Phosphorylation at serine 482 affects stability of NF90 and its functional role in mitosis.

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Regulation of AU-Rich Element RNA Binding Proteins by Phosphorylation and the Prolyl Isomerase Pin1 Induction of p53, p21 and apoptosis by silencing the NF90/NF45 complex in human papilloma virus-transformed cervical carcinoma cells.Ilf3 and NF90 functions in RNA biology.

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Phosphorylation at serine 482 affects stability of NF90 and its functional role in mitosis.

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http://www.wikidata.org/entity/Q39576474

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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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2011年论文

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name

Phosphorylation at serine 482 ...... ts functional role in mitosis.

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Phosphorylation at serine 482 ...... ts functional role in mitosis.

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type

Item

label

Phosphorylation at serine 482 ...... ts functional role in mitosis.

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Phosphorylation at serine 482 ...... ts functional role in mitosis.

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prefLabel

Phosphorylation at serine 482 ...... ts functional role in mitosis.

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Phosphorylation at serine 482 ...... ts functional role in mitosis.

@nl

P1476

Phosphorylation at serine 482 ...... ts functional role in mitosis.

@en

P2093

N L Smith

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

W K Miskimins

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P2860

DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR

The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells

Large-scale characterization of HeLa cell nuclear phosphoproteins

Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90

Identification of novel M phase phosphoproteins by expression cloning

DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45

ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing

Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope

A quantitative atlas of mitotic phosphorylation

Nuclear factor-90 of activated T-cells: A double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR

P304

147-155

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P31

scholarly article

P356

10.1111/J.1365-2184.2011.00742.X

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P478

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

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2011-04-01T00:00:00Z

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21401756

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P921

phosphorylation

P932

5609450

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Phosphorylation at serine 482 affects stability of NF90 and its functional role in mitosis.

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P2860

P2860

Phosphorylation at serine 482 affects stability of NF90 and its functional role in mitosis.

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type

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P1433

P1476

P2093

P2860

P304

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P356

P433

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P577

P698

P921

P932

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P1433

P1476

P2093

P2860

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P31

P356

P433

P478

P577

P698

P921

P932