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in microarray experiments. BMC Bioinformatics 2006, 7:538.PubMedCrossRef 42. Histobase [http://​histo.​ucsf.​edu] 43. The Genome Center at Washington University [http://​genome.​wustl.​edu] 44. Histoplasma capsulatum Database (BROAD Institute) [http://​www.​broad.​mit.​edu/​annotation/​genome/​histoplasma_​capsulatum/​MultiHome.​html] Authors’ contributions MCL performed the molecular genetics, protein, and mating studies, and drafted the document.

AGS generated strains and molecular reagents, G protein-coupled receptor kinase directed design and coordination of the studies, and helped draft the document. Both authors have read and approved the final manuscript.”
“Background Antimicrobial peptides (AMPs) are peptides that are selectively toxic against microbes. To date, more than 800 AMPs have been discovered in various organisms including vertebrates, invertebrates, plants, protozoans, and microbes. The structures of AMPs are extremely diverse. They are categorized into distinct structural groups such as amphipathic α-helical peptides, and β-sheet peptides stabilized by intramolecular disulfide bridges [1]. Several AMPs are already in practical use. For instance, nisin is a widely used food-preservative in more than 50 countries including the United States of America, and countries within the European Union [2]. Polymyxin B has been used as a clinical antibiotic for more than half a century [3]. Many AMPs have also been investigated for practical use [4]. Microbial killing by AMPs is often correlated mainly with membrane disruption although some other intracelluar and extracellular mechanisms also contribute to overall activity [1]. Several AMPs such as indolicidin attack intracellular targets without membrane disruption [5]. Using combinations of agents is common in a clinical setting in order to obtain more effective antimicrobial properties.

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