The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Structure of a Fibronectin Type III Domain from Tenascin Phased by MAD Analysis of the Selenomethionyl Protein
Abstract
Fibronectin type III domains are found in many different proteins including cell surface receptors and cell adhesion molecules. The crystal structure of one such domain from the extracellular matrix protein tenascin was determined. The structure was solved by multiwavelength anomalous diffraction (MAD) phasing of the selenomethionyl protein and has been refined to 1.8 angstrom resolution. The folding topology of this domain is identical to that of the extracellular domains of the human growth hormone receptor, the second domain of CD4, and PapD. Although distinct, this topology is similar to that of immunoglobulin constant domains. An Arg-Gly-Asp (RGD) sequence that can function for cell adhesion is found in a tight turn on an exposed loop.
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
Integrins: Versatility, modulation, and signaling in cell adhesion
Hynes, R. O. (1992) · Cell · doi:10.1016/0092-8674(92)90115-s · Cited by 9,859
[6] Use of T7 RNA polymerase to direct expression of cloned genes
William Studier, F., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562
New Perspectives in Cell Adhesion: RGD and Integrins
Ruoslahti, E., & Pierschbacher, M. D. (1987) · Science · doi:10.1126/science.2821619 · Cited by 4,865
Pierschbacher, M. D., & Ruoslahti, E. (1984) · Nature · doi:10.1038/309030a0 · Cited by 3,658
The Anatomy and Taxonomy of Protein Structure
Richardson, J. S. (1981) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,375
Relativistic Calculation of Anomalous Scattering Factors for X Rays
Cromer, D. T., & Liberman, D. (1970) · The Journal of Chemical Physics · doi:10.1063/1.1674266 · Cited by 2,973
Human Growth Hormone and Extracellular Domain of Its Receptor: Crystal Structure of the Complex
de Vos, A. M., Ultsch, M., & Kossiakoff, A. A. (1992) · Science · doi:10.1126/science.1549776 · Cited by 2,239
Structural design and molecular evolution of a cytokine receptor superfamily.
Bazan, J. F. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.6934 · Cited by 2,069
Deisenhofer, J. (1981) · PubMed · Cited by 1,422
Deisenhofer, J. (1981) · Biochemistry · doi:10.1021/bi00512a001 · Cited by 1,333
Cited by
RGD AND OTHER RECOGNITION SEQUENCES FOR INTEGRINS
Ruoslahti, E. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.697 · Cited by 3,191
The fibronectin type III domain as a scaffold for novel binding proteins
Koide, A., Bailey, C. W., Huang, X., & Koide, S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2238 · Cited by 585
Daniels, D. A., Chen, H., Hicke, B. J., Swiderek, K. M., & Gold, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2136683100 · Cited by 567
Nedd8 Modification of Cul-1 Activates SCFβTrCP-Dependent Ubiquitination of IκBα
Read, M. A., Brownell, J. E., Gladysheva, T. B., Hottelet, M., Parent, L. A., Coggins, M. B., Pierce, J. W., Podust, V. N., Luo, R.-S., Chau, V., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2326-2333.2000 · Cited by 363
[28] Phase determination from multiwavelength anomalous diffraction measurements
Hendrickson, W. A., & Ogata, C. M. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76074-9 · Cited by 349
Self-citation
Metadata
- Authors
- Leahy, D. J., Hendrickson, W. A., Aukhil, L., & Erickson, H. P.
- Venue
- Science
- Published
- 1992-11-06
- Volume
- 258
- Issue
- 5084
- Pages
- 987-991
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2002304568
- Cited by
- 503
- References
- 28
- FWCI
- 38.12
- Type
- journal article
- Language
- en
- Open access
- closed
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: Structure of a Fibronectin Type III Domain from Tenascin Phased by MAD Analysis of the Selenomethionyl Protein. https://app.cochat.ai/papers/10.1126/science.1279805
- The paper
- Leahy, D. J., Hendrickson, W. A., Aukhil, L., & Erickson, H. P. (1992). Structure of a Fibronectin Type III Domain from Tenascin Phased by MAD Analysis of the Selenomethionyl Protein. Science. https://doi.org/10.1126/science.1279805
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.
