The design of potential antidiabetic drugs: experimental investigation of a number of beta-D-glucose analogue inhibitors of glycogen phosphorylase

Autor: Maria Kontou, H. S. Tsitoura, Louise N. Johnson, K.R. Acharya, C. J. F. Bichard, K.A. Watson, Spyros E. Zographos, Demetres D. Leonidas, E. P. Mitchell, George W. J. Fleet, Nikos G. Oikonomakos, Jong Chan Son

alpha-D-glucose is a weak inhibitor (Ki = 1.7 mM) of glycogen phosphorylase (GP) and acts as physiological regulator of hepatic glycogen metabolism; it binds to GP at the catalytic site and stabilizes the inactive T state of the enzyme promoting the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17b4e8773c0f89d62eb8d10ee6f38a0b
https://doi.org/10.1007/bf03188920

Structural analysis of the anaphase-promoting complex reveals multiple active sites and insights into polyubiquitylation

Autor: Wah Chiu, Catherine Vénien-Bryan, Céline Fioretto, Louise N. Johnson, Steven J. Ludtke, Christopher R. Booth, David Barford, Lori A. Passmore

The anaphase-promoting complex/cyclosome (APC/C) is an E3 ubiquitin ligase composed of approximately 13 distinct subunits required for progression through meiosis, mitosis, and the G1 phase of the cell cycle. Despite its central role in these process

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e2cbffdbbc881e10a58ae3e0d09c516
https://doi.org/10.1016/j.molcel.2005.11.003

The Structural Basis for Control of Eukaryotic Protein Kinases

Autor: Louise N. Johnson, Martin E.M. Noble, Jane A. Endicott

Publikováno v: Annual Review of Biochemistry. 81:587-613

Eukaryotic protein kinases are key regulators of cell processes. Comparison of the structures of protein kinase domains, both alone and in complexes, allows generalizations to be made about the mechanisms that regulate protein kinase activation. Prot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2287f8af1274d68d13bb8e5106a55912
https://doi.org/10.1146/annurev-biochem-052410-090317

The regulation of protein phosphorylation

Autor: Louise N. Johnson

Publikováno v: Biochemical Society Transactions. 37:627-641

Phosphorylation plays essential roles in nearly every aspect of cell life. Protein kinases regulate signalling pathways and cellular processes that mediate metabolism, transcription, cell-cycle progression, differentiation, cytoskeleton arrangement a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eda2bf1e04dc3682ff8605a1da6b48b
https://doi.org/10.1042/bst0370627

The Structure of Phosphorylase Kinase Holoenzyme at 9.9 Å Resolution and Location of the Catalytic Subunit and the Substrate Glycogen Phosphorylase

Autor: Nicolas Boisset, Catherine Vénien-Bryan, Nikos G. Oikonomakos, Slavica Jonic, Nicolas Bischler, Louise N. Johnson, Vasiliki Skamnaki, Nick Brown

Publikováno v: Structure
Structure, Elsevier (Cell Press), 2009, 17, pp.117-127. ⟨10.1016/j.str.2008.10.013⟩
Structure(London, England:1993)
Structure, 2009, 17, pp.117-127. ⟨10.1016/j.str.2008.10.013⟩

Phosphorylase kinase (PhK) coordinates hormonal and neuronal signals to initiate the breakdown of glycogen. The enzyme catalyzes the phosphorylation of inactive glycogen phosphorylase b (GPb), resulting in the formation of active glycogen phosphoryla

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1aeebf806dbb0b7a5431b9ea4a6c62b4