The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.
A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos
Open accessAbstract
A Drosophila gene (drk) encodes a widely expressed protein with a single SH2 domain and two flanking SH3 domains, which is homologous to the Sem-5 protein of C. elegans and mammalian GRB2. Genetic analysis suggests that drk function is essential for signaling by the sevenless receptor tyrosine kinase. Drk biological activity correlates with binding of its SH2 domain to activated receptor tyrosine kinases and concomitant localization of drk to the plasma membrane. In vitro, drk also binds directly to the C-terminal tail of Sos, a Ras guanine nucleotide-releasing protein (GNRP), which, like Ras1 and drk, is required for sevenless signaling. These results suggest that drk binds autophosphorylated receptor tyrosine kinases with its SH2 domain and the Sos GNRP through its SH3 domains, thereby coupling receptor tyrosine kinases to Ras activation. The conservation of these signaling proteins during evolution indicates that this is a general mechanism for linking tyrosine kinases to Ras.
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
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
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
Oncogenes and signal transduction
Cantley, L. C., Auger, K. R., Carpenter, C., Duckworth, B., Graziani, A., Kapeller, R., & Soltoff, S. (1991) · Cell · doi:10.1016/0092-8674(91)90639-g · Cited by 2,694
Tautz, D., & Pfeifle, C. (1989) · Chromosoma · doi:10.1007/bf00291041 · Cited by 2,523
Hunter, T., & Cooper, J. A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.004341 · Cited by 2,107
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
Koch, C. A., Anderson, D., Moran, M. F., Ellis, C., & Pawson, T. (1991) · Science · doi:10.1126/science.1708916 · Cited by 1,868
The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
Lowenstein, E. J., Daly, R. J., Batzer, A. G., Li, W., Margolis, B., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar-Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,631
A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
Pelicci, G., Lanfrancone, L., Grignani, F., McGlade, J., Cavallo, F., Forni, G., Nicoletti, I., Grignani, F., Pawson, T., & Giuseppe Pelicci, P. (1992) · Cell · doi:10.1016/0092-8674(92)90536-l · Cited by 1,326
Identification of a Ten-Amino Acid Proline-Rich SH3 Binding Site
Ren, R., Mayer, B. J., Cicchetti, P., & Baltimore, D. (1993) · Science · doi:10.1126/science.8438166 · Cited by 1,191
Drosophila: a laboratory manual
(1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90257-7 · Cited by 1,074
Cited by
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
Proteins regulating Ras and its relatives
Boguski, M. S., & McCormick, F. (1993) · Nature · doi:10.1038/366643a0 · Cited by 1,901
A Protein Interaction Map of Drosophila melanogaster
Giot, L., Bader, J. S., Brouwer, C., Chaudhuri, A., Kuang, B., Li, Y., Hao, Y. L., Ooi, C. E., Godwin, B., Vitols, E., et al. (2003) · Science · doi:10.1126/science.1090289 · Cited by 1,863
Signal Transduction through MAP Kinase Cascades
(1998) · Advances in Cancer Research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759
Mechanisms and functions of eph and ephrin signalling
Kullander, K., & Klein, R. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm856 · Cited by 1,156
Metadata
- Authors
- Olivier, J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1993-04-09
- Volume
- 73
- Issue
- 1
- Pages
- 179-191
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2073146277
- Cited by
- 537
- References
- 69
- FWCI
- 35.10
- Type
- journal article
- Language
- en
- Open access
- green
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: A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. https://app.cochat.ai/papers/10.1016/0092-8674(93)90170-u
- The paper
- Olivier, J. (1993). A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. Cell. https://doi.org/10.1016/0092-8674(93)90170-u
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.
