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1 the zinc containing Escherichia coli peptide deformylase.
2 metal chelators strongly inhibit the E. coli deformylase.
3  a modest success with inhibitors of peptide deformylase.
4  essential prokaryotic gene encoding peptide deformylase.
5 te N-formyl-methionine processing by peptide deformylase.
6 ometric assay has been developed for peptide deformylase.
7 oup confirming the physiological role of the deformylase.
8  examine the sequence specificity of peptide deformylase.
9 he nascent polypeptide is removed by peptide deformylase.
10 be reconstituted in vitro from the denatured deformylase.
11 sitive method for kinetic studies of peptide deformylase.
12 nt, time-dependent inhibitors of the peptide deformylase.
13 g the processed forms of Arabidopsis peptide deformylase 1 and 2 (pAtDEF1 and 2, respectively) were e
14 fective in vitro against Arabidopsis peptide deformylase 1 and 2 activity, respectively.
15 ormyl group, we postulate the existence of a deformylase, acting later in the pathway.
16                                      Peptide deformylase activity was thought to be limited to riboso
17 Arabidopsis peptide deformylases had peptide deformylase activity with unique kinetic parameters that
18 e culture medium, thereby inhibiting peptide deformylase activity.
19 l formyl group is usually removed by peptide deformylase, an enzymatic activity requiring iron.
20 t of direct changes in interactions with the deformylase and Met aminopeptidase cannot be excluded.
21 nts that are inhibitors of bacterial peptide deformylase and UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylg
22 cription regulators, an apparent polypeptide deformylase, and a protein related to a virulence-associ
23 n the active site of all eubacterial peptide deformylases, and N-terminal extensions identifiable as
24   Similar results were obtained with peptide deformylase, another essential enzyme of the mononuclear
25                                              Deformylases are metalloproteases in bacteria, plants, a
26 here has been increasing interest in peptide deformylase as a potential target for antibacterial chem
27           Enzymatic exclusion of O2 from the deformylase assays renders the deformylase highly stable
28 ding sequence (def gene) of Escherichia coli deformylase behind a bacteriophage T7 promoter, we have,
29 of coordinated cysteine suggest that E. coli deformylase belongs to a new subfamily of metalloproteas
30 the zinc containing Escherichia coli peptide deformylase bound to the transition-state analogue, (S)-
31                  In addition, active peptide deformylase can be reconstituted in vitro from the denat
32                                      Peptide deformylase catalyzes the removal of the N-formyl group
33                                      Peptide deformylase catalyzes the removal of the N-terminal form
34 ecies, we suggest that antibiotics targeting deformylase could have wide applicability.
35      Coexpression of the E. coli polypeptide deformylase (DEF), which removes the formyl group from t
36 eing a broad-specificity enzyme, the peptide deformylase deformylates different peptides at drastical
37                                      Peptide deformylase (EC 3.5.1.31) catalyzes the removal of a for
38 n has allowed the purification of > 50 mg of deformylase enzyme from each liter of cell culture.
39 fied iron-enriched form of S. aureus peptide deformylase enzyme retained high activity over many mont
40 ned to possess varying potencies against the deformylase enzyme revealed a linear correlation between
41                                          The deformylase exhibits strong preference for an L-methioni
42      In addition, the selectivity of peptide deformylase for the N-formyl over the N-acetyl group has
43 proximately 10 mg of pure, fully active Fe2+ deformylase from a liter of cells.
44           As an example, recombinant peptide deformylase from Bacillus subtilis was overexpressed, de
45 nd to be excellent substrates of the peptide deformylase from Escherichia coli (k(cat)/K(M) = 6.9 x 1
46 e inhibitors of purified recombinant peptide deformylase from Escherichia coli and Bacillus subtilis.
47 imum and the catalytic activity of a peptide deformylase from Escherichia coli.
48  recently solved structure of the eukaryotic deformylase from Plasmodium falciparum, a complete pictu
49         Both recombinant Arabidopsis peptide deformylases had peptide deformylase activity with uniqu
50  first crystal structure of Class II peptide deformylase has been determined.
51               A new, sensitive assay for the deformylase has been developed by measuring the amount o
52               A continuous assay for peptide deformylase has been developed using a formylated dipept
53 Escherichia coli extracts 3 decades ago, the deformylase has resisted all attempts of purification or
54 ntibiotics, inhibitors of bacterial peptidyl-deformylase, has been discovered by combining mechanism-
55 duct Sch 382583 (1), an inhibitor of peptide deformylase, has been synthesized in 16 steps from comme
56 fication and characterization of the peptide deformylase have remained a major challenge because this
57 f O2 from the deformylase assays renders the deformylase highly stable under otherwise identical cond
58         We describe here a new human peptide deformylase (Homo sapiens PDF, or HsPDF) that is localiz
59                 The human homolog of peptide deformylase (HsPDF) resides in the mitochondria, along w
60 have, however, been able to overexpress this deformylase in Escherichia coli.
61 esults suggest an essential role for peptide deformylase in protein processing in all plant plastids.
62                GSK1322322 is a novel peptide deformylase inhibitor in the early phase of development
63  antibiotics, a glycylcycline, and a peptide deformylase inhibitor, a member of a new antibacterial c
64 eatment of Escherichia coli with the peptide deformylase inhibitor, actinonin, results in the expecte
65                Actinonin, a specific peptide deformylase inhibitor, was effective in vitro against Ar
66                        The proteins for both deformylase-inhibitor complexes show basically the same
67 , guidelines for the design of high-affinity deformylase inhibitors are suggested.
68 sults will facilitate the design of specific deformylase inhibitors as potential antibacterial agents
69 l quinolones that have high potency, peptide deformylase inhibitors, and new lincosamide, oxazolidino
70 play a role in the design of general peptide deformylase inhibitors.
71           We show that DefA, a minor peptide deformylase, inhibits the activity of BY-kinase PtkA whe
72 f oxidation of the catalytic Fe2+ ion of the deformylase into catalytically inactive Fe3+ ion by atmo
73                                          The deformylase is also capable of efficient deformylation o
74                                      Peptide deformylase is an essential Fe2+ metalloenzyme that cata
75                                 In vivo, the deformylase is capable of deformylating most of the poly
76                                     Purified deformylase is highly active toward N-formylated peptide
77           These results suggest that peptide deformylase is the likely molecular target responsible f
78  inhibitory activity toward Escherichia coli deformylase (K(I) = 0.67 nM) and antibacterial activity
79 otes, PurU (10-formyl tetrahydrofolate [THF] deformylase) metabolizes 10-formyl THF to formate and TH
80 recombinant form of Escherichia coli peptide deformylase (PDF(Ec)) via isothermal titration microcalo
81 the most potent natural inhibitor of peptide deformylase (PDF) and exerts antimicrobial and herbicida
82 ructs their ensuing deformylation by peptide deformylase (PDF) and hydrolysis by methionyl aminopepti
83  is mediated by 2 essential enzymes, peptide deformylase (PDF) and methionine aminopeptidase (MAP).
84                                      Peptide deformylase (PDF) catalyzes the hydrolytic removal of th
85                                      Peptide deformylase (PDF) catalyzes the hydrolytic removal of th
86                                      Peptide deformylase (PDF) catalyzes the removal of the N-termina
87                                      Peptide deformylase (PDF) catalyzes the subsequent removal of th
88           When the streptococcal polypeptide deformylase (PDF) gene (def1, encoding PDF) was placed u
89                                      Peptide deformylase (PDF) has been identified as a promising ant
90                                      Peptide deformylase (PDF) has received considerable attention du
91                                  Polypeptide deformylase (PDF) is a highly conserved bacterial enzyme
92                                  Polypeptide deformylase (PDF) is a novel broad-spectrum antibacteria
93                                      Peptide deformylase (PDF) is among the few antibacterial targets
94                                      Peptide deformylase (PDF) is an enzyme that is responsible for r
95                                  Polypeptide deformylase (PDF) is an essential bacterial metalloenzym
96                                      Peptide deformylase (PDF) is essential in prokaryotes and absent
97                                      Peptide deformylase (PDF) is involved in bacterial protein matur
98 actinonin, an inhibitor of bacterial peptide deformylase (PDF) whose activity is dependent on a hydro
99 able promoter region of the gene for peptide deformylase (PDF), a metal-dependent enzyme that removes
100 rminal Met residue of the peptide by peptide deformylase (PDF).
101 plication to kinetic characterization of the deformylase, pH profile studies, and enzyme inhibition a
102 ation for the protection of the epitope from deformylases present in the bacterial cell and suggests
103 ctive species, which covalently modifies the deformylase protein, most likely by oxidizing cysteine-9
104                                      Peptide deformylase proteins (PDFs) participate in the N-termina
105                                          The deformylase reaction is conveniently monitored on a UV-V
106     Removal of the formyl group by a peptide deformylase renders the dipeptide product, which contain
107  Limited treatment with the Escherichia coli deformylase resulted in the deformylation of those pepti
108 alciparum, a complete picture of the peptide deformylase structure and function relationship is emerg
109 employs a novel class of peptide mimetics as deformylase substrates which, upon enzymatic removal of
110 tylase may have an analogous function to the deformylase that generates undecaprenyl phosphate-4-amin
111 eir protein biosynthetic mechanisms, peptide deformylase, the bacterial enzyme responsible for deform
112 n of effective antibiotics targeting peptide deformylase, the structures of the protein-inhibitor com
113 d, three sample mononuclear enzymes, peptide deformylase, threonine dehydrogenase, and cytosine deami
114 sment of the catalytic properties of peptide deformylase using a series of synthetic N-formylated pep
115                                          The deformylase was also shown to exhibit esterase activity.
116 ocyclic, peptidomimetic inhibitor of peptide deformylase was designed by covalently cross-linking the
117 rotein expressed in a strain lacking peptide deformylase was shown to retain the formyl group confirm
118  rapid method to study kinetic properties of deformylases without the use of any coupling enzymes.

 
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