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1  interaction with the structural core of the methionine aminopeptidase.
2 insight in designing effective inhibitors of methionine aminopeptidase.
3 ore the methionine residue can be cleaved by methionine aminopeptidase.
4 cDNAs coding for human beta-globin chain and methionine aminopeptidase.
5               We identify Zn metalloprotease methionine aminopeptidase 1 (METAP1) as a COG0523 client
6                    The Plasmodium falciparum methionine aminopeptidase 1b (PfMetAP1b), one of four Me
7                      For over three decades, methionine aminopeptidase 2 (MetAP2) has been a tentativ
8           In the present study we found that methionine aminopeptidase 2 (MetAP2), a critical compone
9 ic initiation factor-2alpha binding protein, methionine aminopeptidase 2 (MetAP2).
10 diated by inhibition of the molecular target methionine aminopeptidase 2 (MetAp2).
11 umagillin, an angiogenic inhibitor, binds to methionine aminopeptidase 2, which is the same as eukary
12 anti-angiogenic activity by binding to human methionine aminopeptidase 2.
13 iangiogenic activity due to binding to human methionine aminopeptidase 2.
14 NP-470 bind to intracellular metalloprotease methionine aminopeptidase-2 (MetAP-2) and inhibit endoth
15 mber of the fumagillin class of irreversible methionine aminopeptidase-2 (MetAP-2) inhibitors, potent
16 l molecule to enter clinical trials, targets methionine aminopeptidase-2 (MetAP-2), a metalloprotease
17                       To this end, we tested methionine aminopeptidase-2 (MetAP-2), which covalently
18        The molecular target of fumagillin is methionine aminopeptidase-2 (MetAP-2).
19 t inhibit the in vitro catalytic activity of methionine aminopeptidase-2 (MetAP2) are effective in bl
20 f the physiological metal cofactor for human methionine aminopeptidase-2 (MetAP2) has not been establ
21                                              Methionine aminopeptidase-2 (MetAP2) is a novel target f
22                                              Methionine aminopeptidase-2 (MetAP2) processes N-termina
23                                Inhibition of methionine aminopeptidase-2 (MetAP2) represents a novel
24 for inhibitors of the human metalloprotease, methionine aminopeptidase-2 (MetAP2), identified a poten
25 ast studies, and structural studies of human methionine aminopeptidase-2 bound to TNP-470 and its ana
26  Xaa-Pro aminopeptidase activity and limited methionine aminopeptidase activity.
27 parallels between the mechanism of action of methionine aminopeptidase and other "pita-bread" enzymes
28  proteolytic cleavage events associated with methionine aminopeptidases and signal peptide peptidases
29 e commonly seen in the active-site cavity of methionine aminopeptidase, and at least one of the metal
30 +), Ni(2+), and Zn(2+), on recombinant human methionine aminopeptidase apoenzymes in releasing N-term
31 KFF- EcH3, derived from the Escherichia coli methionine aminopeptidase can disrupt secondary and tert
32  reveals a core domain that is homologous to methionine aminopeptidases, coupled to a C-terminal exte
33 ression and purification of Escherichia coli methionine aminopeptidase (eMetAP) and using slightly di
34 at have been postulated for Escherichia coli methionine aminopeptidase (eMetAP), the modes of binding
35  Herein, we have investigated members of the methionine aminopeptidase family as potential antimalari
36                   We applied this concept to methionine aminopeptidase from Mycobacterium tuberculosi
37 noyl-L-Ala-L-Leu-L-Val-L-Phe-OMe, bound to a methionine aminopeptidase, has also been determined.
38 ength and truncated form of the type 2 human methionine aminopeptidase (hMetAP2) were analyzed by con
39  disease to define the expression pattern of methionine aminopeptidase II (MetAP2), a cytosolic metal
40 ived structure-disrupting peptides targeting methionine aminopeptidase in pathogenic bacteria: a new
41 ting the wide-ranging importance of the host methionine aminopeptidase in phage replication.
42  demonstrate that the Salmonella typhimurium methionine aminopeptidase is totally inactive on an N-fo
43 rmation is available for dimetalated enzyme, methionine aminopeptidase likely functions as a monometa
44 n apparently enhancing cleavage of alpha1 by methionine aminopeptidase (MAP), resulting in acetylatio
45 6-L18-S5-L30-L15-SecY-adenylate kinase (Adk)-methionine aminopeptidase (Map)-initiation factor 1 (IF1
46 ntial enzymes, peptide deformylase (PDF) and methionine aminopeptidase (MAP).
47 zymes that catalyze this reaction are called Methionine Aminopeptidases (MAPs).
48 on and acetylation, mediated sequentially by methionine aminopeptidase (MetAP) and N-acetyltransferas
49 e 60S subunit enhances fidelity by anchoring methionine aminopeptidase (MetAP) at the nascent protein
50                                              Methionine aminopeptidase (MetAP) carries out an importa
51    In eukaryotes, two isozymes (I and II) of methionine aminopeptidase (MetAP) catalyze the removal o
52                                              Methionine aminopeptidase (MetAP) catalyzes the co-trans
53                                              Methionine aminopeptidase (MetAP) catalyzes the hydrolyt
54                                              Methionine aminopeptidase (MetAP) exists in two forms (t
55                                          The methionine aminopeptidase (MetAP) family is responsible
56                 The crystal structure of the methionine aminopeptidase (MetAP) from Mycobacterium tub
57 are the structures of a Type I and a Type II methionine aminopeptidase (MetAP) from the same organism
58                                              Methionine aminopeptidase (MetAP) is a promising target
59 rIIA6, to show that a host gene coding for a methionine aminopeptidase (metAP) is necessary for phage
60                                              Methionine aminopeptidase (MetAP) removes the amino-term
61 ch as NAC, N-terminal-modifying enzymes like Methionine aminopeptidase (MetAP), and the signal recogn
62                                              Methionine aminopeptidase (MetAP)-2 has been suggested a
63 terminal methionine from nascent proteins by methionine aminopeptidase (MetAP).
64 g protein was found to be a metalloprotease, methionine aminopeptidase (MetAP-2), that is highly cons
65                                              Methionine aminopeptidases (MetAP) are responsible for t
66  the absence of MetAP-1, a distantly related methionine aminopeptidase, MetAP-2 function is essential
67  have their N-terminal methionine removed by methionine aminopeptidases (MetAP1 and MetAP2) prior to
68                   Fumagalone inhibits type 2 methionine aminopeptidase (MetAP2) with IC(50) = 8 micro
69 or TNP-470 has been identified as the type 2 methionine aminopeptidase (MetAP2), how inhibition of th
70 gh the irreversible inhibition of the type 2 methionine aminopeptidase (MetAP2).
71 alicin recently was identified as the type 2 methionine aminopeptidase (MetAP2).
72                                              Methionine aminopeptidases (MetAPs) are essential enzyme
73                                              Methionine aminopeptidases (MetAPs) are ubiquitous metal
74  antiproliferative activity and target human methionine aminopeptidases (MetAPs) for their cellular e
75                           Arx1 is related to methionine aminopeptidases (MetAPs), and Rei1 is a C2H2
76                                              Methionine aminopeptidases (MetAPs), which remove the in
77 at remove N-terminal methionine are known as methionine aminopeptidases (MetAPs).
78 ctrophotometric assay has been developed for methionine aminopeptidases (MetAPs).
79 rophotometric assays have been developed for methionine aminopeptidases (MetAPs).
80  the excision of the initiator methionine by methionine aminopeptidases (METAPs).
81 wing excision of the initiator methionine by methionine aminopeptidases (MetAPs).
82 to be the second Co-containing member (after methionine aminopeptidase) of the binuclear N-terminal e
83 o-EM map to the presence of another protein (methionine aminopeptidase, or MetAP), rather than to the
84                          Inhibitors of human methionine aminopeptidase type 2 (hMetAP2) are of intere
85  mechanism of action of the orally available methionine aminopeptidase type 2 inhibitor, [(1R)-1-carb
86              PPI-2458, a potent irreversible methionine aminopeptidase type 2 inhibitor, was administ
87  of PPI-2458 was linked to the inhibition of methionine aminopeptidase type 2.