97 related articles for article (PubMed ID: 12804778)
1. The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27.
Chabaud S; Lambert H; Sasseville AM; Lavoie H; Guilbault C; Massie B; Landry J; Langelier Y
FEBS Lett; 2003 Jun; 545(2-3):213-8. PubMed ID: 12804778
[TBL] [Abstract][Full Text] [Related]
2. The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function.
Chabaud S; Sasseville AM; Elahi SM; Caron A; Dufour F; Massie B; Langelier Y
J Gen Virol; 2007 Feb; 88(Pt 2):384-394. PubMed ID: 17251554
[TBL] [Abstract][Full Text] [Related]
3. Characterization of heterosubunit complexes formed by the R1 and R2 subunits of herpes simplex virus 1 and equine herpes virus 4 ribonucleotide reductase.
Sun Y; Conner J
Biochem J; 2000 Apr; 347 Pt 1(Pt 1):97-104. PubMed ID: 10727407
[TBL] [Abstract][Full Text] [Related]
4. The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8.
Dufour F; Sasseville AM; Chabaud S; Massie B; Siegel RM; Langelier Y
Apoptosis; 2011 Mar; 16(3):256-71. PubMed ID: 21107701
[TBL] [Abstract][Full Text] [Related]
5. Identification of structural domains within the large subunit of herpes simplex virus ribonucleotide reductase.
Conner J; Cross A; Murray J; Marsden H
J Gen Virol; 1994 Dec; 75 ( Pt 12)():3327-35. PubMed ID: 7996127
[TBL] [Abstract][Full Text] [Related]
6. Characterization of the novel protein kinase activity present in the R1 subunit of herpes simplex virus ribonucleotide reductase.
Cooper J; Conner J; Clements JB
J Virol; 1995 Aug; 69(8):4979-85. PubMed ID: 7609068
[TBL] [Abstract][Full Text] [Related]
7. The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation.
Langelier Y; Bergeron S; Chabaud S; Lippens J; Guilbault C; Sasseville AM; Denis S; Mosser DD; Massie B
J Gen Virol; 2002 Nov; 83(Pt 11):2779-2789. PubMed ID: 12388814
[TBL] [Abstract][Full Text] [Related]
8. The ribonucleotide reductase R1 subunits of herpes simplex virus 1 and 2 protect cells against poly(I · C)-induced apoptosis.
Dufour F; Bertrand L; Pearson A; Grandvaux N; Langelier Y
J Virol; 2011 Sep; 85(17):8689-701. PubMed ID: 21697465
[TBL] [Abstract][Full Text] [Related]
9. Herpes simplex virus type 1 ribonucleotide reductase large subunit: regions of the protein essential for subunit interaction and dimerization.
Conner J; Furlong J; Murray J; Meighan M; Cross A; Marsden H; Clements JB
Biochemistry; 1993 Dec; 32(49):13673-80. PubMed ID: 8257701
[TBL] [Abstract][Full Text] [Related]
10. A solid-phase assay for the binding of peptidic subunit association inhibitors to the herpes simplex virus ribonucleotide reductase large subunit.
Krogsrud RL; Welchner E; Scouten E; Liuzzi M
Anal Biochem; 1993 Sep; 213(2):386-94. PubMed ID: 8238915
[TBL] [Abstract][Full Text] [Related]
11. The unique N terminus of herpes simplex virus type 1 ribonucleotide reductase large subunit is phosphorylated by casein kinase 2, which may have a homologue in Escherichia coli.
Conner J
J Gen Virol; 1999 Jun; 80 ( Pt 6)():1471-1476. PubMed ID: 10374965
[TBL] [Abstract][Full Text] [Related]
12. Affinity of synthetic peptides for the HSV-2 ribonucleotide reductase R1 subunit measured with an iodinated photoaffinity peptide.
Lamarche N; Gaudreau P; Massie B; Langelier Y
Anal Biochem; 1994 Aug; 220(2):315-20. PubMed ID: 7978273
[TBL] [Abstract][Full Text] [Related]
13. 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.
Lankinen H; Everett R; Cross A; Conner J; Marsden HS
J Gen Virol; 1993 Sep; 74 ( Pt 9)():1871-7. PubMed ID: 7690841
[TBL] [Abstract][Full Text] [Related]
14. Resistance of herpes simplex virus type 1 to peptidomimetic ribonucleotide reductase inhibitors: selection and characterization of mutant isolates.
Bonneau AM; Kibler P; White P; Bousquet C; Dansereau N; Cordingley MG
J Virol; 1996 Feb; 70(2):787-93. PubMed ID: 8551616
[TBL] [Abstract][Full Text] [Related]
15. Herpes Simplex Virus 1 (HSV-1) and HSV-2 Mediate Species-Specific Modulations of Programmed Necrosis through the Viral Ribonucleotide Reductase Large Subunit R1.
Yu X; Li Y; Chen Q; Su C; Zhang Z; Yang C; Hu Z; Hou J; Zhou J; Gong L; Jiang X; Zheng C; He S
J Virol; 2016 Jan; 90(2):1088-95. PubMed ID: 26559832
[TBL] [Abstract][Full Text] [Related]
16. Intracellular localisation of herpes simplex virus type 1 ribonucleotide reductase subunits during infection of cultured cells.
Conner J; Murray J; Cross A; Clements JB; Marsden HS
Virology; 1995 Nov; 213(2):615-23. PubMed ID: 7491785
[TBL] [Abstract][Full Text] [Related]
17. Affinity purification of active subunit 1 of herpes simplex virus type 1 ribonucleotide reductase exhibiting a protein kinase activity.
Paradis H; Gaudreau P; Massie B; Lamarche N; Guilbault C; Gravel S; Langelier Y
J Biol Chem; 1991 May; 266(15):9647-51. PubMed ID: 1851753
[TBL] [Abstract][Full Text] [Related]
18. 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.
Peng T; Hunter JR; Nelson JW
Virology; 1996 Feb; 216(1):184-96. PubMed ID: 8614985
[TBL] [Abstract][Full Text] [Related]
19. Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant.
Ahmad MF; Raman B; Ramakrishna T; Rao ChM
J Mol Biol; 2008 Jan; 375(4):1040-51. PubMed ID: 18061612
[TBL] [Abstract][Full Text] [Related]
20. The unique N terminus of the herpes simplex virus type 1 large subunit is not required for ribonucleotide reductase activity.
Conner J; Macfarlane J; Lankinen H; Marsden H
J Gen Virol; 1992 Jan; 73 ( Pt 1)():103-12. PubMed ID: 1309856
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]