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

10.18632/oncotarget.10791

محفوظ في:

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Ramachandran, S, Pan, C.Q, Zimmermann, S.C, Duvall, B, Tsukamoto, T, Low, B.C, Sivaraman, J
مؤلفون آخرون:	BIOLOGY
التنسيق:	مقال
منشور في:	2020
الموضوعات:	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
الوصول للمادة أونلاين:	https://scholarbank.nus.edu.sg/handle/10635/174108
الوسوم:	إضافة وسم لا توجد وسوم, كن أول من يضع وسما على هذه التسجيلة!

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