Structurally and Functionally Distinct Ca2+ Binding Sites in the gamma-Carboxyglutamic Acid-Containing Domain of Factor VIIa
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.293_c.x/fullpdf
Reference48 articles.
1. Structural requirements for Ca2+ binding to the gamma-carboxyglutamic acid and epidermal growth factor-like regions of factor IX. Studies using intact domains isolated from controlled proteolytic digests of bovine factor IX
2. Human leukocyte granule elastase: rapid isolation and characterization
3. Prothrombin requires two sequential metal-dependent conformational transitions to bind phospholipid. Conformation-specific antibodies directed against the phospholipid-binding site on prothrombin.
4. Cooperative Interaction of Divalent Metal Ions, Substrate, and Tissue Factor with Factor VIIa
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2. Structural modulation of factor VIIa by full-length tissue factor (TF1-263): implication of novel interactions between EGF2 domain and TF;Journal of Biomolecular Structure and Dynamics;2017-02-17
3. Calcium‐Binding Proteins;eLS;2016-02-15
4. Structure–Function Relationship of the Interaction between Tissue Factor and Factor VIIa;Seminars in Thrombosis and Hemostasis;2015-09-26
5. Acidity and metal (Mg 2+ , Ca 2+ , Zn 2+ ) affinity of l -γ-carboxyglutamic acid and its peptide analog;Chemical Physics Letters;2014-10
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