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microcin E492 biosynthetic process by siderophore ester modification of peptidyl-serine

Known as: microcin E492 anabolism by siderophore ester modification of peptidyl-serine, microcin E492 formation by siderophore ester modification of peptidyl-serine, microcin E492 synthesis by siderophore ester modification of peptidyl-serine 
The modification of serine to N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl… 
National Institutes of Health

Papers overview

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Highly Cited
2015
Highly Cited
2015
Characterization of Sviceucin from Streptomyces Provides Insight into Enzyme Exchangeability and Disulfide Bond Formation in Lasso Peptides.
Lasso peptides are bacterial ribosomally synthesized and post-translationally modified peptides. They have sparked increasing… 
Highly Cited
2012
Highly Cited
2012
Sequence Determinants Governing the Topology and Biological Activity of a Lasso Peptide, Microcin J25
Microcin J25 is a potent antibacterial peptide produced by Escherichia coli AY25. It displays a lasso structure, which consists… 
Review
2009
Review
2009
Antibacterial and antitumorigenic properties of microcin E492, a pore-forming bacteriocin.
Microcins are a family of low-molecular weight bacteriocins produced and secreted by Gram-negative bacteria. This review is… 
Highly Cited
2007
Highly Cited
2007
Biosynthetic tailoring of microcin E492m: post-translational modification affords an antibacterial siderophore-peptide conjugate.
The present work reveals that four proteins, MceCDIJ, encoded by the MccE492 gene cluster are responsible for the remarkable post… 
Highly Cited
2002
Highly Cited
2002
Mutations of Bacterial RNA Polymerase Leading to Resistance to Microcin J25*
A mutation in the conserved segment of therpoC gene, which codes for the largest RNA polymerase (RNAP) subunit, β′, was found to… 
Highly Cited
2002
Highly Cited
2002
Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae, induces apoptosis in some human cell lines
The cytotoxic effect of microcin E492, a low-molecular-mass channel-forming bacteriocin (7,887 Da) produced by a strain of… 
Highly Cited
2001
Highly Cited
2001
Structure, organization and characterization of the gene cluster involved in the production of microcin E492, a channel‐forming bacteriocin
Microcin E492 is a low‐molecular‐weight, channel‐forming bacteriocin produced and excreted by Klebsiella pneumoniae RYC492. A 13… 
Highly Cited
2000
Highly Cited
2000
Antibacterial Activity Evaluation of Microcin J25 against Diarrheagenic Escherichia coli
ABSTRACT The inhibitory activities of known microcins were evaluated against some diarrheagenic Escherichia coli strains. Some… 
Highly Cited
1993
Highly Cited
1993
Microcin E492 forms ion channels in phospholipid bilayer membranes
Highly Cited
1985
Highly Cited
1985
Microcin E492, a low-molecular-weight peptide antibiotic which causes depolarization of the Escherichia coli cytoplasmic membrane
Microcin E492 is a 5,000- to 7,000-molecular-weight peptide antibiotic which depolarizes the cytoplasmic membrane of sensitive… 
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