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Calorimetric Studies of Ligands Binding to Glutathione S -Transferase from the Malarial Parasite Plasmodium falciparum

https://doi.org/10.1021/bi400007g
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb07729.xopenalex-snapshot
The three‐dimensional structure of class pi glutathione S‐transferase in complex with glutathione sulfonate at 2.3 A resolution.
inferredcites →https://doi.org/10.1002/jmr.1040openalex-snapshot
Diuretic drug binding to human glutathione transferase P1‐1: potential role of Cys‐101 revealed in the double mutant C47S/Y108V
inferredcites →https://doi.org/10.1002/pro.253openalex-snapshot
Influence of the H‐site residue 108 on human glutathione transferase P1‐1 ligand binding: Structure‐thermodynamic relationships and thermal stability
inferredcites →https://doi.org/10.1006/abio.1999.4402openalex-snapshot
Exact Analysis of Competition Ligand Binding by Displacement Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1006/abio.2001.5218openalex-snapshot
Enzyme Kinetics Determined Using Calorimetry: A General Assay for Enzyme Activity?
inferredcites →https://doi.org/10.1006/expr.1995.1099openalex-snapshot
Plasmodium berghei: Implication of Intracellular Glutathione and Its Related Enzyme in Chloroquine Resistance in Vivo
inferredcites →https://doi.org/10.1006/jmbi.1994.1232openalex-snapshot
Molecular Structure at 1·8 Å of Mouse Liver Class Pi Glutathione S-transferase Complexed with S-(p-Nitrobenzyl)glutathione and Other Inhibitors
inferredcites →https://doi.org/10.1006/jmbi.1994.1631openalex-snapshot
Refined Crystal Structure of Porcine Class Pi Glutathione S-Transferase (pGST P1-1) at 2·1 Å Resolution
inferredcites →https://doi.org/10.1006/jmbi.1997.1364openalex-snapshot
The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution
inferredcites →https://doi.org/10.1006/jmbi.1998.1927openalex-snapshot
Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106
inferredcites →https://doi.org/10.1006/jmbi.2000.3904openalex-snapshot
Tyr115, Gln165 and Trp209 contribute to the 1,2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-111Edited by R. Huber
inferredcites →https://doi.org/10.1016/0003-2697(89)90213-3openalex-snapshot
Rapid measurement of binding constants and heats of binding using a new titration calorimeter
inferredcites →https://doi.org/10.1016/0003-2697(89)90602-7openalex-snapshot
Calculation of protein extinction coefficients from amino acid sequence data
inferredcites →https://doi.org/10.1016/j.abb.2009.05.011openalex-snapshot
Structural, functional and unfolding characteristics of glutathione S-transferase of Plasmodium vivax
inferredcites →https://doi.org/10.1016/j.actatropica.2007.08.005openalex-snapshot
Glutathione transferases from parasites: A biochemical view
inferredcites →https://doi.org/10.1016/j.biochi.2009.10.008openalex-snapshot
Kinetic properties and specificity of trimeric Plasmodium falciparum and human dUTPases
inferredcites →https://doi.org/10.1016/j.biochi.2011.09.003openalex-snapshot
Binding properties of ferrocene–glutathione conjugates as inhibitors and sensors for glutathione S-transferases
inferredcites →https://doi.org/10.1016/j.bpc.2004.12.015openalex-snapshot
ITC in the post-genomic era…? Priceless
inferredcites →https://doi.org/10.1016/j.bpc.2011.04.005openalex-snapshot
Energetics of ligand binding to human glutathione transferase A1-1: Tyr-9 associated localisation of the C-terminal helix is ligand-dependent
inferredcites →https://doi.org/10.1016/j.exppara.2007.02.005openalex-snapshot
Plasmodium vivax: Molecular cloning, expression and characterization of glutathione S-transferase
inferredcites →https://doi.org/10.1016/j.ijpara.2003.09.011openalex-snapshot
Oxidative stress in malaria parasite-infected erythrocytes: host–parasite interactions
inferredcites →https://doi.org/10.1016/j.tca.2006.06.019openalex-snapshot
Applications of isothermal titration calorimetry to measure enzyme kinetics and activity in complex solutions
inferredcites →https://doi.org/10.1016/s0022-2836(03)00347-4openalex-snapshot
Glutathione Reductase of the Malarial Parasite Plasmodium falciparum: Crystal Structure and Inhibitor Development
inferredcites →https://doi.org/10.1016/s0076-6879(05)01015-3openalex-snapshot
Glutathione S‐transferase from Malarial Parasites: Structural and Functional Aspects
inferredcites →https://doi.org/10.1016/s0166-6851(02)00160-3openalex-snapshot
The glutathione S-transferase from Plasmodium falciparum
inferredcites →https://doi.org/10.1038/415670aopenalex-snapshot
Malaria in 2002
inferredcites →https://doi.org/10.1038/nprot.2006.28openalex-snapshot
Isothermal titration calorimetry to determine association constants for high-affinity ligands
inferredcites →https://doi.org/10.1042/bj2740409openalex-snapshot
Theta, a new class of glutathione transferases purified from rat and man
inferredcites →https://doi.org/10.1046/j.1365-3156.1999.00387.xopenalex-snapshot
Glutathione‐S‐transferase activity in malarial parasites
inferredcites →https://doi.org/10.1046/j.1432-1327.2001.02349.xopenalex-snapshot
Thermodynamic analysis of the binding of glutathione to glutathione S‐transferase over a range of temperatures
inferredcites →https://doi.org/10.1073/pnas.2333763100openalex-snapshot
X-ray structure of glutathione S -transferase from the malarial parasite Plasmodium falciparum
inferredcites →https://doi.org/10.1073/pnas.74.6.2236openalex-snapshot
Heat capacity and entropy changes in processes involving proteins.
inferredcites →https://doi.org/10.1074/jbc.m001706200openalex-snapshot
Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases
inferredcites →https://doi.org/10.1074/jbc.m109.015198openalex-snapshot
Tetramerization and Cooperativity in Plasmodium falciparum Glutathione S-Transferase Are Mediated by Atypic Loop 113–119
inferredcites →https://doi.org/10.1074/jbc.m305043200openalex-snapshot
Thermodynamic Description of the Effect of the Mutation Y49F on Human Glutathione Transferase P1-1 in Binding with Glutathione and the Inhibitor S-Hexylglutathione
inferredcites →https://doi.org/10.1074/jbc.m309663200openalex-snapshot
Native and Inhibited Structure of a Mu class-related Glutathione S-transferase from Plasmodium falciparum
inferredcites →https://doi.org/10.1074/jbc.m503889200openalex-snapshot
Cooperativity and Pseudo-cooperativity in the Glutathione S-Transferase from Plasmodium falciparum
inferredcites →https://doi.org/10.1093/toxsci/49.2.156openalex-snapshot
Concise review of the glutathione S-transferases and their significance to toxicology
inferredcites →https://doi.org/10.1110/ps.051891106openalex-snapshot
Plasmodium falciparum glutathione S‐transferase—Structural and mechanistic studies on ligand binding and enzyme inhibition
inferredcites →https://doi.org/10.1110/ps.052055206openalex-snapshot
Calorimetric and structural studies of the nitric oxide carrier S‐nitrosoglutathione bound to human glutathione transferase P1‐1
inferredcites →https://doi.org/10.1146/annurev.pharmtox.45.120403.095857openalex-snapshot
GLUTATHIONE TRANSFERASES
inferredcites →https://doi.org/10.1186/1472-6807-7-60openalex-snapshot
Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases
inferredcites →https://doi.org/10.1515/bc.2002.086openalex-snapshot
Glutathione S-Transferase of the Malarial Parasite Plasmodium falciparum: Characterization of a Potential Drug Target
inferredcites →https://doi.org/10.2174/0929867306666220208213032openalex-snapshot
Glutathione S-Transferases - A Review
inferredcites →https://doi.org/10.3109/10409239509083491openalex-snapshot
The Glut athione S-Transferase Supergene Family: Regulation of GST and the Contribution of the lsoenzymes to Cancer Chemoprotection and Drug Resistance Part I
inferredcites →https://doi.org/10.5772/1434openalex-snapshot
Thermodynamics - Physical Chemistry of Aqueous Systems

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4769330openalex-extracted
Characterizing the Ligandin Properties of Plasmodium Falciparum and Vivax Glutathione Transferase Towards Selected Antimalarial Drugs
inferred← citeshttps://doi.org/10.1016/j.bbapap.2014.04.017openalex-snapshot
Asn112 in Plasmodium falciparum glutathione S-transferase is essential for induced reversible tetramerization by phosphate or pyrophosphate
inferred← citeshttps://doi.org/10.1016/j.biochi.2017.01.005openalex-snapshot
Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics
inferred← citeshttps://doi.org/10.1016/j.pestbp.2021.104873openalex-snapshot
Delta class glutathione S-transferase (TuGSTd01) from the two-spotted spider mite Tetranychus urticae is inhibited by abamectin
inferred← citeshttps://doi.org/10.1080/07391102.2024.2329291openalex-snapshot
Describing the ligandin properties of Plasmodium falciparum and vivax glutathione transferase towards bromosulfophthalein from empirical and computational modelling viewpoints
inferred← citeshttps://doi.org/10.3390/ph19081287openalex-snapshot
Revisiting Glutathione Transferases of Plasmodium as Potential Targets for Coadjuvant Therapies and the Development of New Antimalarials
inferred← citeshttps://doi.org/10.3390/toxins13090664openalex-snapshot
A Novel Glutathione S-Transferase Gtt2 Class (VpGSTT2) Is Found in the Genome of the AHPND/EMS Vibrio parahaemolyticus Shrimp Pathogen
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