The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Integrins: dynamic scaffolds for adhesion and signaling in platelets
Abstract
The major platelet integrin, αIIbβ3, is required for platelet interactions with proteins in plasma and the extracellular matrices (ECMs) that are essential for platelet adhesion and aggregation during hemo stasis and arterial thrombosis. Lig and binding to αIIbβ3 is controlled by inside-out signals that modulate receptor conformation and clustering. In turn, ligand binding triggers outside-in signals through αIIbβ3 that, when disrupted, can cause a bleeding diathesis. In the past 5 years there has been an explosion of knowledge about the structure and function ofαIIbβ3 and the related integrin, αVβ3. These developments are discussed here, and current models of bidirectional αIIbβ3 signaling are presented as frameworks for future investigations. An understanding that αIIbβ3 functions as a dynamic molecular scaffold for extracellular and intracellular proteins has translated into diagnostic and therapeutic insights relevant to hematology and cardiovascular medicine, and further advances can be anticipated. (Blood. 2004;104:1606-1615)
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Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
Calderwood, D. A., Zent, R., Grant, R., Rees, D. J. G., Hynes, R. O., & Ginsberg, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28071 · Cited by 720
Platelets in inflammation and thrombosis
Wagner, D. D., & Burger, P. C. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000095974.95122.ec · Cited by 570 · cited 2×
“Portrayed were such structural features as (1) an IIb subunit composed of an approximately 120kDa heavy-chain disulfide bonded to an approximately 23-kDa light chain; (2) 4 IIb calcium-binding domains; (3) a small N-terminal cysteine-rich domain in 3 attached by a disulfide bond to “cysteine-rich repeats” within the b…”
BackgroundType Iγ phosphatidylinositol phosphate kinase targets and regulates focal adhesions
Ling, K., Doughman, R. L., Firestone, A. J., Bunce, M. W., & Anderson, R. A. (2002) · Nature · doi:10.1038/nature01082 · Cited by 443
Deficiency or inhibition of Gas6 causes platelet dysfunction and protects mice against thrombosis
Angelillo-Scherrer, A., de Frutos, P. G., Aparicio, C., Melis, E., Savi, P., Lupu, F., Arnout, J., Dewerchin, M., Hoylaerts, M. F., Herbert, J.-M., et al. (2001) · Nature Medicine · doi:10.1038/84667 · Cited by 441
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Signaling During Platelet Adhesion and Activation
Li, Z., Delaney, M. K., O'Brien, K. A., & Du, X. (2010) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.110.207522 · Cited by 911
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Metadata
- Authors
- Shattil, S. J., & Newman, P. J.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2004-09-15
- Volume
- 104
- Issue
- 6
- Pages
- 1606-1615
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2046737719
- Cited by
- 601
- References
- 5
- FWCI
- 19.51
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
