| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8261309 | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease | 2012 | 11 Pages |
Abstract
⺠GCK-MODY mutations S263P and G264S cause reduced GK catalytic activity (S263P < G264S). ⺠The mutations cause misfolded proteins (S263P > G264S). ⺠The mutant proteins self-associate (G264S > S263P) and form homodimers/aggregates. ⺠Prevention of self-association may represent new therapeutic approach.
Keywords
α-d-glucosePDBGlcRRLHEK293MIN6GKRPhGKTEV proteaseDimerizationTobacco etch virus proteaseDegradationSelf-associationMaturity-onset diabetes of the youngrabbit reticulocyte lysatehuman embryonic kidney 293 cellsubiquitin–proteasome systemProtein misfoldingCatalytic activityMODYAntibodyProtein Data BankGlucokinase regulatory proteinPNSGlucokinaseUPS
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Authors
Maria Negahdar, Ingvild Aukrust, Bente B. Johansson, Janne Molnes, Anders Molven, Franz M. Matschinsky, Oddmund Søvik, Rohit N. Kulkarni, Torgeir Flatmark, Pål Rasmus Njølstad, Lise Bjørkhaug,