The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The Crystal Structure of the Human (S100A8/S100A9)2 Heterotetramer, Calprotectin, Illustrates how Conformational Changes of Interacting α-Helices Can Determine Specific Association of Two EF-hand Proteins
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In the citing paper
“Each CP αβ heterodimer has two transition metal binding sites at the S100A8/S100A9 interface: a His3Asp site that sequesters Zn(II) and a His6 site that sequesters Mn(II), Fe(II), Ni(II) and Zn(II).4-9”
From Bacterial Responses to Iron Withholding by Calprotectin (2021) · cites this paper as [4]
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Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Intracellular and extracellular roles of S100 proteins
Donato, R. (2003) · Microscopy Research and Technique · doi:10.1002/jemt.10296 · Cited by 974
Hyperzincaemia and hypercalprotectinaemia: a new disorder of zinc metabolism
Sampson, B., Fagerhol, M. K., Sunderkötter, C., Golden, B. E., Richmond, P., Klein, N., Kovar, I. Z., Beattie, J. H., Wolska-Kusnierz, B., Saito, Y., et al. (2002) · The Lancet · doi:10.1016/s0140-6736(02)11683-7 · Cited by 122
Cited by
Donato, R., R. Cannon, B., Sorci, G., Riuzzi, F., Hsu, K., J. Weber, D., & L. Geczy, C. (2013) · Current Molecular Medicine · doi:10.2174/156652413804486214 · Cited by 1,316
Metal Chelation and Inhibition of Bacterial Growth in Tissue Abscesses
Corbin, B. D., Seeley, E. H., Raab, A., Feldmann, J., Miller, M. R., Torres, V. J., Anderson, K. L., Dattilo, B. M., Dunman, P. M., Gerads, R., et al. (2008) · Science · doi:10.1126/science.1152449 · Cited by 857
Calprotectin: from biomarker to biological function
Jukic, A., Bakiri, L., Wagner, E. F., Tilg, H., & Adolph, T. E. (2021) · Gut · doi:10.1136/gutjnl-2021-324855 · Cited by 500
Damo, S. M., Kehl-Fie, T. E., Sugitani, N., Holt, M. E., Rathi, S., Murphy, W. J., Zhang, Y., Betz, C., Hench, L., Fritz, G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220341110 · Cited by 388
Human calprotectin is an iron-sequestering host-defense protein
Nakashige, T. G., Zhang, B., Krebs, C., & Nolan, E. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1891 · Cited by 291
Metadata
- Authors
- Korndörfer, I. P., Brueckner, F., & Skerra, A.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2007-07
- Volume
- 370
- Issue
- 5
- Pages
- 887-898
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2044992731
- Cited by
- 276
- References
- 3
- FWCI
- 3.83
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
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- This page
- CoChat. (2026). Citation check: The Crystal Structure of the Human (S100A8/S100A9)2 Heterotetramer, Calprotectin, Illustrates how Conformational Changes of Interacting α-Helices Can Determine Specific Association of Two EF-hand Proteins. https://app.cochat.ai/papers/10.1016/j.jmb.2007.04.065
- The paper
- Korndörfer, I. P., Brueckner, F., & Skerra, A. (2007). The Crystal Structure of the Human (S100A8/S100A9)2 Heterotetramer, Calprotectin, Illustrates how Conformational Changes of Interacting α-Helices Can Determine Specific Association of Two EF-hand Proteins. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2007.04.065
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.
