Nucleocytoplasmic shuttling of the rabies virus P protein requires a nuclear localization signal and a CRM1-dependent nuclear export signal (Q40444617)

20 September 2017

title

Nucleocytoplasmic shuttling of the rabies virus P protein requires a nuclear localization signal and a CRM1-dependent nuclear export signal (English)

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20 September 2017

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rabies virus

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6

Danielle Blondel

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20 September 2017

David Pasdeloup

1

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20 September 2017

Nicolas Poisson

2

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20 September 2017

Hélène Raux

3

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20 September 2017

Yves Gaudin

4

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20 September 2017

Rob W H Ruigrok

5

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20 September 2017

language of work or name

English

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publication date

1 April 2005

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20 September 2017

number of pages

10

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inferred from page(s)

published in

Virology

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20 September 2017

volume

334

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20 September 2017

issue

2

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20 September 2017

page(s)

284-293

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Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer

20 September 2017

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Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies.

7 January 2021

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In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): existence of two N-binding sites on P protein

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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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CRM1 is an export receptor for leucine-rich nuclear export signals

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Both the N- and the C-terminal domains of the nominal phosphoprotein of rabies virus are involved in binding to the nucleoprotein

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Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase

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Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization

7 January 2021

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Nucleocytoplasmic transport

7 January 2021

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Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope

7 January 2021

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The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C

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A novel nuclear export signal and a REF interaction domain both promote mRNA export by the Epstein-Barr virus EB2 protein.

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The protein kinase CK2 site (Ser111/112) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin

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Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein

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Sequence requirements for nuclear location of simian virus 40 large-T antigen

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Evidence for distinct substrate specificities of importin alpha family members in nuclear protein import

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Isolation and characterisation of the rabies virus N degrees-P complex produced in insect cells

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Interaction of the rabies virus P protein with the LC8 dynein light chain

7 January 2021

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Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence

7 January 2021

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Phosphorylation of the N and M1 proteins of rabies virus

7 January 2021

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Characterization of an unusual importin alpha binding motif in the borna disease virus p10 protein that directs nuclear import

7 January 2021

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Mapping the interacting domains between the rabies virus polymerase and phosphoprotein

7 January 2021

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Translation initiation at alternate in-frame AUG codons in the rabies virus phosphoprotein mRNA is mediated by a ribosomal leaky scanning mechanism.

7 January 2021

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inferred from DOI database lookup

7 January 2021

based on heuristic

The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VIROL.2005.02.005

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20 September 2017

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