19 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
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Article Title
Organization
Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase.
Imperial College
Discovery of pyridyl-based inhibitors of Plasmodium falciparum N-myristoyltransferase.
Imperial College
Lead optimization of a pyrazole sulfonamide series of Trypanosoma brucei N-myristoyltransferase inhibitors: identification and evaluation of CNS penetrant compounds as potential treatments for stage 2 human African trypanosomiasis.
University of Dundee
Structure-based design of potent and selective Leishmania N-myristoyltransferase inhibitors.
Imperial College
Discovery of novel and ligand-efficient inhibitors of Plasmodium falciparum and Plasmodium vivax N-myristoyltransferase.
Imperial College
Design and synthesis of inhibitors of Plasmodium falciparum N-myristoyltransferase, a promising target for antimalarial drug discovery.
Imperial College
Discovery of Plasmodium vivax N-myristoyltransferase inhibitors: screening, synthesis, and structural characterization of their binding mode.
Imperial College
Discovery of a novel class of orally active trypanocidal N-myristoyltransferase inhibitors.
University of Dundee
Derivatives of aryl amines containing the cytotoxic 1,4-dioxo-2-butenyl pharmacophore.
Acadia University
A chiral recognition element with an unusual size constraint affects the potency and selectivity for peptidomimetic inhibitors of Candida albicans myristoyl-CoA:protein N-myristoyltransferase
TBA
How To Design Selective Ligands for Highly Conserved Binding Sites: A Case Study Using
Johannes Gutenberg-Universit£T Mainz
A Molecular Hybridization Approach for the Design of Potent, Highly Selective, and Brain-Penetrant N-Myristoyltransferase Inhibitors.
University of Dundee
Design and Synthesis of Brain Penetrant Trypanocidal N-Myristoyltransferase Inhibitors.
University of Dundee
PYRIMIDINE COMPOUND AS WEE-1 INHIBITOR
Wigen Biomedicine Technology (Shanghai) Co.
Peptidomimetic 2-cyanopyrrolidines as potent selective cathepsin L inhibitors.
The M. S. University of Baroda