Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import (Q27865295)

4

object named as

P Palese

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author name string

R Jaskunas

2

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R E O'Neill

1

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J Moroianu

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

29 September 1995

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published in

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Microinjected U snRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways

PubMed

volume

270

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page(s)

22701-4

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issue

39

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cites work

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Influenza virus, an RNA virus, synthesizes its messenger RNA in the nucleus of infected cells

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Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel

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Identification of the sequence responsible for the nuclear accumulation of the influenza virus nucleoprotein in Xenopus oocytes

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Complex structure of the nuclear translocation signal of influenza virus polymerase PA subunit

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NPI-1, the human homolog of SRP-1, interacts with influenza virus nucleoprotein

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Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes

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Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins

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The GTP-binding protein Ran/TC4 is required for protein import into the nucleus

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Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein

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

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The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors

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N protein of vesicular stomatitis virus selectively encapsidates leader RNA in vitro

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