The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
The Extracellular Actin-Scavenger System and Actin Toxicity
Abstract
ACTIN is the most abundant protein in mammalian cells. Cell motility and change in the size and shape of cells depend on the ability of monomers of actin to polymerize to actin filaments. When actin is released from cells, however, its strong tendency to polymerize can become a liability, and the presence of filaments of actin in blood vessels can be fatal. Cell necrosis is associated with the release of actin in a variety of clinical situations, including hepatic necrosis, septic shock, the adult respiratory distress syndrome, and certain disorders of pregnancy. A newly described homeostatic mechanism, termed the actin-scavenger . . .
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Cites
Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults
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ACTIN AND ACTIN-BINDING PROTEINS. A CRITICAL EVALUATION OF MECHANISMS AND FUNCTIONS
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Actin polymerization and its regulation by proteins from nonmuscle cells.
Korn, E. D. (1982) · Physiological Reviews · doi:10.1152/physrev.1982.62.2.672 · Cited by 739
Kwiatkowski, D. J., Stossel, T. P., Orkin, S. H., Mole, J. E., Coltens, H. R., & Yin, H. L. (1986) · Nature · doi:10.1038/323455a0 · Cited by 478
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Group-specific component (Gc) proteins bind vitamin D and 25-hydroxyvitamin D.
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Thymosin β4 and Fx, an actin-sequestering peptide, are indistinguishable
Safer, D., Elzinga, M., & Nachmias, V. T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64278-8 · Cited by 353
Actin: protein structure and filament dynamics.
Carlier, M. F. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52391-7 · Cited by 315
Enhanced Motility in NIH 3T3 Fibroblasts That Overexpress Gelsolin
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Dominguez, R., & Holmes, K. C. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155359 · Cited by 1,211
Traction Force Microscopy of Migrating Normal and H-ras Transformed 3T3 Fibroblasts
Munevar, S., Wang, Y.-L., & Dembo, M. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76145-0 · Cited by 527
Biological and clinical aspects of the vitamin D binding protein (Gc-globulin) and its polymorphism
Speeckaert, M., Huang, G., Delanghe, J. R., & Taes, Y. E. C. (2006) · Clinica Chimica Acta · doi:10.1016/j.cca.2006.03.011 · Cited by 480
Vitamin D Binding Protein: A Historic Overview
Bouillon, R., Schuit, F., Antonio, L., & Rastinejad, F. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00910 · Cited by 316
Cauwe, B., & Opdenakker, G. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.501783 · Cited by 299
Metadata
- Authors
- Epstein, F. H., Lee, W. M., & Galbraith, R. M.
- Venue
- New England Journal of Medicine
- Publisher
- Massachusetts Medical Society
- Published
- 1992-05-14
- Volume
- 326
- Issue
- 20
- Pages
- 1335-1341
- ISSN
- 0028-4793 (ISSN-L)
- 1533-4406
- OpenAlex
- W2069521331
- Cited by
- 373
- References
- 50
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- closed
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- Epstein, F. H., Lee, W. M., & Galbraith, R. M. (1992). The Extracellular Actin-Scavenger System and Actin Toxicity. New England Journal of Medicine. https://doi.org/10.1056/nejm199205143262006
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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.
