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PLoS ONE, ISSN 1932-6203, 07/2013, Volume 8, Issue 7, p. e69420
Glycogen phosphorylase (GP) catalyzes the breakdown of glycogen and largely contributes to hepatic glucose production making GP inhibition an attractive target... 
CELLS | MULTIDISCIPLINARY SCIENCES | LIVER | MUSCLE | MICE | PROLIFERATION | UNCOUPLING PROTEIN-2 | GLUCOPYRANOSYLIDENE-SPIRO-THIOHYDANTOIN | CANCER | MTOR | REVEALS | Diabetes Mellitus, Experimental - drug therapy | Gene Expression - drug effects | TOR Serine-Threonine Kinases - metabolism | Diabetes Mellitus, Experimental - enzymology | Glucose - analogs & derivatives | Ion Channels - genetics | Male | Multiprotein Complexes - genetics | Mitochondrial Proteins - genetics | Mitochondrial Proteins - agonists | Enzyme Inhibitors - chemical synthesis | Mechanistic Target of Rapamycin Complex 2 | Urea - chemical synthesis | Multiprotein Complexes - metabolism | Glucose - chemical synthesis | Liver Glycogen - metabolism | TOR Serine-Threonine Kinases - genetics | Liver - drug effects | Liver Glycogen - antagonists & inhibitors | Mitochondrial Proteins - metabolism | Urea - analogs & derivatives | Diabetes Mellitus, Experimental - physiopathology | Glucose Tolerance Test | Liver - metabolism | Enzyme Inhibitors - pharmacology | Glucose - pharmacology | Glycogen Phosphorylase - metabolism | Animals | Ion Channels - metabolism | Oxygen Consumption - drug effects | Ion Channels - agonists | Mice, Obese | Multiprotein Complexes - agonists | Glycogen Phosphorylase - antagonists & inhibitors | Mice | Uncoupling Protein 2 | Urea - pharmacology | TOR protein | Mitochondrial uncoupling protein 2 | Animal models | Liver | Science | Biology | Glucose | Kinases | Proteins | Signal transduction | Mitochondria | Rodents | Hepatology | Oxidation | Inhibition | Glycogen | Diabetes mellitus | Oxygen consumption | Rapamycin | Metabolism | Phosphorylase | Glucose tolerance | Urea | Organic chemistry | Musculoskeletal system | Signaling | Sensitivity | Inhibitors | Glycogen phosphorylase | Sensitivity enhancement | Accommodation | Diabetes | Cancer
Journal Article
Protein Science, ISSN 0961-8368, 07/2005, Volume 14, Issue 7, pp. 1760 - 1771
Acyl ureas were discovered as a novel class of inhibitors for glycogen phosphorylase, a molecular target to control hyperglycemia in type 2 diabetics. This... 
rmGPa, rabbit muscle glycogen phosphorylase a | glucose, α‐D‐glucose | W1807, (−)(S)‐3‐isopropyl 4‐(2‐chlorophenyl)‐1,4‐dihydro‐1‐ethyl‐2‐methyl‐pyridine‐3,5,6‐tricarboxylate | rmGPb, rabbit muscle glycogen phosphorylase b | PLP, pyridoxal 5′‐phosphate | compound 3, 4‐{4‐[3‐(2,4‐dichloro‐benzoyl)‐ureido]‐2,3‐dimethyl‐phenoxy}‐butyric acid | inhibition | CP320626, 5‐chloro‐1H‐indole‐2‐carboxylic acid [1‐(4‐fluorobenzyl)‐ 2‐(4‐hydroxypiperidin‐1‐yl)‐2‐oxoethyl]amide | GP, glycogen phosphorylase, 1,4‐α‐D‐glucan:orthophosphate α‐glucosyltransferase (EC 2.4.1.1) | r.m.s. deviation, root‐mean‐square deviation | type 2 diabetes | acyl ureas | compound 4, 5‐{3‐[3‐ (2,4‐dichloro‐benzoyl)‐ureido]‐2‐methyl‐phenoxy}‐pentanoic acid | compound 2, 4‐{3‐chloro‐4‐[3‐(2,4‐dichloro‐benzoyl)‐ureido]‐ phenoxy}‐butyric acid | X‐ray crystallography | Glc‐1‐P, α‐D‐glucose 1‐phosphate | Glc‐6‐P, D‐glucose 6‐phosphate | hlGPa, human liver glycogen phosphorylase a | compound 1, 6‐{2,6‐dichloro‐4‐[3‐(2‐chloro‐benzoyl)‐ureido]‐phenoxy}‐hexanoic acid | glycogen phosphorylase | Type 2 diabetes | X-ray crystallography | Acyl ureas | Inhibition | Glycogen phosphorylase | TARGET | ASSAY | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUSCLE | INORGANIC-PHOSPHATE | MOLSCRIPT | MAPS | BINDING | Glycogen Phosphorylase, Liver Form - metabolism | Humans | Protein Conformation - drug effects | Crystallography, X-Ray | Glycogen Phosphorylase, Muscle Form - antagonists & inhibitors | Hypoglycemic Agents | Glycogen Phosphorylase, Liver Form - chemistry | Urea - analogs & derivatives | Urea - metabolism | Molecular Structure | Binding Sites | Rabbits | Enzyme Inhibitors - metabolism | Adenosine Monophosphate - metabolism | Enzyme Inhibitors - pharmacology | Enzyme Stability | Models, Molecular | Glycogen Phosphorylase, Muscle Form - chemistry | Animals | Muscles - enzymology | Glycogen Phosphorylase, Muscle Form - metabolism | Allosteric Site | Protein Binding | Glycogen Phosphorylase, Liver Form - antagonists & inhibitors | Kinetics | Urea - pharmacology
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/1998, Volume 95, Issue 4, pp. 1776 - 1781
Journal Article
Journal Article