Design, Synthesis, and Evaluation of 9-d-Ribityl-1,3,7-trihydro-2,6,8-purinetrione, a Potent Inhibitor of Riboflavin Synthase and Lumazine Synthase

2001 ◽  
Vol 66 (25) ◽  
pp. 8320-8327 ◽  
Author(s):  
Mark Cushman ◽  
Donglai Yang ◽  
Klaus Kis ◽  
Adelbert Bacher
Keyword(s):  
Potent Inhibitor ◽  
Design Synthesis ◽  
Lumazine Synthase

AMP Deaminase Inhibitors. 5. Design, Synthesis, and SAR of a Highly Potent Inhibitor Series

2001 ◽  
Vol 44 (4) ◽  
pp. 613-618 ◽  
Author(s):  
Srinivas Rao Kasibhatla ◽  
Brett C. Bookser ◽  
Wei Xiao ◽  
Mark D. Erion
Keyword(s):  
Potent Inhibitor ◽  
Amp Deaminase ◽  
Design Synthesis

Design, Synthesis, and Biological Activity of a Potent Inhibitor of the Neuropeptidase N-Acetylated α-Linked Acidic Dipeptidase

1996 ◽  
Vol 39 (2) ◽  
pp. 619-622 ◽  
Author(s):  
Paul F. Jackson ◽  
Derek C. Cole ◽  
Barbara S. Slusher ◽  
Susan L. Stetz ◽  
Laurie E. Ross ◽  
...  
Keyword(s):  
Biological Activity ◽  
Potent Inhibitor ◽  
Design Synthesis

scholarly journals Pyrazolobenzothiazine-based carbothioamides as new structural leads for the inhibition of monoamine oxidases: design, synthesis, in vitro bioevaluation and molecular docking studies

MedChemComm ◽  
2017 ◽  
Vol 8 (2) ◽  
pp. 452-464 ◽  
Author(s):  
Syed Mobasher Ali Abid ◽  
Sana Aslam ◽  
Sumera Zaib ◽  
Syeda Mahwish Bakht ◽  
Matloob Ahmad ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Active Site ◽  
Potent Inhibitor ◽  
Binding Mode ◽  
Docking Studies ◽  
Design Synthesis ◽  
Molecular Docking Studies ◽  
Monoamine Oxidases ◽  
Mao B

Binding mode of potent inhibitor (green) & cognate ligand (pink) in the active site of MAO-B.

ChemInform Abstract: Design, Synthesis, and Biological Activity of a Potent Inhibitor of the Neuropeptidase N-Acetylated α-Linked Acidic Dipeptidase.

ChemInform ◽  
2010 ◽  
Vol 27 (19) ◽  
pp. no-no
Author(s):  
P. F. JACKSON ◽  
D. C. COLE ◽  
B. S. SLUSHER ◽  
S. L. STETZ ◽  
L. E. ROSS ◽  
...  
Keyword(s):  
Biological Activity ◽  
Potent Inhibitor ◽  
Design Synthesis

scholarly journals Chemoproteomic study uncovers HemK2/KMT9 as a new target for NTMT1 bisubstrate inhibitors

2021 ◽  
Author(s):  
Dongxing Chen ◽  
Ying Meng ◽  
Dan Yu ◽  
Nicholas Noinaj ◽  
Xiaodong Cheng ◽  
...  
Keyword(s):  
Rational Design ◽  
Biochemical Characterization ◽  
Potent Inhibitor ◽  
Protein Networks ◽  
Selective Inhibitors ◽  
Chemical Probe ◽  
Design Synthesis ◽  
Bisubstrate Inhibitors ◽  
Methyltransferase 1

Understanding the selectivity of methyltransferase inhibitors is important to dissect the functions of each methyltransferase target. From this perspective, here we report a chemoproteomic study to profile the selectivity of a potent protein N-terminal methyltransferase 1 (NTMT1) bisubstrate inhibitor NAH-C3-GPKK (Ki, app = 7 nM) in endogenous proteomes. First, we describe the rational design, synthesis, and biochemical characterization of a new chemical probe 6, a biotinylated analogue of NAH-C3-GPKK. Next, we systematically analyze protein networks that may selectively interact with the biotinylated probe 6 in concert with the competitor NAH-C3-GPKK. Besides NTMT1, the designated NTMT1 bisubstrate inhibitor NAH-C3-GPKK was found to also potently inhibit a methyltransferase complex HemK2-Trm112 (also known as KMT9-Trm112), highlighting the importance of systematic selectivity profiling. Furthermore, this is the first potent inhibitor for HemK2/KMT9 reported to date. Thus, our studies lay the foundation for future efforts towards the development of selective inhibitors for NTMT1 and HemK2/KMT9.

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