Year |
Citation |
Score |
2013 |
Qu X, Afelik S, Jensen JN, Bukys MA, Kobberup S, Schmerr M, Xiao F, Nyeng P, Veronica Albertoni M, Grapin-Botton A, Jensen J. Notch-mediated post-translational control of Ngn3 protein stability regulates pancreatic patterning and cell fate commitment. Developmental Biology. 376: 1-12. PMID 23370147 DOI: 10.1016/J.Ydbio.2013.01.021 |
0.301 |
|
2010 |
Hirbawi J, Vaughn JL, Bukys MA, Vos HL, Kalafatis M. Contribution of amino acid region 659-663 of Factor Va heavy chain to the activity of factor Xa within prothrombinase . Biochemistry. 49: 8520-34. PMID 20722419 DOI: 10.1021/Bi101097T |
0.802 |
|
2010 |
Vaughn JL, Hirbawi J, Bukys MA, Kalafatis M. Role of the N-Terminal Amino Acid Region of Factor Va Light Chain In Prothrombinase Assembly and Function. Blood. 116: 1127-1127. DOI: 10.1182/Blood.V116.21.1127.1127 |
0.771 |
|
2008 |
Barhoover MA, Orban T, Bukys MA, Kalafatis M. Cooperative regulation of the activity of factor Xa within prothrombinase by discrete amino acid regions from factor Va heavy chain. Biochemistry. 47: 12835-43. PMID 18991406 DOI: 10.1021/Bi801241R |
0.805 |
|
2008 |
Hirbawi J, Bukys MA, Barhoover MA, Erdogan E, Kalafatis M. Role of the acidic hirudin-like COOH-terminal amino acid region of factor Va heavy chain in the enhanced function of prothrombinase. Biochemistry. 47: 7963-74. PMID 18590276 DOI: 10.1021/Bi800593K |
0.822 |
|
2008 |
Barhoover MA, Orban T, Beck DO, Bukys MA, Kalafatis M. Contribution of amino acid region 334-335 from factor Va heavy chain to the catalytic efficiency of prothrombinase. Biochemistry. 47: 6840-50. PMID 18537263 DOI: 10.1021/Bi800057R |
0.802 |
|
2008 |
Bukys MA, Orban T, Kim PY, Nesheim ME, Kalafatis M. The interaction of fragment 1 of prothrombin with the membrane surface is a prerequisite for optimum expression of factor Va cofactor activity within prothrombinase. Thrombosis and Haemostasis. 99: 511-22. PMID 18327399 DOI: 10.1160/Th07-08-0532 |
0.788 |
|
2008 |
Erdogan E, Bukys MA, Kalafatis M. The contribution of amino acid residues 1508-1515 of factor V to light chain generation. Journal of Thrombosis and Haemostasis : Jth. 6: 118-24. PMID 17944989 DOI: 10.1111/J.1538-7836.2007.02803.X |
0.807 |
|
2008 |
Kalafatis M, Hirbawi J, Barhoover MA, Bukys MA. The Effect of Factor Va on Prothrombinase Function Blood. 112: 1020-1020. DOI: 10.1182/Blood.V112.11.1020.1020 |
0.812 |
|
2007 |
Erdogan E, Bukys MA, Orfeo T, Mann KG, Kalafatis M. Identification of an inactivating cleavage site for alpha-thrombin on the heavy chain of factor Va. Thrombosis and Haemostasis. 98: 998-1006. PMID 18000604 DOI: 10.1160/Th07-06-0431 |
0.766 |
|
2007 |
Bukys MA, Orban T, Kim PY, Nesheim ME, Kalafatis M. Factor Va Cofactor Activity Is Dependent on the Interaction of Prothrombin with the Membrane Surface. Blood. 110: 2702-2702. DOI: 10.1182/Blood.V110.11.2702.2702 |
0.793 |
|
2007 |
Kalafatis M, Bukys MA, Hirbawi J, Kim PY, Barhoover MA, Nesheim ME. Understanding the Factor Va Cofactor Effect within Prothrombinase. Blood. 110: 2700-2700. DOI: 10.1182/Blood.V110.11.2700.2700 |
0.806 |
|
2007 |
Hirbawi J, Bukys MA, Barhoover MA, Kalafatis M. The Acidic COOH-Terminal Region of Factor Va Heavy Chain Controls the Rate of Prothrombin Activation by Prothrombinase. Blood. 110: 1745-1745. DOI: 10.1182/Blood.V110.11.1745.1745 |
0.832 |
|
2006 |
Bukys MA, Kim PY, Nesheim ME, Kalafatis M. A control switch for prothrombinase: characterization of a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain that regulates the rate and pathway for prothrombin activation. The Journal of Biological Chemistry. 281: 39194-204. PMID 17020886 DOI: 10.1074/Jbc.M604482200 |
0.754 |
|
2006 |
Bukys MA, Orban T, Kim PY, Beck DO, Nesheim ME, Kalafatis M. The structural integrity of anion binding exosite I of thrombin is required and sufficient for timely cleavage and activation of factor V and factor VIII. The Journal of Biological Chemistry. 281: 18569-80. PMID 16624813 DOI: 10.1074/Jbc.M600752200 |
0.788 |
|
2006 |
Bukys MA, Simioni P, Smith K, Spiezia L, Kalafatis M. Isolation and Characterization of an Antifactor VIII Antibody from a Patient with Acquired Hemophilia A and a Severe Hemorrhagic Syndrome. Blood. 108: 4073-4073. DOI: 10.1182/Blood.V108.11.4073.4073 |
0.642 |
|
2006 |
Erdogan E, Bukys MA, Orfeo T, Mann KG, Kalafatis M. Cleavage of Factor Va Heavy Chain at Arg643 by Thrombin Partially Inactivates the Cofactor. Blood. 108: 1703-1703. DOI: 10.1182/Blood.V108.11.1703.1703 |
0.84 |
|
2006 |
Bukys MA, Kim PY, Nesheim ME, Kalafatis M. Controlling the Pathway for Prothrombin Activation by Prothrombinase. Blood. 108: 1695-1695. DOI: 10.1182/Blood.V108.11.1695.1695 |
0.78 |
|
2005 |
Bukys MA, Blum MA, Kim PY, Brufatto N, Nesheim ME, Kalafatis M. Incorporation of factor Va into prothrombinase is required for coordinated cleavage of prothrombin by factor Xa. The Journal of Biological Chemistry. 280: 27393-401. PMID 15897196 DOI: 10.1074/Jbc.M503435200 |
0.765 |
|
2005 |
Bukys MA, Orban T, Kim PY, Nesheim ME, Kalafatis M. Exposure of Anion Binding Exosite I of Thrombin Is Required and Sufficient for Timely Cleavage and Activation of Factor V and Factor VIII. Blood. 106: 1951-1951. DOI: 10.1182/Blood.V106.11.1951.1951 |
0.781 |
|
2005 |
Hirbawi J, Blum MA, Bukys MA, Orban T, Kalafatis M. Evidence That the COOH-Terminal Region of Factor Va Heavy Chain Is Involved in the Regulation of Prothrombinase Activity. Blood. 106: 1025-1025. DOI: 10.1182/Blood.V106.11.1025.1025 |
0.807 |
|
2004 |
Beck DO, Bukys MA, Singh LS, Szabo KA, Kalafatis M. The contribution of amino acid region ASP695-TYR698 of factor V to procofactor activation and factor Va function. The Journal of Biological Chemistry. 279: 3084-95. PMID 14559913 DOI: 10.1074/Jbc.M306850200 |
0.786 |
|
2004 |
Bukys MA, Kim P, Blum MA, Nesheim ME, Kalafatis M. Cofactor Directed Catalysis. Blood. 104: 1715-1715. DOI: 10.1182/Blood.V104.11.1715.1715 |
0.737 |
|
2003 |
Singh LS, Bukys MA, Beck DO, Kalafatis M. Amino acids Glu323, Tyr324, Glu330, and Val331 of factor Va heavy chain are essential for expression of cofactor activity. The Journal of Biological Chemistry. 278: 28335-45. PMID 12738785 DOI: 10.1074/Jbc.M300233200 |
0.773 |
|
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