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Cited by 534

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Primary structures of three human neutrophil defensins.

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Selsted, M E, Harwig, S S, Ganz, T, Schilling, J W, Lehrer, R I·1985·Journal of Clinical Investigation

Abstract

The primary structures of three human neutrophil antimicrobial peptides (HNP) were determined. The peptides, HNP-1, HNP-2, and HNP-3, which we have termed defensins, were rich in cystine, arginine, and aromatic residues, but were devoid of free sulfhydryl groups and carbohydrate moieties. They were 29-30 residues in length and identical in sequence in all but their amino terminal residues. The defensins were homologous in sequence to peptides of similar size and biological activity previously purified from rabbit polymorphonuclear leukocytes, but unrelated to other neutrophil proteins of known sequence. 11 amino acid residues of the human defensins, including all six cysteinyl residues, were invariantly conserved in the six rabbit members of this multigene peptide family. That similarly structured antimicrobial peptides are present in both rabbit and human leukocytes supports their purported role as cidal agents in phagocyte-mediated host defense.

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Metadata

Authors
Selsted, M. E., Harwig, S. S., Ganz, T., Schilling, J. W., & Lehrer, R. I.
Venue
Journal of Clinical Investigation
Published
1985-10-01
Volume
76
Issue
4
Pages
1436-1439
ISSN
0021-9738 (ISSN-L)
OpenAlex
W2022577580
Cited by
534
References
0
FWCI
14.66
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Primary structures of three human neutrophil defensins. https://app.cochat.ai/papers/10.1172/jci112121
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Selsted, M. E., Harwig, S. S., Ganz, T., Schilling, J. W., & Lehrer, R. I. (1985). Primary structures of three human neutrophil defensins. Journal of Clinical Investigation. https://doi.org/10.1172/jci112121

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.