The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Endoglin is a component of the transforming growth factor-beta receptor system in human endothelial cells.
Open accessAbstract
Endoglin, a dimeric membrane glycoprotein expressed at high levels on human vascular endothelial cells, shares regions of sequence identity with betaglycan, a major binding protein for transforming growth factor-beta (TGF-beta) that co-exists with TGF-beta receptors I and II in a variety of cell lines but is low or absent in endothelial cells. We have examined whether endoglin also binds TGF-beta and demonstrate here that the major TGF-beta 1-binding protein co-existing with TGF-beta receptors I and II on human umbilical vein endothelial cells is endoglin, as determined by specific immunoprecipitation of endoglin affinity-labeled with 125I-TGF-beta. Furthermore, endoglin ectopically expressed in COS cells binds TGF-beta 1. Competition affinity-labeling experiments showed that endoglin binds TGF-beta 1 (KD approximately 50 pM) and TGF-beta 3 with high affinity but fails to bind TGF-beta 2. This difference in affinity of endoglin for the TGF-beta isoforms is in contrast to beta-glycan which recognizes all three isoforms. TGF-beta however is binding with high affinity to only a small fraction of the available endoglin molecules, suggesting that some rate-limiting event is required to sustain TGF-beta binding to endoglin.
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
Assoian, R. K., Komoriya, A., Meyers, C. A., Miller, D. M., & Sporn, M. B. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32345-7 · Cited by 1,598
Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase
Lin, H. Y., Wang, X.-F., Ng-Eaton, E., Weinberg, R. A., & Lodish, H. F. (1992) · Cell · doi:10.1016/0092-8674(92)90152-3 · Cited by 1,057
Seed, B., & Aruffo, A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3365 · Cited by 909
Expression cloning of an activin receptor, a predicted transmembrane serine kinase
Mathews, L. S., & Vale, W. W. (1991) · Cell · doi:10.1016/0092-8674(91)90549-e · Cited by 738
López-Casillas, F., Cheifetz, S., Doody, J., Andres, J. L., Lane, W. S., & Massague, J. (1991) · Cell · doi:10.1016/0092-8674(91)90073-8 · Cited by 676
Self-citationExpression cloning and characterization of the TGF-β type III receptor
Wang, X.-F., Lin, H. Y., Ng-Eaton, E., Downward, J., Lodish, H. F., & Weinberg, R. A. (1991) · Cell · doi:10.1016/0092-8674(91)90074-9 · Cited by 637
Receptors for the TGF-β family
Massagué, J. (1992) · Cell · doi:10.1016/0092-8674(92)90627-o · Cited by 637
Self-citationAttisano, L., Wrana, J. L., Cheifetz, S., & Massague, J. (1992) · Cell · doi:10.1016/0092-8674(92)90209-u · Cited by 474
Self-citationPrimary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells.
Gougos, A., & Letarte, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38892-1 · Cited by 452
Self-citationCheifetz, S., Hernandez, H., Laiho, M., ten Dijke, P., Iwata, K. K., & Massagué, J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30535-5 · Cited by 348
Self-citation
Cited by
Soluble endoglin contributes to the pathogenesis of preeclampsia
Venkatesha, S., Toporsian, M., Lam, C., Hanai, J.-I., Mammoto, T., Kim, Y. M., Bdolah, Y., Lim, K.-H., Yuan, H.-T., Libermann, T. A., et al. (2006) · Nature Medicine · doi:10.1038/nm1429 · Cited by 1,855
Self-citationGressner, A. M., & Weiskirchen, R. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00292.x · Cited by 718
Transforming Growth Factor-β1 to the Bone
Janssens, K., ten Dijke, P., Janssens, S., & Van Hul, W. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0001 · Cited by 710
TGF-β signaling in vascular biology and dysfunction
Goumans, M.-J., Liu, Z., & ten Dijke, P. (2009) · Cell Research · doi:10.1038/cr.2008.326 · Cited by 601
TGF-β – an excellent servant but a bad master
Kubiczkova, L., Sedlarikova, L., Hajek, R., & Sevcikova, S. (2012) · Journal of Translational Medicine · doi:10.1186/1479-5876-10-183 · Cited by 511
Metadata
- Authors
- Cheifetz, S., Bellón, T., Calés, C., Vera, S., Bernabeu, C., Massagué, J., & Letarte, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-09
- Volume
- 267
- Issue
- 27
- Pages
- 19027-19030
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1590052782
- Cited by
- 836
- References
- 27
- FWCI
- 8.02
- 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: Endoglin is a component of the transforming growth factor-beta receptor system in human endothelial cells. https://app.cochat.ai/papers/10.1016/s0021-9258(18)41732-2
- The paper
- Cheifetz, S., Bellón, T., Calés, C., Vera, S., Bernabeu, C., Massagué, J., & Letarte, M. (1992). Endoglin is a component of the transforming growth factor-beta receptor system in human endothelial cells. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)41732-2
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.
