(Q45758504)

English

The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase

scientific article published in January 1998

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase (English)

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

author name string

Langelier Y

1

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Champoux L

2

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Hamel M

3

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Guilbault C

4

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Lamarche N

5

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Gaudreau P

6

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Massie B

7

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

language of work or name

0 references

publication date

1 January 1998

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

273

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

3

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

1435-1443

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Structural features of ribonucleotide reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The unique N terminus of the herpes simplex virus type 1 large subunit is not required for ribonucleotide reductase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Identification of structural domains within the large subunit of herpes simplex virus ribonucleotide reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Epitope mapping identifies an exposed loop between the unique amino- and conserved carboxy-domains of the large subunit of herpes simplex virus type 1 ribonucleotide reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The herpes simplex virus type 1 ribonucleotide reductase is a tight complex of the type alpha 2 beta 2 composed of 40K and 140K proteins, of which the latter shows multiple forms due to proteolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Improved adenovirus vector provides herpes simplex virus ribonucleotide reductase R1 and R2 subunits very efficiently

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The large subunit of herpes simplex virus type 1 ribonucleotide reductase: Expression in Escherichia coli and purification

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The novel protein kinase of the RR1 subunit of herpes simplex virus has autophosphorylation and transphosphorylation activity that differs in its ATP requirements for HSV-1 and HSV-2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Phosphopeptide mapping and phosphoamino acid analysis by electrophoresis and chromatography on thin-layer cellulose plates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Measurement of picomoles of phosphoamino acids by high-performance liquid chromatography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

An ultrafiltration assay for nucleotide binding to ribonucleotide reductase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

ATP-dependent protein kinases in bacteria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

One-dimensional gel electrophoresis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-293, and T-291 and is required for its degradation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Casein kinase II binds to and phosphorylates cytoplasmic dynein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The BCR gene encodes a novel serine/threonine kinase activity within a single exon

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The 140-kDa RR1 protein from both HSV-1 and HSV-2 contains an intrinsic protein kinase activity capable of autophosphorylation but it is transphosphorylation defective

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Localization of the antigenic sites and intrinsic protein kinase domain within a 300 amino acid segment of the ribonucleotide reductase large subunit from herpes simplex virus type 2

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Myristylation and polylysine-mediated activation of the protein kinase domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

ATP and SH3 binding sites in the protein kinase of the large subunit of herpes simplex virus type 2 of ribonucleotide reductase (ICP10).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

The transmembrane domain of the large subunit of HSV-2 ribonucleotide reductase (ICP10) is required for protein kinase activity and transformation-related signaling pathways that result in ras activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Conformation-dependent phosphorylation of p53.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.3.1435

21 January 2018

Identifiers

10.1074/JBC.273.3.1435

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9430680

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q45758504&oldid=2081320008"