The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Dimerization of the Extracellular Domain of the Human Growth Hormone Receptor by a Single Hormone Molecule
Abstract
Human growth hormone (hGH) forms a 1:2 complex with the extracellular domain of its receptor-binding protein (hGHbp) as studied by crystallization, size exclusion chromatography, calorimetry, and a previously undescribed fluorescence quenching assay. These and other experiments with protein engineered variants of hGH have led to the identification of the binding determinants for two distinct but adjacent sites on hGH for the hGHbp, and the data indicated that there are two overlapping binding sites on the hGHbp for hGH. Furthermore, the binding of hGH to the hGHbp occurred sequentially; a first hGHbp molecule bound to site 1 on hGH and then a second hGHbp bound to site 2. Hormone-induced receptor dimerization is proposed to be relevant to the signal transduction mechanism for the hGH receptor and other related cytokine 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
Solvent content of protein crystals
Matthews, B. W. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90205-2 · Cited by 7,961
Signal transduction by receptors with tyrosine kinase activity
Ullrich, A., & Schlessinger, J. (1990) · Cell · doi:10.1016/0092-8674(90)90801-k · Cited by 5,435
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
GROWTH FACTOR RECEPTOR TYROSINE KINASES
Yarden, Y., & Ullrich, A. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.002303 · Cited by 1,838
High-Resolution Epitope Mapping of hGH-Receptor Interactions by Alanine-Scanning Mutagenesis
Cunningham, B. C., & Wells, J. A. (1989) · Science · doi:10.1126/science.2471267 · Cited by 1,367
Self-citationInterleukin 2 high-affinity receptor expression requires two distinct binding proteins.
Teshigawara, K., Wang, H. M., Kato, K., & Smith, K. A. (1987) · The Journal of experimental medicine · doi:10.1084/jem.165.1.223 · Cited by 548
A new cytokine receptor superfamily
Cosman, D., Lyman, S. D., Idzerda, R. L., Beckmann, M. P., Park, L. S., Goodwin, R. G., & March, C. J. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90051-c · Cited by 476
Three-dimensional structure of a genetically engineered variant of porcine growth hormone.
Abdel-Meguid, S. S., Shieh, H. S., Smith, W. W., Dayringer, H. E., Violand, B. N., & Bentle, L. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.18.6434 · Cited by 458
Cloning of an Interleukin-3 Receptor Gene: a Member of a Distinct Receptor Gene Family
Itoh, N., Yonehara, S., Schreurs, J., Gorman, D. M., Maruyama, K., Ishii, A., Yahara, I., Arai, K.-I., & Miyajima, A. (1990) · Science · doi:10.1126/science.2404337 · Cited by 401
Hormone phage: An enrichment method for variant proteins with altered binding properties
Bass, S., Greene, R., & Wells, J. A. (1990) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340080405 · Cited by 356
Self-citation
Cited by
Dimerization of cell surface receptors in signal transduction
Heldin, C.-H. (1995) · Cell · doi:10.1016/0092-8674(95)90404-2 · Cited by 1,634
The IL-4 receptor: signaling mechanisms and biologic functions
Nelms, K., Keegan, A. D., Zamorano, J., Ryan, J. J., & Paul, W. E. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.701 · Cited by 1,545
Leptin receptor missense mutation in the fatty Zucker rat
Phillips, M. S., Liu, Q., Hammond, H. A., Dugan, V., Hey, P. J., Caskey, C. T., & Hess, J. F. (1996) · Nature Genetics · doi:10.1038/ng0596-18 · Cited by 822
Spivak-Kroizman, T., Lemmon, M. A., Dikic, I., Ladbury, J. E., Pinchasi, D., Huang, J., Jaye, M., Crumley, G., Schlessinger, J., & Lax, I. (1994) · Cell · doi:10.1016/0092-8674(94)90032-9 · Cited by 658
Assessment of Growth Parameters and Life Span of GHR/BP Gene-Disrupted Mice 1
Coschigano, K. T., Clemmons, D., Bellush, L. L., & Kopchick, J. J. (2000) · Endocrinology · doi:10.1210/endo.141.7.7586 · Cited by 611
Metadata
- Authors
- Cunningham, B. C., Ultsch, M., de Vos, A. M., Mulkerrin, M. G., Clauser, K. R., & Wells, J. A.
- Venue
- Science
- Published
- 1991-11-08
- Volume
- 254
- Issue
- 5033
- Pages
- 821-825
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2068187158
- Cited by
- 874
- References
- 18
- FWCI
- 52.80
- 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: Dimerization of the Extracellular Domain of the Human Growth Hormone Receptor by a Single Hormone Molecule. https://app.cochat.ai/papers/10.1126/science.1948064
- The paper
- Cunningham, B. C., Ultsch, M., de Vos, A. M., Mulkerrin, M. G., Clauser, K. R., & Wells, J. A. (1991). Dimerization of the Extracellular Domain of the Human Growth Hormone Receptor by a Single Hormone Molecule. Science. https://doi.org/10.1126/science.1948064
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.
