BindingDB Entry 2672: Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors.

Name: BindingDB Entry 2672: Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors.
Creator: BindingDB
Keywords: 3. Good health, Bcl-xL/BAK, Lactate Dehydrogenase, Malate Dehydrogenase (pfMDH), Malate Dehydrogenase, mitochondrial, and Malate dehydrogenase cytoplasmic, University of Mississippi, Affinity

Research datakeyboard_double_arrow_right Dataset 01 Jan 2008 English Publisher:BindingDB

Authors: BindingDB;

doi: 10.7270/q2hh6hcv

BindingDB Entry 2672: Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors.

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Abstract

Small molecule binding data for protein Bcl-xL/BAK, Lactate Dehydrogenase, Malate Dehydrogenase (pfMDH), Malate Dehydrogenase, mitochondrial, and Malate dehydrogenase cytoplasmic, Uniprot P00346, P11708, Q07817, Q27743, and Q5E9B1

Keywords

Bcl-xL/BAK, Lactate Dehydrogenase, Malate Dehydrogenase (pfMDH), Malate Dehydrogenase, mitochondrial, and Malate dehydrogenase cytoplasmic, University of Mississippi, Affinity

8 Research products, page 1 of 1

Functional characterization of an alternative [lactate dehydrogenase-like] malate dehydrogenase in Plasmodium falciparum
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Structure and function of Plasmodium falciparum malate dehydrogenase: Role of critical amino acids in co-substrate binding pocket
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Analysis of quaternary structure of a [LDH-like] malate dehydrogenase of Plasmodium falciparum with oligomeric mutants
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Oligomeric interfaces as a tool in drug discovery: Specific interference with activity of malate dehydrogenase of Plasmodium falciparum in vitro
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Crystallization and preliminary X-ray diffraction of malate dehydrogenase fromPlasmodium falciparum
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Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase: evidence for a very divergent long-chain dehydrogenase family
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Design, Synthesis, and Biological Evaluation of Plasmodium falciparum Lactate Dehydrogenase Inhibitors
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BindingDB Entry 2672: Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors.

BindingDB Entry 2672: Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors.

8 Research products, page 1 of 1

Functional characterization of an alternative [lactate dehydrogenase-like] malate dehydrogenase in Plasmodium falciparum

Structure and function of Plasmodium falciparum malate dehydrogenase: Role of critical amino acids in co-substrate binding pocket

Analysis of quaternary structure of a [LDH-like] malate dehydrogenase of Plasmodium falciparum with oligomeric mutants

Oligomeric interfaces as a tool in drug discovery: Specific interference with activity of malate dehydrogenase of Plasmodium falciparum in vitro

Crystallization and preliminary X-ray diffraction of malate dehydrogenase fromPlasmodium falciparum

Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase: evidence for a very divergent long-chain dehydrogenase family

Design, Synthesis, and Biological Evaluation of Plasmodium falciparum Lactate Dehydrogenase Inhibitors

Design, Synthesis, and Biological Evaluation of Plasmodium falciparum Lactate Dehydrogenase Inhibitors