Journal ArticleDOI
Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance.
TLDR
In hagfish cathelicidins, the unusual amino acid bromotryptophan may make the active peptides less susceptible to proteolysis for steric reasons, and such protease resistance could extend the pharmacokinetic lifetimes of cathe Licidins in vivo, sustaining antimicrobial activity.About:
This article is published in Bioorganic Chemistry.The article was published on 2003-12-01. It has received 149 citations till now. The article focuses on the topics: Cathelicidins & Cathelicidin.read more
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The Front Line of Enteric Host Defense against Unwelcome Intrusion of Harmful Microorganisms: Mucins, Antimicrobial Peptides, and Microbiota
TL;DR: Whether the cells producing mucins or antimicrobial peptides and the resident microbiota act in partnership and whether they function individually and/or synergistically to provide the host with an effective front line of defense against harmful enteric pathogens is examined.
Journal ArticleDOI
Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases
Magdalena Sieprawska-Lupa,Piotr Mydel,Katarzyna Krawczyk,Kinga Wójcik,Magdalena Puklo,Boguslaw Lupa,Piotr Suder,Jerzy Silberring,Matthew S. Reed,Jan Pohl,William M. Shafer,William M. Shafer,Fionnuala McAleese,Timothy J. Foster,J. Travis,Jan Potempa +15 more
TL;DR: Data suggest that aureolysin production by S. aureus contributes to the resistance of this pathogen to the innate immune system of humans mediated by LL-37.
Journal ArticleDOI
Antimicrobial peptide resistance mechanisms of human bacterial pathogens.
TL;DR: Experimental analysis has identified diverse mechanisms of bacterial AMP resistance including altered cell surface charge, active efflux, production of proteases or trapping proteins, and modification of host cellular processes.
Journal ArticleDOI
The human cathelicidin LL-37--A pore-forming antibacterial peptide and host-cell modulator.
Daniela Xhindoli,Sabrina Pacor,Monica Benincasa,Marco Scocchi,Renato Gennaro,Alessandro Tossi +5 more
TL;DR: This review considers the human cathelicidin hCAP18/LL-37's modes of interaction with bacterial membranes and capacity to act as a pore-forming toxin directed by the organism against bacterial cells, contrasting this with the mode of action of related peptides from other species.
Journal ArticleDOI
Antimicrobial Peptides from Fish
TL;DR: Some of the unique properties of fish peptides, including their ability to act even in very high salt concentrations, make them good potential targets for development as therapeutic antimicrobials.
References
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Journal ArticleDOI
Antimicrobial peptides of multicellular organisms
TL;DR: As the need for new antibiotics becomes more pressing, could the design of anti-infective drugs based on the design principles these molecules teach us?
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Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites.
TL;DR: A new method for the identification of signal peptides and their cleavage sites based on neural networks trained on separate sets of prokaryotic and eukaryotic sequence that performs significantly better than previous prediction schemes and can easily be applied on genome-wide data sets.
SHORT COMMUNICATION Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
TL;DR: In this paper, a new method for the identification of in performance compared with the weight matrix method signal peptides and their cleavage sites based on neural (Arrigo et al., 1991; Ladunga et al, 1991; Schneider and networks trained on separate sets of prokaryotic and eukaryotic sequence.
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On the size of the active site in proteases. I. Papain.
Israel Schechter,Arieh Berger +1 more
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Serine protease mechanism and specificity
TL;DR: This article will review recent work on the mechanism and specificity of chymotrypsin-like enzymes, with the occasional references to pertinent experiments with subtilisin.