Proteomic Analysis of Rat Liver Phosphoproteins after Treatment with Protein Kinase Inhibitor H89 (N-(2-[p-Bromocinnamylamino-]ethyl)-5-isoquinolinesulfonamide)-Reference-Cited by-同舟云学术

Proteomic Analysis of Rat Liver Phosphoproteins after Treatment with Protein Kinase Inhibitor H89 (N-(2-[p-Bromocinnamylamino-]ethyl)-5-isoquinolinesulfonamide)

Published:2006-05-10 Issue:2 Volume:318 Page:589-595
ISSN:0022-3565
Container-title:Journal of Pharmacology and Experimental Therapeutics
language:en
Short-container-title:J Pharmacol Exp Ther

Author:

Davis Myrtle A.,Hinerfeld Douglas,Joseph Sajan,Hui Yu-Hua,Huang Naijia H.,Leszyk John,Rutherford-Bethard Jennifer,Tam Sun W.

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference26 articles.

1. Inhibition of Kv1.3 channels by H-89 (N-[2- (p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide) independent of protein kinase A11Abbreviations: AMP-PNP, 5′-adenylyl-imidodiphosphate; CHO, Chinese hamster ovary; H-89, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide; PKA, protein kinase A; PKC, protein kinase C; PKI 5-24, protein kinase A inhibitor 5-24; Rp-cAMPS, adenosine 3′, 5′-cyclic phosphorothioate-Rp

2. Biphasic modulation of nociceptive processing by the cyclic AMP-protein kinase A signalling pathway in sheep spinal cord

3. G2 arrest in Xenopus oocytes depends on phosphorylation of cdc25 by protein kinase A

4. Rat liver fructose-1,6-bisphosphatase. Identification of serine 338 as a third major phosphorylation site for cyclic AMP-dependent protein kinase and activity changes associated with multisite phosphorylation in vitro.

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