Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations
By M. Melo, R. Ferré, Miguel A. R. B. Castanho. Nature Reviews Microbiology, 2009
674 citations recorded by the source corpus.
Subfields: Immunology, Microbiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/8527c84db0732614a4f2e69d656025d1cc4555a9
How researchers see this paper
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In Immunology
- M. Malmsten
- A. Schmidtchen
- Mukesh Pasupuleti
- Robert E. W. Hancock
- Gisbert Schneider
- Christopher D. Fjell
- Jan A. Hiss
In Microbiology
- M. Malmsten
- A. Schmidtchen
- Mukesh Pasupuleti
- Christopher D. Fjell
- Robert E. W. Hancock
- Gisbert Schneider
In Molecular Biology
- Christopher D. Fjell
- Robert E. W. Hancock
- Jan A. Hiss
- Gisbert Schneider
- M. Malmsten
- A. Schmidtchen
- Mukesh Pasupuleti
- Roderick E. Hubbard
Citations in the corpus
- Insights into Cronobacter sakazakii Biofilm Formation and Control Strategies in the Food Industry (2020, background): “AMPs can be classified into four types based on secondary structure—namely, b-sheet, a-helical, loop, and extended peptide—with the first two classes being the most common in nature [108].”
- Antimicrobial peptides: key components of the innate immune system (2012, background): “Prior to formation of both barrelstave and toroidal pores, the peptide adsorbs parallel to the membrane surface (Huang, 2006; Huang, 2009; Melo et al., 2009).”
- Designing antimicrobial peptides: form follows function (2011, background): “Some natural AMPs, like porcine protegrin, exhibit strong antimicrobial effects but in general the activity of AMPs is improved by their increased concentrations in phagocyte granules, the crypts of the intestine and near degranulating phagocytes 15–17 .”