The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
The Solution Structures of the Human β-Defensins Lead to a Better Understanding of the Potent Bactericidal Activity of HBD3 against Staphylococcus aureus
Open accessAbstract
The three human beta-defensins, HBD1--3, are 33--47-residue, cationic antimicrobial proteins expressed by epithelial cells. All three proteins have broad spectrum antimicrobial activity, with HBD3 consistently being the most potent. Additionally, HBD3 has significant bactericidal activity against Gram-positive Staphylococcus aureus at physiological salt concentrations. We have compared the multimeric state of the three beta-defensins using NMR diffusion spectroscopy, dynamic and static light scattering, and analysis of the migration of the three beta-defensins on a native gel. All three techniques are in agreement, suggesting that HBD-3 is a dimer, while HBD-1 and HBD-2 are monomeric. Subsequently, the NMR solution structures of HBD1 and HBD3 were determined using standard homonuclear techniques and compared with the previously determined solution structure of HBD2. Both HBD1 and HBD3 form well defined structures with backbone root mean square deviations of 0.451 and 0.616 A, respectively. The tertiary structures of all three beta-defensins are similar, with a short helical segment preceding a three-stranded antiparallel beta-sheet. The surface charge density of each of the defensins is markedly different, with the surface of HBD3 significantly more basic. Analysis of the NMR data and structures led us to suggest that HBD3 forms a symmetrical dimer through strand beta2 of the beta-sheet. The increased anti-Staphylococcal activity of HBD3 may be explained by the capacity of the protein to form dimers in solution at low concentrations, an amphipathic dimer structure, and the increased positive surface charge compared with HBD1 and HBD2.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Thompson, J. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.24.4876 · Cited by 38,993
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,965
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics News · doi:10.1051/epn/19861701011 · Cited by 7,989
MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,163
NMR of Proteins and Nucleic Acids
(2006) · Nuclear Magnetic Resonance · doi:10.1039/9781847555236-00336 · Cited by 5,863
NMR View: A computer program for the visualization and analysis of NMR data
Johnson, B. A., & Blevins, R. A. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00404272 · Cited by 3,090
Proteins: Structures and Molecular Properties
Creighton, T. E. (1986) · Medical Entomology and Zoology · Cited by 2,645
Wishart, D. S., Sykes, B. D., & Richards, F. M. (1992) · Biochemistry · doi:10.1021/bi00121a010 · Cited by 2,051
β-Defensins: Linking Innate and Adaptive Immunity Through Dendritic and T Cell CCR6
Yang, D., Chertov, O., Bykovskaia, S. N., Chen, Q., Buffo, M. J., Shogan, J., Anderson, M., Schröder, J. M., Wang, J. M., Howard, O. M. Z., et al. (1999) · Science · doi:10.1126/science.286.5439.525 · Cited by 1,809
Cited by
Cytokines and chemokines orchestrate atopic skin inflammation
Homey, B., Steinhoff, M., Ruzicka, T., & Leung, D. Y. M. (2006) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2006.03.047 · Cited by 579
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
Lehrer, R. I. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro976 · Cited by 448
Hunter, H. N., Fulton, D. B., Ganz, T., & Vogel, H. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205305200 · Cited by 400
Self-citationHuman β-defensin-3 activates professional antigen-presenting cells via Toll-like receptors 1 and 2
Funderburg, N., Lederman, M. M., Feng, Z., Drage, M. G., Jadlowsky, J., Harding, C. V., Weinberg, A., & Sieg, S. F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702130104 · Cited by 373
Metadata
- Authors
- Schibli, D. J., Hunter, H. N., Aseyev, V., Starner, T. D., Wiencek, J. M., McCray, P. B., Tack, B. F., & Vogel, H. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-03
- Volume
- 277
- Issue
- 10
- Pages
- 8279-8289
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1990519548
- Cited by
- 347
- References
- 59
- FWCI
- 15.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The Solution Structures of the Human β-Defensins Lead to a Better Understanding of the Potent Bactericidal Activity of HBD3 against Staphylococcus aureus. https://app.cochat.ai/papers/10.1074/jbc.m108830200
- The paper
- Schibli, D. J., Hunter, H. N., Aseyev, V., Starner, T. D., Wiencek, J. M., McCray, P. B., Tack, B. F., & Vogel, H. J. (2002). The Solution Structures of the Human β-Defensins Lead to a Better Understanding of the Potent Bactericidal Activity of HBD3 against Staphylococcus aureus. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m108830200
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
