Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II. (Q40499514)

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English	Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II.	scientific article

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scholarly article

1 reference

Europe PubMed Central

21 September 2017

Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II. (English)

1 reference

Europe PubMed Central

21 September 2017

African swine fever virus

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phosphorylation

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African swine fever

1 reference

based on heuristic

inferred from title

author name string

Sandra Stefanovic

1

1 reference

Europe PubMed Central

21 September 2017

Miriam Windsor

2

1 reference

Europe PubMed Central

21 September 2017

Koh-Ici Nagata

3

1 reference

Europe PubMed Central

21 September 2017

Masaki Inagaki

4

1 reference

Europe PubMed Central

21 September 2017

Thomas Wileman

5

1 reference

Europe PubMed Central

21 September 2017

language of work or name

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publication date

1 September 2005

1 reference

Europe PubMed Central

21 September 2017

Journal of Virology

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Europe PubMed Central

21 September 2017

79

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Europe PubMed Central

21 September 2017

18

1 reference

Europe PubMed Central

21 September 2017

11766-11775

1 reference

Europe PubMed Central

21 September 2017

Virus factories: associations of cell organelles for viral replication and morphogenesis

1 reference

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Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

1 reference

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The subcellular distribution of multigene family 110 proteins of African swine fever virus is determined by differences in C-terminal KDEL endoplasmic reticulum retention motifs

1 reference

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1 reference

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Membrane association facilitates the correct processing of pp220 during production of the major matrix proteins of African swine fever virus

1 reference

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1 reference

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1 reference

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African swine fever virus infection of porcine aortic endothelial cells leads to inhibition of inflammatory responses, activation of the thrombotic state, and apoptosis.

1 reference

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Aggresomes resemble sites specialized for virus assembly

1 reference

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1 reference

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1 reference

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African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum.

1 reference

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Rapid movements of vimentin on microtubule tracks: kinesin-dependent assembly of intermediate filament networks

1 reference

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Motile properties of vimentin intermediate filament networks in living cells

1 reference

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African swine fever virus is wrapped by the endoplasmic reticulum.

1 reference

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Involvement of the endoplasmic reticulum in the assembly and envelopment of African swine fever virus

1 reference

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Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes

1 reference

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1 reference

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1 reference

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1 reference

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Widespread occurrence of intermediate-sized filaments of the vimentin-type in cultured cells from diverse vertebrates

1 reference

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1 reference

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1 reference

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Differential targeting of protein kinase C and CaM kinase II signalings to vimentin

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Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure.

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1 reference

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/16140754

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1 reference

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Site-specific phosphorylation induces disassembly of vimentin filaments in vitro

1 reference

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The regulation of intermediate filament reorganization in mitosis. p34cdc2 phosphorylates vimentin at a unique N-terminal site

1 reference

https://pubmed.ncbi.nlm.nih.gov/16140754

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Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis

1 reference

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Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis

1 reference

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12 December 2020

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Identifiers

10.1128/JVI.79.18.11766-11775.2005

1 reference

Europe PubMed Central

21 September 2017

1 reference

Europe PubMed Central

21 September 2017

1 reference

Europe PubMed Central

21 September 2017

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