Structural basis for exploring the allosteric inhibition of human kidney type glutaminase

• Main Authors: Ramachandran, S, Pan, C.Q, Zimmermann, S.C, Duvall, B, Tsukamoto, T, Low, B.C, Sivaraman, J
• Other Authors: BIOLOGICAL SCIENCES
• Format: Article
• Published: 2020
• Subjects: antineoplastic agent; bis 2 (5 phenylacetamido 1,3,4 thiadiazol 2 yl)ethyl sulfide; cb 839; enzyme inhibitor; glutaminase; kidney type glutaminase; n,n' [5,5' (cyclohexane 1,3 diyl)bis(1,3,4 tiadiazole 5,2 diyl)]bis(2 phenylacetamide); unclassified drug; bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide; protein binding; sulfide; thiadiazole derivative; allosterism; Article; binding affinity; complex formation; concentration response; controlled study; crystal structure; drug mechanism; drug protein binding; drug structure; embryo; enzyme inhibition; human; human cell; IC50; structure analysis; allosteric site; antagonists and inhibitors; cell proliferation; chemistry; conformation; enzymology; HEK293 cell line; kidney; kidney tumor; protein conformation; Allosteric Site; Antineoplastic Agents; Cell Proliferation; Glutaminase; HEK293 Cells; Humans; Inhibitory Concentration 50; Kidney; Kidney Neoplasms; Molecular Conformation; Protein Binding; Protein Conformation; Sulfides; Thiadiazoles
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/174108
• Institution: National University of Singapore

10.18632/oncotarget.10791