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Critical Reviews™ in Eukaryotic Gene Expression

Published 6 issues per year

ISSN Print: 1045-4403

ISSN Online: 2162-6502

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.6 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.2 The Immediacy Index is the average number of times an article is cited in the year it is published. The journal Immediacy Index indicates how quickly articles in a journal are cited. Immediacy Index: 0.3 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00058 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.33 SJR: 0.345 SNIP: 0.46 CiteScore™:: 2.5 H-Index: 67

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Contributions of Gla and EGF-Like Domains to the Function of Vitamin K-Dependent Coagulation Factors

Volume 9, Issue 1, 1999, pp. 59-88
DOI: 10.1615/CritRevEukaryotGeneExpr.v9.i1.50
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ABSTRACT

Blood coagulation is a response to vascular injury leading to the activation of platelets and coagulation factors with the ultimate formation of a fibrin plug. Several coagulation factors are zymogens of serine proteases that require vitamin K for normal biosynthesis. The active forms of these proteases and their cofactors form membrane-bound macromolecular complexes. In the final step prothrombin is activated to thrombin by active factor X in complex with its cofactor, factor V. Thrombin then cleaves designated peptide bonds in fibrinogen, resulting in the formation of fibrin monomers that polymerize to insoluble fibrin strands. This process is regulated by an anticoagulant counterpart, the so-called protein C anticoagulant system. Balance between the two systems is crucial to avoid bleeding on the one hand and thrombosis on the other. The coagulation and anticoagulation proteases, factors VII, IX, and X, and protein C, have a common domain structure with an N-terminal γ-carboxyglutamic acid (Gla)-containing domain that is followed by two domains that are homologous to the epidermal growth factor (EGF), whereas the C-terminal half of each protein is occupied by a trypsin-like serine protease domain. Prothrombin also has an N-terminal Gla domain and a C-terminal serine protease domain, but they are separated by two so-called kringle domains rather than EGF-like domains. Finally, the vitamin K-dependent cofactor protein S has one domain with thrombin-sensitive bonds and four EGF-like domains in tandem between the Gla domain and a C-terminal domain that is homologous to plasma steroid hormone-binding proteins. The N-terminal noncatalytic Gla and EGF-like domains that provide the coagulation serine proteases with unique properties, such as affinity for certain biological membranes, and also mediate protein-protein interactions, are the subject of this review.

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