Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98 (Q28139522)

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2 November 2019

title

Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98 (English)

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2 November 2019

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2 November 2019

von Kobbe C

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2 November 2019

van Deursen JM

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2 November 2019

J P Rodrigues

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2 November 2019

D Sitterlin

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2 November 2019

X Wu

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2 November 2019

M Carmo-Fonseca

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E Izaurralde

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2 November 2019

language of work or name

English

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publication date

1 November 2000

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2 November 2019

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volume

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issue

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2 November 2019

page(s)

1243-1252

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Effect of vesicular stomatitis virus matrix protein on transcription directed by host RNA polymerases I, II, and III.

2 November 2019

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The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates

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Targeting and function in mRNA export of nuclear pore complex protein Nup153.

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Vesicular stomatitis virus matrix protein inhibits host cell-directed transcription of target genes in vivo

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Role of matrix protein in cytopathogenesis of vesicular stomatitis virus.

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A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo

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The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs

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A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96

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Rapid inhibition of processing and assembly of small nuclear ribonucleoproteins after infection with vesicular stomatitis virus

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TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus

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Monomethylated cap structures facilitate RNA export from the nucleus

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Inhibition of Ran guanosine triphosphatase-dependent nuclear transport by the matrix protein of vesicular stomatitis virus

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Regulation of nuclear localization: a key to a door

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Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA.

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CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity

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RNP export is mediated by structural reorganization of the nuclear pore basket.

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Vesicular stomatitis virus M protein in the nuclei of infected cells

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Interaction between tubulin and the viral matrix protein of vesicular stomatitis virus: possible implications in the viral cytopathic effect

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Differential detergent treatment allows immunofluorescent localization of the Newcastle disease virus matrix protein within the nucleus of infected cells

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7 January 2021

Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication

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7 January 2021

The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways

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RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains

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7 January 2021

The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex

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Consolidated OpenCitations Corpus – April 2017

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2 November 2019

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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