|
1
|
Two enzymes catalyze the maturation of a lasso peptide in Escherichia coli.
|
Chem Biol
|
2007
|
2.10
|
|
2
|
Identification of peptaibols from Trichoderma virens and cloning of a peptaibol synthetase.
|
J Biol Chem
|
2002
|
1.47
|
|
3
|
Microcin C51 plasmid genes: possible source of horizontal gene transfer.
|
Antimicrob Agents Chemother
|
2003
|
1.35
|
|
4
|
Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.
|
J Biol Chem
|
2004
|
1.27
|
|
5
|
Microcin E492 antibacterial activity: evidence for a TonB-dependent inner membrane permeabilization on Escherichia coli.
|
Mol Microbiol
|
2003
|
1.11
|
|
6
|
The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11-Pro16 beta-hairpin region in the recognition mechanism.
|
Biochem J
|
2005
|
1.09
|
|
7
|
Dissecting the maturation steps of the lasso peptide microcin J25 in vitro.
|
Chembiochem
|
2012
|
0.96
|
|
8
|
Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity.
|
Eur J Biochem
|
2002
|
0.95
|
|
9
|
Microcin J25, from the macrocyclic to the lasso structure: implications for biosynthetic, evolutionary and biotechnological perspectives.
|
Curr Protein Pept Sci
|
2004
|
0.94
|
|
10
|
Sequence determinants governing the topology and biological activity of a lasso peptide, microcin J25.
|
Chembiochem
|
2012
|
0.85
|
|
11
|
Post-translational modification and folding of a lasso-type gene-encoded antimicrobial peptide require two enzymes only in Escherichia coli.
|
Adv Exp Med Biol
|
2009
|
0.78
|
|
12
|
Combined use of LC/MS and a biological test for rapid identification of marine mycotoxins produced by Trichoderma koningii.
|
J Microbiol Methods
|
2002
|
0.77
|