The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. (Q45742612)

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scientific article published in May 2000

Language	Label	Description	Also known as
English	The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C.	scientific article published in May 2000

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. (English)

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

phosphorylation

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author name string

J Reinhardt

1

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

T Wolff

2

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

publication date

1 May 2000

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

number of pages

14

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inferred from page(s)

Veterinary Microbiology

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

74

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

1-2

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

87-100

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

Incorporation of influenza virus M-protein into liposomes

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RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells

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Influenza virus M1 protein binds to RNA through its nuclear localization signal

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Fine structure of influenza A virus observed by electron cryo-microscopy.

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7 January 2021

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The membrane (M1) protein of influenza virus occurs in two forms and is a phosphoprotein

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7 January 2021

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The phosphorylation of the integral membrane (M1) protein of influenza virus

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Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2

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Mechanism of influenza virus transcription inhibition by matrix (M1) protein

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The PROSITE database, its status in 1999

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7 January 2021

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Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling

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Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins

1 reference

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Differential phosphorylation of the nucleoprotein of influenza A viruses

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Membrane association of influenza virus matrix protein does not require specific hydrophobic domains or the viral glycoproteins

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Negative-strand virus M and retrovirus MA proteins: all in a family?

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Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit

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A fatal relationship--influenza virus interactions with the host cell

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Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import

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Localization of protein kinases by anchoring proteins: a theme in signal transduction

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The ancient regulatory-protein family of WD-repeat proteins

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The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins

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The Intracellular Distribution of Influenza Virus Matrix Protein and Nucleoprotein in Infected Cells and Their Relationship to Haemagglutinin in the Plasma Membrane

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Improved tools for biological sequence comparison

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The matrix 1 protein of influenza A virus inhibits the transcriptase activity of a model influenza reporter genome in vivo.

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7 January 2021

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Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins

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Electron microscopy of the influenza virus submembranal structure

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The WD repeat: a common architecture for diverse functions

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RNA-binding properties of influenza A virus matrix protein M1

1 reference

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The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform

1 reference

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Growth control of influenza A virus by M1 protein: analysis of transfectant viruses carrying the chimeric M gene

1 reference

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Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites

1 reference

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Characterization of the membrane association of the influenza virus matrix protein in living cells

1 reference

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based on heuristic

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Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent

1 reference

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1 reference

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7 January 2021

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inferred from DOI database lookup

Identifiers

10.1016/S0378-1135(00)00169-3

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/10799781

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