Intracellular processing of the Sendai virus C' protein leads to the generation of a Y protein module: structure-functional implications.

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Proteolytic products of the porcine reproductive and respiratory syndrome virus nsp2 replicase protein.Evolution and structural organization of the C proteins of paramyxovirinae.

P2860

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P2860

Intracellular processing of the Sendai virus C' protein leads to the generation of a Y protein module: structure-functional implications.

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2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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Intracellular processing of th ...... cture-functional implications.

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Intracellular processing of th ...... cture-functional implications.

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Item

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Intracellular processing of th ...... cture-functional implications.

@en

Intracellular processing of th ...... cture-functional implications.

@nl

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Intracellular processing of th ...... cture-functional implications.

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Intracellular processing of th ...... cture-functional implications.

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P1476

Intracellular processing of th ...... cture-functional implications.

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P2093

Joseph Curran

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

Romaine Stalder

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

Sylvain de Breyne

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P2860

"Rule of six": how does the Sendai virus RNA polymerase keep count?

Identification of a cis-acting element required for shunt-mediated translational initiation of the Sendai virus Y proteins.

Fusion of green fluorescent protein to the C-terminus of granulysin alters its intracellular localization in comparison to the native molecule

Intrinsically disordered protein

Versatility of the accessory C proteins of Sendai virus: contribution to virus assembly as an additional role.

Y2, the smallest of the Sendai virus C proteins, is fully capable of both counteracting the antiviral action of interferons and inhibiting viral RNA synthesis.

Regulation of CCAAT/enhancer-binding protein-beta isoform synthesis by alternative translational initiation at multiple AUG start sites

The amino-terminal extensions of the longer Sendai virus C proteins modulate pY701-Stat1 and bulk Stat1 levels independently of interferon signaling.

What does it mean to be natively unfolded?

All four Sendai Virus C proteins bind Stat1, but only the larger forms also induce its mono-ubiquitination and degradation.

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5685-5690

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

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scholarly article

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10.1016/J.FEBSLET.2005.09.052

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English

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

P478

579

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P577

2005-10-05T00:00:00Z

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P5875

7547389

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P698

16219307

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P921

Sendai virus

protein structure

Intracellular processing of the Sendai virus C' protein leads to the generation of a Y protein module: structure-functional implications.

about

P2860

P2860

Intracellular processing of the Sendai virus C' protein leads to the generation of a Y protein module: structure-functional implications.

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921