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Hassanul G. Choudhury et al.
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Synthetic peptides derived from the sequence of a lasso peptide microcin J25 show antibacterial activity
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Microcin J25 membrane interaction: Selectivity toward gel phase
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Sequence Diversity in the Lasso Peptide Framework: Discovery of Functional Microcin J25 Variants with Multiple Amino Acid Substitutions
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Computational design of the lasso peptide antibiotic microcin J25
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Proton motive force dissipation precludes interaction of microcin J25 with RNA polymerase, but enhances reactive oxygen species overproduction
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Antimicrobial properties of aqueous extracts from three medicinal plants growing wild in arid regions of Tunisia
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Linear analogues of human β-defensin 3:: Concepts for design of antimicrobial peptides with reduced cytotoxicity to mammalian cells
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Microcin J25 induces the opening of the mitochondrial transition pore and cytochrome c release through superoxide generation
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FEBS JOURNAL (2008)
Systematic structure-activity analysis of microcin J25
Olga Pavlova et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
FTIR studies of temperature influence on the DPPG model membrane
Feride Severcan et al.
JOURNAL OF MOLECULAR STRUCTURE (2008)
Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
John D. F. Hale et al.
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Microcin J25 has dual and independent mechanisms of action in Escherichia coli:: RNA polymerase inhibition and increased superoxide production
Augusto Bellomio et al.
JOURNAL OF BACTERIOLOGY (2007)
Efficacy of microcin J25 in biomatrices and in a mouse model of Salmonella infection
Fabian E. Lopez et al.
JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY (2007)
Maturation of McjA precursor peptide into active microcin MccJ25
David J. Clarke et al.
ORGANIC & BIOMOLECULAR CHEMISTRY (2007)
Microcin J25 uptake:: His5 of the MccJ25 lariat ring is involved in interaction with the inner membrane MccJ25 transporter protein SbmA
RE de Cristóbal et al.
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Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
David I. Chan et al.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES (2006)
The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25:: role of the microcin Val11-Pro16 β-hairpin region in the recognition mechanism
D Destoumieux-Garzón et al.
BIOCHEMICAL JOURNAL (2005)
MccJ25 C-terminal is involved in RNA-polymerase inhibition but not in respiration inhibition
PA Vincent et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2005)
Structure-activity analysis of microcin J25: Distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase
E Semenova et al.
JOURNAL OF BACTERIOLOGY (2005)
The microcin J25 β-hairpin region is important for antibiotic uptake but not for RNA polymerase and respiration inhibition
A Bellomio et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2004)
Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel
J Mukhopadhyay et al.
MOLECULAR CELL (2004)
Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail
KA Wilson et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2003)
Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone
KJ Rosengren et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2003)
Structure of antibacterial peptide microcin J25: A 21-residue lariat protoknot
MJ Bayro et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2003)
Chemical modification of microcin J25 with diethylpyrocarbonate and carbodiimide: evidence for essential histidyl and carboxyl residues
A Bellomio et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2003)
Binding of pediocin PA-1 with anionic lipid induces model membrane destabilization
H Gaussier et al.
APPLIED AND ENVIRONMENTAL MICROBIOLOGY (2003)
Mutations of bacterial RNA polymerase leading to resistance to microcin J25
J Yuzenkova et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity
A Blond et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2002)
Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25
MA Delgado et al.
JOURNAL OF BACTERIOLOGY (2001)
The Use of Circular Dichroism in the Investigation of Protein Structure and Function
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Antibacterial activity evaluation of microcin J25 against diarrheagenic Escherichia coli
S Sable et al.
APPLIED AND ENVIRONMENTAL MICROBIOLOGY (2000)