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

10.18632/oncotarget.10791

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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
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1741082024-04-03T05:13:27Z Structural basis for exploring the allosteric inhibition of human kidney type glutaminase Ramachandran, S Pan, C.Q Zimmermann, S.C Duvall, B Tsukamoto, T Low, B.C Sivaraman, J BIOLOGICAL SCIENCES MECHANOBIOLOGY INSTITUTE BIOLOGY (NU) 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 antineoplastic agent bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide glutaminase 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 10.18632/oncotarget.10791 Oncotarget 7 36 57943-57954 2020-09-03T10:31:33Z 2020-09-03T10:31:33Z 2016 Article Ramachandran, S, Pan, C.Q, Zimmermann, S.C, Duvall, B, Tsukamoto, T, Low, B.C, Sivaraman, J (2016). Structural basis for exploring the allosteric inhibition of human kidney type glutaminase. Oncotarget 7 (36) : 57943-57954. ScholarBank@NUS Repository. https://doi.org/10.18632/oncotarget.10791 19492553 https://scholarbank.nus.edu.sg/handle/10635/174108 Unpaywall 20200831
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	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 antineoplastic agent bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide glutaminase 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
spellingShingle	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 antineoplastic agent bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide glutaminase 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 Ramachandran, S Pan, C.Q Zimmermann, S.C Duvall, B Tsukamoto, T Low, B.C Sivaraman, J Structural basis for exploring the allosteric inhibition of human kidney type glutaminase
description	10.18632/oncotarget.10791
author2	BIOLOGICAL SCIENCES
author_facet	BIOLOGICAL SCIENCES Ramachandran, S Pan, C.Q Zimmermann, S.C Duvall, B Tsukamoto, T Low, B.C Sivaraman, J
format	Article
author	Ramachandran, S Pan, C.Q Zimmermann, S.C Duvall, B Tsukamoto, T Low, B.C Sivaraman, J
author_sort	Ramachandran, S
title	Structural basis for exploring the allosteric inhibition of human kidney type glutaminase
title_short	Structural basis for exploring the allosteric inhibition of human kidney type glutaminase
title_full	Structural basis for exploring the allosteric inhibition of human kidney type glutaminase
title_fullStr	Structural basis for exploring the allosteric inhibition of human kidney type glutaminase
title_full_unstemmed	Structural basis for exploring the allosteric inhibition of human kidney type glutaminase
title_sort	structural basis for exploring the allosteric inhibition of human kidney type glutaminase
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/174108
_version_	1795301045875769344

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

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