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1 insight in designing effective inhibitors of methionine aminopeptidase.
2 ore the methionine residue can be cleaved by methionine aminopeptidase.
3 cDNAs coding for human beta-globin chain and methionine aminopeptidase.
8 umagillin, an angiogenic inhibitor, binds to methionine aminopeptidase 2, which is the same as eukary
11 NP-470 bind to intracellular metalloprotease methionine aminopeptidase-2 (MetAP-2) and inhibit endoth
12 mber of the fumagillin class of irreversible methionine aminopeptidase-2 (MetAP-2) inhibitors, potent
13 l molecule to enter clinical trials, targets methionine aminopeptidase-2 (MetAP-2), a metalloprotease
16 t inhibit the in vitro catalytic activity of methionine aminopeptidase-2 (MetAP2) are effective in bl
17 f the physiological metal cofactor for human methionine aminopeptidase-2 (MetAP2) has not been establ
21 for inhibitors of the human metalloprotease, methionine aminopeptidase-2 (MetAP2), identified a poten
22 ast studies, and structural studies of human methionine aminopeptidase-2 bound to TNP-470 and its ana
24 parallels between the mechanism of action of methionine aminopeptidase and other "pita-bread" enzymes
25 proteolytic cleavage events associated with methionine aminopeptidases and signal peptide peptidases
26 e commonly seen in the active-site cavity of methionine aminopeptidase, and at least one of the metal
27 +), Ni(2+), and Zn(2+), on recombinant human methionine aminopeptidase apoenzymes in releasing N-term
28 reveals a core domain that is homologous to methionine aminopeptidases, coupled to a C-terminal exte
29 ression and purification of Escherichia coli methionine aminopeptidase (eMetAP) and using slightly di
30 at have been postulated for Escherichia coli methionine aminopeptidase (eMetAP), the modes of binding
31 Herein, we have investigated members of the methionine aminopeptidase family as potential antimalari
33 noyl-L-Ala-L-Leu-L-Val-L-Phe-OMe, bound to a methionine aminopeptidase, has also been determined.
34 ength and truncated form of the type 2 human methionine aminopeptidase (hMetAP2) were analyzed by con
35 demonstrate that the Salmonella typhimurium methionine aminopeptidase is totally inactive on an N-fo
36 rmation is available for dimetalated enzyme, methionine aminopeptidase likely functions as a monometa
37 n apparently enhancing cleavage of alpha1 by methionine aminopeptidase (MAP), resulting in acetylatio
38 6-L18-S5-L30-L15-SecY-adenylate kinase (Adk)-methionine aminopeptidase (Map)-initiation factor 1 (IF1
41 In eukaryotes, two isozymes (I and II) of methionine aminopeptidase (MetAP) catalyze the removal o
47 are the structures of a Type I and a Type II methionine aminopeptidase (MetAP) from the same organism
50 ch as NAC, N-terminal-modifying enzymes like Methionine aminopeptidase (MetAP), and the signal recogn
53 g protein was found to be a metalloprotease, methionine aminopeptidase (MetAP-2), that is highly cons
55 the absence of MetAP-1, a distantly related methionine aminopeptidase, MetAP-2 function is essential
56 have their N-terminal methionine removed by methionine aminopeptidases (MetAP1 and MetAP2) prior to
58 or TNP-470 has been identified as the type 2 methionine aminopeptidase (MetAP2), how inhibition of th
63 antiproliferative activity and target human methionine aminopeptidases (MetAPs) for their cellular e
69 to be the second Co-containing member (after methionine aminopeptidase) of the binuclear N-terminal e
71 mechanism of action of the orally available methionine aminopeptidase type 2 inhibitor, [(1R)-1-carb
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