab2) is required for correct mRNA 3'-end formation.

http://www.wikidata.org/entity/Q42120315

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Splice variants of the human ZC3H14 gene generate multiple isoforms of a zinc finger polyadenosine RNA binding protein The long and the short of it: the role of the zinc finger polyadenosine RNA binding protein, Nab2, in control of poly(A) tail length Structural Basis for Polyadenosine-RNA Binding by Nab2 Zn Fingers and Its Function in mRNA Nuclear Export Structural basis for the molecular recognition of polyadenosine RNA by Nab2 Zn fingers The mitogen-activated protein kinase Slt2 regulates nuclear retention of non-heat shock mRNAs during heat shock-induced stress.The poly(A)-binding protein Nab2 functions in RNA polymerase III transcription Mutation of the conserved polyadenosine RNA binding protein, ZC3H14/dNab2, impairs neural function in Drosophila and humans Links between mRNA splicing, mRNA quality control, and intellectual disability Harnessing natural sequence variation to dissect posttranscriptional regulatory networks in yeast Poly(A) RNA-binding proteins and polyadenosine RNA: new members and novel functions.Two Conserved Cysteine Residues Are Required for the Masculinizing Activity of the Silkworm Masc Protein.The Evolutionarily-conserved Polyadenosine RNA Binding Protein, Nab2, Cooperates with Splicing Machinery to Regulate the Fate of pre-mRNA.A conserved role for the zinc finger polyadenosine RNA binding protein, ZC3H14, in control of poly(A) tail length.New kid on the ID block: neural functions of the Nab2/ZC3H14 class of Cys₃His tandem zinc-finger polyadenosine RNA binding proteins.The Conserved, Disease-Associated RNA Binding Protein dNab2 Interacts with the Fragile X Protein Ortholog in Drosophila Neurons.Structural basis for the dimerization of Nab2 generated by RNA binding provides insight into its contribution to both poly(A) tail length determination and transcript compaction in Saccharomyces cerevisiae Poly(A) tail-mediated gene regulation by opposing roles of Nab2 and Pab2 nuclear poly(A)-binding proteins in pre-mRNA decay.The RNA-binding protein, ZC3H14, is required for proper poly(A) tail length control, expression of synaptic proteins, and brain function in mice.

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Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly(A) RNA-binding protein 2 (Nab2) is required for correct mRNA 3'-end formation.

http://www.wikidata.org/entity/Q42120315

description

2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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2010年论文

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name

Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly

@nl

Recognition of polyadenosine R ...... correct mRNA 3'-end formation.

@en

type

label

Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly

@nl

Recognition of polyadenosine R ...... correct mRNA 3'-end formation.

@en

prefLabel

Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly

@nl

Recognition of polyadenosine R ...... correct mRNA 3'-end formation.

@en

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JBC.M110.141127

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Journal of Biological Chemistry

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Recognition of polyadenosine R ...... correct mRNA 3'-end formation

@en

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Anita H Corbett

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Anna M Bramley

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Luciano H Apponi

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

Sara W Leung

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Seth M Kelly

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Susan R Wente

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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

Splice variants of the human ZC3H14 gene generate multiple isoforms of a zinc finger polyadenosine RNA binding protein

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

Molecular dissection of mRNA poly(A) tail length control in yeast

Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression

Structure of the N-Terminal Mlp1-Binding Domain of the Saccharomyces cerevisiae mRNA-Binding Protein, Nab2

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

Structural basis for the assembly of a nuclear export complex.

The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export.

Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export

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26022-26032

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scholarly article

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10.1074/JBC.M110.141127

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34

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285

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Elizabeth J. Tran

Julia A Chekanova

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2010-06-16T00:00:00Z

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20554526

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2924000

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