The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Antibacterial peptides: basic facts and emerging concepts
Abstract
Abstract. Boman HG (Microbiology and Tumor Biology Center, Karolinska Institutet, Stockholm, Sweden). Antibacterial peptides: basic facts and emerging concepts (Review). J Intern Med 2003; 254: 197–215. Antibacterial peptides are the effector molecules of innate immunity. Generally they contain 15–45 amino acid residues and the net charge is positive. The cecropin type of linear peptides without cysteine were found first in insects, whilst the defensin type with three disulphide bridges were found in rabbit granulocytes. Now a database stores more than 800 sequences of antibacterial peptides and proteins from the animal and plant kingdoms. Generally, each species has 15–40 peptides made from genes, which code for only one precursor. The dominating targets are bacterial membranes and the killing reaction must be faster than the growth rate of the bacteria. Some antibacterial peptides are clearly multifunctional and an attempt to predict this property from the hydrophobicity of all amino acid side chains are given. Gene structures and biosynthesis are known both in the fruit fly Drosophila and several mammals. Humans need two classes of defensins and the cathelicidin‐derived linear peptide LL‐37. Clinical cases show that deficiencies in these peptides give severe symptoms. Examples given are morbus Kostmann and atopic allergy. Several antibacterial peptides are being developed as drugs.
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Citations
Cites
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Endogenous Antimicrobial Peptides and Skin Infections in Atopic Dermatitis
Ong, P. Y., Ohtake, T., Brandt, C., Strickland, I., Boguniewicz, M., Ganz, T., Gallo, R. L., & Leung, D. Y. M. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa021481 · Cited by 1,960
Innate antimicrobial peptide protects the skin from invasive bacterial infection
Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198
Comparative Genome and Proteome Analysis of Anopheles gambiae and Drosophila melanogaster
Zdobnov, E. M., von Mering, C., Letunic, I., Torrents, D., Suyama, M., Copley, R. R., Christophides, G. K., Thomasova, D., Holt, R. A., Subramanian, G. M., et al. (2002) · Science · doi:10.1126/science.1077061 · Cited by 553
Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study
Pütsep, K., Carlsson, G., Boman, H. G., & Andersson, M. (2002) · The Lancet · doi:10.1016/s0140-6736(02)11201-3 · Cited by 499
Self-citation
Cited by
LL-37, the only human member of the cathelicidin family of antimicrobial peptides
Dürr, U. H. N., Sudheendra, U. S., & Ramamoorthy, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.030 · Cited by 1,049
APD2: the updated antimicrobial peptide database and its application in peptide design.
Wang, G., Li, X., & Wang, Z. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn823 · Cited by 941
Defensins in innate antiviral immunity
Klotman, M. E., & Chang, T. L. (2006) · Nature Reviews Immunology · doi:10.1038/nri1860 · Cited by 471
Dermal adipocytes protect against invasive Staphylococcus aureus skin infection
Zhang, L.-J., Guerrero-Juarez, C. F., Hata, T., Bapat, S. P., Ramos, R., Plikus, M. V., & Gallo, R. L. (2015) · Science · doi:10.1126/science.1260972 · Cited by 471
Adrenergic regulation of innate immunity: a review
Scanzano, A., & Cosentino, M. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00171 · Cited by 323
Book, M., Chen, Q., Lehmann, L. E., Klaschik, S., Weber, S., Schewe, J.-C., Luepertz, M., Hoeft, A., & Stuber, F. (2007) · Critical Care · doi:10.1186/cc5694 · Cited by 37
Main methods and tools for peptide development based on protein-protein interactions (PPIs)
Baeza, J., Bedoya, M., Cruz, P., Ojeda, P., Adasme-Carreño, F., Cerda, O., & González, W. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151623 · Cited by 8
Metadata
- Authors
- Boman, H. G.
- Venue
- Journal of Internal Medicine
- Publisher
- Wiley
- Published
- 2003-08-20
- Volume
- 254
- Issue
- 3
- Pages
- 197-215
- ISSN
- 0954-6820 (ISSN-L)
- 1365-2796
- OpenAlex
- W1997868832
- Cited by
- 1,158
- References
- 5
- FWCI
- 36.94
- Type
- journal article
- Language
- en
- Open access
- closed
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