The regulation of the interaction between F-actin and muscle fructose 1,6-bisphosphatase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Biochemistry,Structural Biology
Reference31 articles.
1. Kinetic properties of d-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle
2. Muscle Aldolase Decreases Muscle FBPase Sensitivity toward AMP Inhibition
3. Rabbit muscle fructose-1,6-bisphosphatase is phosphorylatedin vivo.
4. Glycogen synthesis from lactate in the three types of skeletal muscle.
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1. Destabilization of fructose 1,6-bisphosphatase–Z-line interactions is a mechanism of glyconeogenesis down-regulation in vivo;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2013-03
2. Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase;Proteins: Structure, Function, and Bioinformatics;2008-01-23
3. Changes in subcellular localization of fructose 1,6-bisphosphatase during differentiation of isolated muscle satellite cells;FEBS Letters;2006-06-27
4. Subcellular localization of muscle FBPase in carp (Cyprinus carpio) tissues;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2006-06
5. The origin of the high sensitivity of muscle fructose 1,6-bisphosphatase towards AMP;FEBS Letters;2005-09-28
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