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1 ght new variants of the five known class IIb microcins.
2 take of microcin B17, microcin J25 (formerly microcin 25), and bleomycin.
3         Here, we identify and characterize a microcin active against pathogenic Vibrio cholerae: MvcC
4 siderophore bacteriocins, known as class IIb microcins, affect the colonization of host-associated pa
5                                              Microcins are a class of ribosomally synthesized antibac
6                                   While some microcins are active as unmodified peptides, others are
7                                              Microcins are antibacterial small proteins secreted by g
8 lecular-weight post-translationally modified microcins are produced by Escherichia coli, inferences b
9                                              Microcins are small antibacterial proteins that mediate
10                                              Microcins are small secreted proteins that possess antim
11                                              Microcin B17 (MccB17) is a 3.1-kDa Escherichia coli anti
12                                              Microcin B17 (MccB17) is a peptidyl antibiotic that is s
13                                              Microcin B17 (MccB17) is a ribosomally encoded DNA-gyras
14                                              Microcin B17 (MccB17) is an antibacterial peptide produc
15 aturation of the Escherichia coli antibiotic Microcin B17 (MccB17), the McbA prepro-antibiotic is mod
16 ta about three such microcins--microcin J25, microcin B17 and microcin C7-C51--are discussed.
17                                              Microcin B17 has no detectable effect on gyrase-catalyse
18                                              Microcin B17 is a 3.1-kDa bactericidal peptide; the puta
19                              Esherichia coli microcin B17 is a posttranslationally modified peptide t
20 eavage produced by gyrase in the presence of microcin B17 is different from that produced by quinolon
21  these motifs (D132, D147, and D199) reduced Microcin B17 production in vivo and heterocycle formatio
22 gue 5'-adenylyl beta,gamma-imidodiphosphate, microcin B17 stabilises a gyrase-dependent DNA cleavage
23 eterocycle formation, and an enzyme complex, microcin B17 synthase, was purified and found to contain
24 ding and downstream heterocycle formation by microcin B17 synthase.
25                                          The microcin B17 synthetase converts glycine, serine, and cy
26 zoles and four oxazoles by the three subunit Microcin B17 synthetase.
27                               One of them is microcin B17, a bacterial topoisomerase inhibitor whose
28                    To produce the antibiotic Microcin B17, four Cys and four Ser residues are convert
29 omycin, gramicidin S, rapamycin, indolmycin, microcin B17, fumagillin, mycotoxins, Monascus pigments,
30 f BacA, SbmA, is implicated in the uptake of microcin B17, microcin J25 (formerly microcin 25), and b
31 bmA mutants, namely, increased resistance to microcin B17, microcin J25, and bleomycin, demonstrating
32 aturation of the Escherichia coli antibiotic Microcin B17, the product of the mcbA gene is modified p
33 ro that confer antibiotic activity on mature microcin B17.
34 ght to protect DNA gyrase from the action of microcin B17.
35 aturation of the Escherichia coli antibiotic Microcin B17.
36 nzymes involved in thiazole/oxazole-modified microcin biosynthesis, a rapidly growing sector of natur
37 ng homology to genes of the Escherichia coli Microcin C (McC) biosynthetic pathway.
38                        Translation inhibitor microcin C (McC) is a heptapeptide with an aspartate alp
39                                              Microcin C (McC) is a peptide-nucleotide antibiotic prod
40                                              Microcin C (McC) is a peptide-nucleotide antibiotic that
41                                              Microcin C (McC) is a potent antibacterial agent produce
42                                              Microcin C (McC) is heptapeptide adenylate antibiotic pr
43                Peptide-nucleotide antibiotic microcin C (McC) is produced by some Escherichia coli st
44                                              Microcin C (McC), a peptide-nucleotide Trojan horse anti
45                                              Microcin C and related antibiotics are Trojan-horse pept
46                                  Recently, a microcin C homologue from Bacillus amyloliquefaciens con
47                                              Microcin C is a heptapeptide-adenylate antibiotic produc
48                    Here, we describe a novel microcin C-like compound from Bacillus amyloliquefaciens
49                                 We show that microcin C-like compounds carrying terminal cytosines ar
50 g sensitive cells in the same way as E. coli microcin C.
51                               The antibiotic microcin C7 (McC) acts as a bacteriocide by inhibiting a
52                                              Microcin C7 (McC) is a Trojan horse peptide-conjugated a
53 tyl tRNA synthetase "Trojan horse" inhibitor microcin C7 (McC7) consists of a nonhydrolyzable asparty
54 oducer strains of Escherichia coli to afford microcin C7 (MccC7), a "Trojan horse" antibiotic that co
55 MccA heptapeptide during the biosynthesis of microcin C7 (MccC7), a 'Trojan horse' antibiotic.
56 ch microcins--microcin J25, microcin B17 and microcin C7-C51--are discussed.
57 ng those that are structurally distinct from microcin C7.
58                       Moreover, we show that microcins can act as narrow-spectrum therapeutics to inh
59 viously recognized and that synthetic hybrid microcins can be a viable tool to target clinically rele
60  providing the first evidence that class IIb microcins can target bacteria outside of the Enterobacte
61                         Importantly, we show microcins discovered here are active against pathogenic
62                                              Microcin E492 (Mcc) is a pore-forming bacteriotoxin.
63                                              Microcin E492 (Mcc), a low molecular weight bacteriocin
64 chinery, to the C-terminal serine residue of microcin E492 (MccE492), an 84 aa ribosomal antibiotic p
65 e remarkable post-translational tailoring of microcin E492 (MccE492), an 84-residue protein toxin sec
66                             The finding that microcin E492 naturally exists both as functional toxic
67                          We report here that microcin E492, a peptide naturally produced by Klebsiell
68                     Here we demonstrate that microcins enable the probiotic bacterium Escherichia col
69 ut microbiomes, we demonstrate that class II microcins encompass diverse sequence space, bacterial st
70                              We suggest that microcin exerts its effects through a mechanism that has
71                         Two newly discovered microcins exhibit activity against Gram-negative ESKAPE
72 iscovered from the thiazole/oxazole-modified microcins family and the linear azole-containing peptide
73 ls the overlooked abundance and diversity of microcins found dispersed throughout Bacteria and opens
74                         Low-molecular-weight microcins from the post-translationally modified group t
75        This study underscores that class IIb microcin genes are more prevalent in the microbial world
76 sed on immunity to the antimicrobial peptide microcin H47 (MccH47).
77 strate fragments of the structurally related microcins H47, I47, and M.
78                                     However, microcins have been found almost exclusively in Enteroba
79 potential, we heterologously expressed these microcins in E. coli and demonstrated efficacy against a
80 e discovered 12 previously unknown class IIb microcins in seven additional Enterobacteriaceae species
81 ne-resistant mutants, are cross resistant to microcin-induced DNA cleavage.
82  Gram-negative bacteriocins, called class II microcins, is in fact a highly abundant, sequence- and f
83 is implicated in the uptake of microcin B17, microcin J25 (formerly microcin 25), and bleomycin.
84 ructures of the antibacterial lasso peptides microcin J25 (MccJ25) and capistruin (Cap) bound to thei
85 al methods, knot-like lasso peptides such as microcin J25 (MccJ25) and their analogues remain elusive
86                                      Peptide microcin J25 (MccJ25) inhibits bacterial RNA polymerase.
87                    The antibacterial peptide microcin J25 (MccJ25) inhibits transcription by bacteria
88                        21 amino acid peptide Microcin J25 (MccJ25) inhibits transcription by bacteria
89                                              Microcin J25 (MccJ25) is a 21-amino acid peptide inhibit
90                                              Microcin J25 (MccJ25) is a 21-residue plasmid-encoded ri
91                                              Microcin J25 (MccJ25) is a ribosomally synthesized antim
92                                              Microcin J25 (MccJ25) is an antimicrobial peptide with a
93                    The antimicrobial peptide microcin J25 (MccJ25) is matured by two enzymes, McjB an
94             Mutagenesis of the lasso peptide microcin J25 (MccJ25) with two cysteine residues followe
95  to make Escherichia coli cells resistant to microcin J25 (MccJ25), a bactericidal 21-amino acid pept
96 in to characterize the folding propensity of microcin J25 (MccJ25), a lasso peptide known for its ant
97 tructure of capistruin is similar to that of microcin J25 (MccJ25), a threaded-lasso antibacterial pe
98 ter and found that is reminiscent of that of microcin J25 (MccJ25), an RNA polymerase-inhibiting lass
99 e (RNAP) inhibition assay using citrocin and microcin J25 against E. coli RNAP.
100 higher minimal inhibition concentration than microcin J25 does against E. coli but surprisingly is ~1
101 igger-loop movements with the RNAP inhibitor microcin J25 prior to commitment inhibits termination, i
102 amely, increased resistance to microcin B17, microcin J25, and bleomycin, demonstrating the functiona
103  functional data about three such microcins--microcin J25, microcin B17 and microcin C7-C51--are disc
104  chemical syntheses of the cyclic antibiotic microcin J25, the 56-amino acid streptococcal protein G
105 press and secrete the antimicrobial peptide, Microcin J25.
106 d compounds in the thiazole/oxazole-modified microcins/linear azole-containing peptides family.
107           We introduce three novel clades of microcins (MccW, MccX, and MccZ), while also identifying
108    Our work provides the first evidence that microcins mediate inter- and intraspecies competition am
109 uctural and functional data about three such microcins--microcin J25, microcin B17 and microcin C7-C5
110        report the discovery of a V. cholerae microcin, MvcC.
111 Our results provide a detailed analysis of a microcin outside of Enterobacteriaceae and its potential
112                                              Microcin PDI inhibits a diversity of pathogenic Escheric
113                                              Microcin-producing EcN limits the growth of competitors
114 therapeutic administration of the wild-type, microcin-producing EcN to mice previously infected with
115               We hypothesized that class IIb microcin production extends beyond these specific compou
116 regulation of iron acquisition, capsule, and microcin secretion genes, thus partially mimicking growt
117 lysaccharide synthesis, drug resistance, and microcin secretion.
118 dified posttranslationally by the multimeric Microcin synthetase complex (composed of McbB, C, and D)
119 ified post-translationally by the multimeric microcin synthetase complex (composed of the McbB, -C, a
120 the overexpression and rapid purification of microcin synthetase has been developed using a calmoduli
121 k indicate that MccPDI is unique amongst the microcins that have been described to date.
122 e repurposing of a thiazole/oxazole-modified microcin (TOMM) cyclodehydratase to site-specifically in
123 lysin S (LLS) is a thiazole/oxazole-modified microcin (TOMM) produced by hypervirulent clones of List
124                    Thiazole/oxazole-modified microcins (TOMMs) are a class of post-translationally mo
125                The thiazole/oxazole-modified microcins (TOMMs) represent a burgeoning class of riboso
126 novel siderophore receptors), cvaC (colicin [microcin] V), traT (serum-resistance associated), ibeA (
127 th antibiotic biosynthesis in vivo, yielding microcin with six, seven, and eight rings, all with bioa

 
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