The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Molecular mechanisms of fibrinolysis
Abstract
Summary: The molecular mechanisms that finely co‐ordinate fibrin formation and fibrinolysis are now well defined. The structure and function of all major fibrinolytic proteins, which include serine proteases, their inhibitors, activators and receptors, have been characterized. Measurements of real time, dynamic molecular interactions during fibrinolysis of whole blood clots can now be carried out in vitro. The development of gene‐targeted mice deficient in one or more fibrinolytic protein(s) has demonstrated expected and unexpected roles for these proteins in both intravascular and extravascular settings. In addition, genetic analysis of human deficiency syndromes has revealed specific mutations that result in human disorders that are reflective of either fibrinolytic deficiency or excess. Elucidation of the fine control of fibrinolysis under different physiological and pathological haemostatic states will undoubtedly lead to novel therapeutic interventions. Here, we review the fundamental features of intravascular plasmin generation, and consider the major clinical syndromes resulting from abnormalities in fibrinolysis.
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Cites
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BackgroundNeuronal Death in the Hippocampus Is Promoted by Plasmin-Catalyzed Degradation of Laminin
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Cited by
Pretorius, E., Vlok, M., Venter, C., Bezuidenhout, J. A., Laubscher, G. J., Steenkamp, J., & Kell, D. B. (2021) · Cardiovascular Diabetology · doi:10.1186/s12933-021-01359-7 · Cited by 518
Inflammation and Coagulation in Inflammatory Bowel Disease: The Clot Thickens
Danese, S., Papa, A., Saibeni, S., Repici, A., Malesci, A., & Vecchi, M. (2007) · The American Journal of Gastroenterology · doi:10.1111/j.1572-0241.2006.00943.x · Cited by 384
Breaking boundaries—coagulation and fibrinolysis at the neurovascular interface
Bardehle, S., Rafalski, V. A., & Akassoglou, K. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00354 · Cited by 76
González-Miguel, J., Morchón, R., Mellado, I., Carretón, E., Montoya-Alonso, J. A., & Simón, F. (2012) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2011.10.010 · Cited by 55
Zheng, Z., Nakamura, K., Gershbaum, S., Wang, X., Thomas, S., Bessler, M., Schrope, B., Krikhely, A., Liu, R.-M., Ozcan, L., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci135919 · Cited by 43
Metadata
- Authors
- Cesarman‐Maus, G., & Hajjar, K. A.
- Venue
- British Journal of Haematology
- Publisher
- Wiley
- Published
- 2005-04-19
- Volume
- 129
- Issue
- 3
- Pages
- 307-321
- ISSN
- 0007-1048 (ISSN-L)
- 1365-2141
- OpenAlex
- W2123811384
- Cited by
- 748
- References
- 5
- FWCI
- 11.24
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
