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Structural Basis for Selective Inhibition of Trypanosomatid Glyceraldehyde-3-Phosphate Dehydrogenase: Molecular Docking and 3D QSAR Studies

https://doi.org/10.1021/ci700453j
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inferredcites →https://doi.org/10.1002/(sici)1099-128x(199703)11:2<157::aid-cem471>3.0.co;2-jopenalex-snapshot
Bootstrapping principal component regression models
inferredcites →https://doi.org/10.1002/9780470125885.ch3openalex-snapshot
Theoretical and Practical Aspects of Three‐Dimensional Quantitative Structure‐Activity Relationships
inferredcites →https://doi.org/10.1002/jcc.540100804openalex-snapshot
Validation of the general purpose tripos 5.2 force field
inferredcites →https://doi.org/10.1002/prot.10465openalex-snapshot
Improved protein–ligand docking using GOLD
inferredcites →https://doi.org/10.1002/qsar.19880070105openalex-snapshot
Crossvalidation, Bootstrapping, and Partial Least Squares Compared with Multiple Regression in Conventional QSAR Studies
inferredcites →https://doi.org/10.1006/jmbi.1996.0477openalex-snapshot
A Fast Flexible Docking Method using an Incremental Construction Algorithm
inferredcites →https://doi.org/10.1006/jmbi.1996.0897openalex-snapshot
Development and validation of a genetic algorithm for flexible docking 1 1Edited by F. E. Cohen
inferredcites →https://doi.org/10.1006/jmbi.2001.4588openalex-snapshot
Conformational changes in Leishmania mexicana glyceraldehyde-3-phosphate dehydrogenase induced by designed inhibitors
inferredcites →https://doi.org/10.1007/bf00124364openalex-snapshot
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inferredcites →https://doi.org/10.1007/bf01593790openalex-snapshot
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inferredcites →https://doi.org/10.1007/s00894-006-0131-1openalex-snapshot
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inferredcites →https://doi.org/10.1016/0040-4020(80)80168-2openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.bmc.2004.01.028openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.bmc.2005.08.055openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.bmc.2007.06.021openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.bmcl.2005.04.017openalex-snapshot
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inferredcites →https://doi.org/10.1016/s0169-4758(00)01810-xopenalex-snapshot
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inferredcites →https://doi.org/10.1021/bi00046a004openalex-snapshot
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inferredcites →https://doi.org/10.1021/ci060089dopenalex-snapshot
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inferredcites →https://doi.org/10.1021/ja00226a005openalex-snapshot
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inferredcites →https://doi.org/10.1021/jm00047a017openalex-snapshot
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inferredcites →https://doi.org/10.1021/jm001044lopenalex-snapshot
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inferredcites →https://doi.org/10.1021/jm0203783openalex-snapshot
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inferredcites →https://doi.org/10.1021/jm050362nopenalex-snapshot
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inferredcites →https://doi.org/10.1021/jm9802620openalex-snapshot
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inferredcites →https://doi.org/10.1054/drup.2000.0177openalex-snapshot
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inferredcites →https://doi.org/10.1073/pnas.030539197openalex-snapshot
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inferredcites →https://doi.org/10.1073/pnas.90.6.2355openalex-snapshot
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inferredcites →https://doi.org/10.1073/pnas.96.8.4273openalex-snapshot
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inferredcites →https://doi.org/10.1074/jbc.274.21.14551openalex-snapshot
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inferredcites →https://doi.org/10.1107/s0907444905042289openalex-snapshot
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inferredcites →https://doi.org/10.1111/j.1365-3156.2006.01715.xopenalex-snapshot
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inferredcites →https://doi.org/10.1146/annurev.pathol.1.110304.100151openalex-snapshot
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Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4763250openalex-extracted
Comprehensive Investigation of The Dihydrogenphosphate Hybrid: Hirshfeld Surface Analysis, Dft Evaluation, Electron Localization Function, Non-Covalent Interaction, and Docking Molecular Study on Anticancer
inferred← citeshttps://doi.org/10.1002/0471266949.bmc141openalex-snapshot
Recent Trends in Structure‐Based Drug Design and Energetics
inferred← citeshttps://doi.org/10.1002/9783527670383.ch4openalex-snapshot
Drug Design and Screening by In Silico Approaches
inferred← citeshttps://doi.org/10.1002/chin.200829217openalex-snapshot
ChemInform Abstract: Structural Basis for Selective Inhibition of Trypanosomatid Glyceraldehyde‐3‐Phosphate Dehydrogenase: Molecular Docking and 3D QSAR Studies.
inferred← citeshttps://doi.org/10.1002/qsar.200860109openalex-snapshot
Fragment‐Based QSAR and Molecular Modeling Studies on a Series of Discodermolide Analogs as Microtubule‐Stabilizing Anticancer Agents
inferred← citeshttps://doi.org/10.1002/wcms.69openalex-snapshot
Two personal perspectives on a key issue in contemporary 3D QSAR
inferred← citeshttps://doi.org/10.1007/s11030-008-9074-zopenalex-snapshot
Fragment-based and classical quantitative structure–activity relationships for a series of hydrazides as antituberculosis agents
inferred← citeshttps://doi.org/10.1007/s11030-009-9112-5openalex-snapshot
Fragment-based QSAR: perspectives in drug design
inferred← citeshttps://doi.org/10.1016/j.bmc.2008.10.052openalex-snapshot
Convergent synthesis and cruzain inhibitory activity of novel 2-(N′-benzylidenehydrazino)-4-trifluoromethyl-pyrimidines
inferred← citeshttps://doi.org/10.1016/j.bmc.2010.01.022openalex-snapshot
Structural basis for selective inhibition of purine nucleoside phosphorylase from Schistosoma mansoni: Kinetic and structural studies
inferred← citeshttps://doi.org/10.1016/j.ejmech.2009.12.059openalex-snapshot
Pharmacophore-based 3D QSAR studies on a series of high affinity 5-HT1A receptor ligands
inferred← citeshttps://doi.org/10.1016/j.jmgm.2009.03.001openalex-snapshot
Quantitative structure–activity relationships for a series of inhibitors of cruzain from Trypanosoma cruzi: Molecular modeling, CoMFA and CoMSIA studies
inferred← citeshttps://doi.org/10.1016/j.jmgm.2014.02.006openalex-snapshot
In silico investigation of medicinal spectrum of imidazo-azines from the perspective of multitarget screening against malaria, tuberculosis and Chagas disease
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2009.09.001openalex-snapshot
Genetic validation of aldolase and glyceraldehyde-3-phosphate dehydrogenase as drug targets in Trypanosoma brucei
inferred← citeshttps://doi.org/10.1016/j.toxicon.2025.108965openalex-snapshot
TcGAPDH peptidic inhibitors derived from dinoponeratoxin M-PONTX-Dq4e with trypanocidal effect
inferred← citeshttps://doi.org/10.1021/ci100128kopenalex-snapshot
Discovery of New Inhibitors of Schistosoma mansoni PNP by Pharmacophore-Based Virtual Screening
inferred← citeshttps://doi.org/10.1021/ci8002182openalex-snapshot
Structure-Based Approach for the Study of Estrogen Receptor Binding Affinity and Subtype Selectivity
inferred← citeshttps://doi.org/10.1021/ci900316eopenalex-snapshot
Role of Halogen Bonds in Thyroid Hormone Receptor Selectivity: Pharmacophore-Based 3D-QSSR Studies
inferred← citeshttps://doi.org/10.1039/c4ay01081gopenalex-snapshot
CoMFA and CoMSIA studies on a series of fluroquinolone derivatives for potential anti-inflammatory activity
inferred← citeshttps://doi.org/10.1111/cbdd.12941openalex-snapshot
Molecular basis for covalent inhibition of glyceraldehyde‐3‐phosphate dehydrogenase by a 2‐phenoxy‐1,4‐naphthoquinone small molecule
inferred← citeshttps://doi.org/10.1111/j.1476-5381.2009.00524.xopenalex-snapshot
Novel ruthenium complexes as potential drugs for Chagas's disease: enzyme inhibition and in vitro/in vivo trypanocidal activity
inferred← citeshttps://doi.org/10.1111/j.1476-5381.2010.00662.xopenalex-snapshot
New drugs for neglected infectious diseases: Chagas' disease
inferred← citeshttps://doi.org/10.11606/t.75.2015.tde-28082015-081328openalex-snapshot
Determinação do modo de interação de inibidores reversíveis da cruzaína de Trypanosoma cruzi via cristalografia de raios X
inferred← citeshttps://doi.org/10.11606/t.76.2008.tde-09062008-110714openalex-snapshot
Planejamento de inibidores da enzima gliceraldeído-3-fosfato desidrogenase de Trypanosoma cruzi: biologia estrutural e química medicinal
inferred← citeshttps://doi.org/10.1351/pac-con-11-11-07openalex-snapshot
Structure- and ligand-based drug design approaches for neglected tropical diseases
inferred← citeshttps://doi.org/10.1517/17460441.2011.563297openalex-snapshot
In silicoscreening strategies for novel inhibitors of parasitic diseases
inferred← citeshttps://doi.org/10.1590/s0103-40142010000300006openalex-snapshot
Planejamento de fármacos, biotecnologia e química medicinal: aplicações em doenças infecciosas
inferred← citeshttps://doi.org/10.2174/09298673113209990139openalex-snapshot
Glycosomal Targets for Anti-Trypanosomatid Drug Discovery
inferred← citeshttps://doi.org/10.2174/0929867324666170830103003openalex-snapshot
New Molecular Targets and Strategies for Antimalarial Discovery
inferred← citeshttps://doi.org/10.2174/1381612826666201113104633openalex-snapshot
Metallodrugs for the Treatment of Trypanosomatid Diseases: Recent Advances and New Insights
inferred← citeshttps://doi.org/10.2174/156802609789207127openalex-snapshot
Structure-Based Drug Design Strategies in Medicinal Chemistry
inferred← citeshttps://doi.org/10.2174/157340609787049299openalex-snapshot
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inferred← citeshttps://doi.org/10.2174/1573406411309030010openalex-snapshot
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inferred← citeshttps://doi.org/10.2174/1573406415666190712111139openalex-snapshot
Design of Inhibitors for Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) Enzyme ofLeishmania mexicana
inferred← citeshttps://doi.org/10.3390/ijms15023186openalex-snapshot
Pattern Recognition Techniques Applied to the Study of Leishmanial Glyceraldehyde-3-Phosphate Dehydrogenase Inhibition
inferred← citeshttps://doi.org/10.3390/molecules18055032openalex-snapshot
Identification of Electronic and Structural Descriptors of Adenosine Analogues Related to Inhibition of Leishmanial Glyceraldehyde-3-Phosphate Dehydrogenase
inferred← citeshttps://doi.org/10.3390/molecules18077761openalex-snapshot
In-silico Leishmania Target Selectivity of Antiparasitic Terpenoids
inferred← citeshttps://doi.org/10.4018/978-1-5225-1762-7.ch037openalex-snapshot
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inferred← citeshttps://doi.org/10.4018/ijqspr.2017010104openalex-snapshot
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inferred← citeshttps://doi.org/10.4155/fmc.11.60openalex-snapshot
Drug Discovery and the Use of Computational Approaches for Infectious Diseases
inferred← citeshttps://doi.org/10.4155/fmc.13.114openalex-snapshot
Interactions of Antiparasitic Alkaloids withLeishmaniaProtein Targets: A Molecular Docking Analysis
inferred← citeshttps://doi.org/10.4155/fmc.13.166openalex-snapshot
A Pharmacophore-Based Virtual Screening Approach for the Discovery of Trypanosoma Cruzi Gapdh Inhibitors
inferred← citeshttps://doi.org/10.4155/fmc.13.213openalex-snapshot
Corrigendum
inferred← citeshttps://doi.org/10.4172/2161-0401.1000107openalex-snapshot
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inferred← citeshttps://doi.org/10.4236/ijoc.2012.223040openalex-snapshot
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