Conformational Changes in Glycogen Phosphorylase Studied with a Spin-Label Probe
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb10016.x/fullpdf
Reference19 articles.
1. 1. D. J. Graves, J. H. Wang, P. D. Boyer, H. Lardy, and K. Myrback (1972 ) The Enzymes , 3rd edn. () vol. 7 , pp.435 -482 , Academic Press, New York.
2. Kinetic Studies of the Activation of Muscle Phosphorylase Phosphatase
3. Inhibition of the phosphorylase kinase catalyzed reaction by glucose-6-P
4. Studies on the Interaction of Ligands with Phosphorylase b Using a Spin-Label Probe
5. A spin label probe for the conformational change on conversion of phosphorylasebto phosphorylasea
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3. Control of phosphorylasebconformation by a modified cofactor: Crystallographic studies on R-state glycogen phosphorylase reconstituted with pyridoxal 5′-diphosphate;Protein Science;1992-09
4. The ammonium sulfate activation of phosphorylaseb;FEBS Letters;1990-02-12
5. The binding of β-glycerophosphate to glycogen phosphorylase b in the crystal;Archives of Biochemistry and Biophysics;1989-04
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