The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Crystallographic Evidence for Preformed Dimers of Erythropoietin Receptor Before Ligand Activation
Abstract
Erythropoietin receptor (EPOR) is thought to be activated by ligand-induced homodimerization. However, structures of agonist and antagonist peptide complexes of EPOR, as well as an EPO-EPOR complex, have shown that the actual dimer configuration is critical for the biological response and signal efficiency. The crystal structure of the extracellular domain of EPOR in its unliganded form at 2.4 angstrom resolution has revealed a dimer in which the individual membrane-spanning and intracellular domains would be too far apart to permit phosphorylation by JAK2. This unliganded EPOR dimer is formed from self-association of the same key binding site residues that interact with EPO-mimetic peptide and EPO ligands. This model for a preformed dimer on the cell surface provides insights into the organization, activation, and plasticity of recognition of hematopoietic cell surface receptors.
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
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Cited by
Principles of interleukin (IL)-6-type cytokine signalling and its regulation
HEINRICH, P. C., BEHRMANN, I., HAAN, S., HERMANNS, H. M., MÜLLER-NEWEN, G., & SCHAPER, F. (2003) · Biochemical Journal · doi:10.1042/bj20030407 · Cited by 3,272
The JAK/STAT signaling pathway: from bench to clinic
Hu, X., li, J., Fu, M., Zhao, X., & Wang, W. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00791-1 · Cited by 2,633
Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
Kunishima, N., Shimada, Y., Tsuji, Y., Sato, T., Yamamoto, M., Kumasaka, T., Nakanishi, S., Jingami, H., & Morikawa, K. (2000) · Nature · doi:10.1038/35039564 · Cited by 1,249
Schlessinger, J., Plotnikov, A. N., Ibrahimi, O. A., Eliseenkova, A. V., Yeh, B. K., Yayon, A., Linhardt, R. J., & Mohammadi, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00073-3 · Cited by 1,199
The molecular details of cytokine signaling via the JAK/STAT pathway
Morris, R., Kershaw, N. J., & Babon, J. J. (2018) · Protein Science · doi:10.1002/pro.3519 · Cited by 943
Metadata
- Authors
- Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K., & Wilson, I. A.
- Venue
- Science
- Published
- 1999-02-12
- Volume
- 283
- Issue
- 5404
- Pages
- 987-990
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2070921472
- Cited by
- 599
- References
- 2
- FWCI
- 24.11
- 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: Crystallographic Evidence for Preformed Dimers of Erythropoietin Receptor Before Ligand Activation. https://app.cochat.ai/papers/10.1126/science.283.5404.987
- The paper
- Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K., & Wilson, I. A. (1999). Crystallographic Evidence for Preformed Dimers of Erythropoietin Receptor Before Ligand Activation. Science. https://doi.org/10.1126/science.283.5404.987
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.
