Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement (Q45446229)

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scientific article published in August 2005

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English	Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement	scientific article published in August 2005

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scholarly article

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Europe PubMed Central

PubMed publication ID

14 December 2017

Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement (English)

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Europe PubMed Central

PubMed publication ID

14 December 2017

1 reference

based on heuristic

inferred from title

mutational analysis

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based on heuristic

inferred from title

Prunus necrotic ringspot virus

object named as

Prunus necrotic ringspot virus

1 reference

based on heuristic

inferred from title

Ismael Mingarro

4

1 reference

Europe PubMed Central

PubMed publication ID

14 December 2017

author name string

Ma Carmen Herranz

1

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Europe PubMed Central

PubMed publication ID

14 December 2017

Jesús-Angel Sanchez-Navarro

2

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Europe PubMed Central

PubMed publication ID

14 December 2017

Ana Saurí

3

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Europe PubMed Central

PubMed publication ID

14 December 2017

Vicente Pallás

5

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Europe PubMed Central

PubMed publication ID

14 December 2017

language of work or name

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publication date

1 August 2005

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Europe PubMed Central

PubMed publication ID

14 December 2017

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Europe PubMed Central

PubMed publication ID

14 December 2017

339

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Europe PubMed Central

PubMed publication ID

14 December 2017

1

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Europe PubMed Central

PubMed publication ID

14 December 2017

31-41

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Europe PubMed Central

PubMed publication ID

14 December 2017

The coat protein of prunus necrotic ringspot virus specifically binds to and regulates the conformation of its genomic RNA.

1 reference

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RNA-binding properties and mapping of the RNA-binding domain from the movement protein of Prunus necrotic ringspot virus.

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The C-terminal 33 amino acids of the cucumber mosaic virus 3a protein affect virus movement, RNA binding and inhibition of infection and translation

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Comparison of the nucleic acid- and NTP-binding properties of the movement protein of cucumber mosaic cucumovirus and tobacco mosaic tobamovirus.

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Human leukocyte interferon does not inhibit alfalfa mosaic virus in protoplasts or tobacco tissue

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Plasmodesmata: intercellular channels for macromolecular transport in plants

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In VivoDetection, RNA-Binding Properties and Characterization of the RNA-Binding Domain of the p7 Putative Movement Protein from Carnation Mottle Carmovirus (CarMV)

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Tobacco mosaic virus movement protein associates with the cytoskeleton in tobacco cells

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The '30K' superfamily of viral movement proteins

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Cell-to-cell movement of plant viruses. Insights from amino acid sequence comparisons of movement proteins and from analogies with cellular transport systems

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Cauliflower mosaic virus gene I product (P1) forms tubular structures which extend from the surface of infected protoplasts

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Molecular studies on bromovirus capsid protein. III. Analysis of cell-to-cell movement competence of coat protein defective variants of cowpea chlorotic mottle virus

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Role of the alfalfa mosaic virus movement protein and coat protein in virus transport

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Nucleotide sequence of apple mosaic ilarvirus RNA 4.

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Evolutionary relationships in the ilarviruses: nucleotide sequence of prunus necrotic ringspot virus RNA 3.

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Binding of RNA by the alfalfa mosaic virus movement protein is biphasic

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10.1016/J.VIROL.2005.05.020

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Europe PubMed Central

PubMed publication ID

14 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

14 December 2017

ResearchGate publication ID

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