Identification of and Structural Insights into Hit Compounds Targeting N-Myristoyltransferase for Cryptosporidium Drug Development

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Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Rudimentary Structure-Activity-Relationship study of the MMV Pathogen Box compound MMV675968 (2,4-diaminoquinazoline) unveils novel inhibitors of Trypanosoma brucei brucei DHFR enzyme
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting N- Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting N- Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Frontiers Mode of action studies confirm on-target engagement of lysyl-tRNA synthetase inhibitor and lead to new selection marker for Cryptosporidium
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
PDF) Structure-Based Design of Potent and Selective Leishmania N- Myristoyltransferase Inhibitors
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Discovery of a Novel Class of Orally Active Trypanocidal N- Myristoyltransferase Inhibitors
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting N- Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Biochemical and structural evidence for the NMT activity on lysine a
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Sequential action of the various enzymes involved in N-terminal
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Structure of the N-terminal region of ScNMT. A, molecular surface of
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting N- Myristoyltransferase for Cryptosporidium Drug Development
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
Compounds 1a-c and 2a-b bind in the Plasmodium NMT peptide binding
Identification of and Structural Insights into Hit Compounds Targeting  N-Myristoyltransferase for Cryptosporidium Drug Development
NMT catalyses Lys-MYR when the NH2 amino group is blocked a–c MS/MS
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