The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Crystal Structure of Defensin HNP-3, an Amphiphilic Dimer: Mechanisms of Membrane Permeabilization
Abstract
Defensins (molecular weight 3500 to 4000) act in the mammalian immune response by permeabilizing the plasma membranes of a broad spectrum of target organisms, including bacteria, fungi, and enveloped viruses. The high-resolution crystal structure of defensin HNP-3 (1.9 angstrom resolution, R factor 0.19) reveals a dimeric β sheet that has an architecture very different from other lytic peptides. The dimeric assembly suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.
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Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Cited by
Defensins: antimicrobial peptides of innate immunity
Ganz, T. (2003) · Nature Reviews Immunology · doi:10.1038/nri1180 · Cited by 3,066
Yang, D., Biragyn, A., Hoover, D. M., Lubkowski, J., & Oppenheim, J. J. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104603 · Cited by 572
Multidimensional signatures in antimicrobial peptides
Yount, N. Y., & Yeaman, M. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401567101 · Cited by 402
Enteric defensins: antibiotic peptide components of intestinal host defense.
Selsted, M. E., Miller, S. I., Henschen, A. H., & Ouellette, A. J. (1992) · The Journal of cell biology · doi:10.1083/jcb.118.4.929 · Cited by 309
Self-citationAndersson, M., Gunne, H., Agerberth, B., Boman, A., Bergman, T., Sillard, R., Jörnvall, H., Mutt, V., Olsson, B., & Wigzell, H. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07150.x · Cited by 283
Metadata
- Authors
- Hill, C. P., Yee, J., Selsted, M. E., & Eisenberg, D.
- Venue
- Science
- Published
- 1991-03-22
- Volume
- 251
- Issue
- 5000
- Pages
- 1481-1485
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2104630130
- Cited by
- 507
- References
- 1
- FWCI
- 19.69
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hill, C. P., Yee, J., Selsted, M. E., & Eisenberg, D. (1991). Crystal Structure of Defensin HNP-3, an Amphiphilic Dimer: Mechanisms of Membrane Permeabilization. Science. https://doi.org/10.1126/science.2006422
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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.
