Philip J. Fay
Affiliations: | University of Rochester, Rochester, NY |
Area:
BiochemistryGoogle:
"Philip J. Fay"Bio:
(1953 - 2014)
https://www.urmc.rochester.edu/biochemistry-biophysics/news.aspx?start=01-01-2014&end=12-31-2014
https://www.urmc.rochester.edu/MediaLibraries/URMCMedia/biochemistry-biophysics/documents/FayObitJTH12697.pdf
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Children
Sign in to add traineeCharles K. Ansong | grad student | 2006 | Rochester |
Fatbardha Varfaj | grad student | 2007 | Rochester |
Yi-Jen Chiu | grad student | 2008 | Rochester |
Jennifer L. Newell | grad student | 2009 | Rochester |
Jennifer P. DeAngelis | grad student | 2012 | Rochester |
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Publications
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Monaghan M, Wakabayashi H, Griffiths AE, et al. (2016) Stabilizing Interactions between D666-S1787 and T657-Y1792 at the A2-A3 Interface Support Factor VIIIa Stability in the Blood Clotting Pathway. Journal of Thrombosis and Haemostasis : Jth |
Leong L, Sim D, Patel C, et al. (2015) Noncovalent stabilization of the factor VIII A2 domain enhances efficacy in hemophilia A mouse vascular injury models. Blood. 125: 392-8 |
Kosloski MP, Shetty KA, Wakabayashi H, et al. (2014) Effects of replacement of factor VIII amino acids Asp519 and Glu665 with Val on plasma survival and efficacy in vivo. The Aaps Journal. 16: 1038-45 |
Monaghan M, Wakabayashi H, Griffiths A, et al. (2014) Enhanced factor VIIIa stability of A2 domain interface variants results from an increased apparent affinity for the A2 subunit. Results from an increased apparent affinity for the A2 subunit. Thrombosis and Haemostasis. 112: 495-502 |
Wakabayashi H, Monaghan M, Fay PJ. (2014) Cofactor activity in factor VIIIa of the blood clotting pathway is stabilized by an interdomain bond between His281 and Ser524 formed in factor VIII. The Journal of Biological Chemistry. 289: 14020-9 |
Wakabayashi H, Wintermute JM, Fay PJ. (2014) Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa. Thrombosis and Haemostasis. 112: 43-52 |
Griffiths AE, Wintermute J, Newell-Caito JL, et al. (2013) Residues flanking scissile bonds in Factor VIII modulate rates of cleavage and proteolytic activation catalyzed by Factor Xa. Biochemistry. 52: 8060-8 |
Wakabayashi H, Fay PJ. (2013) Replacing the factor VIII C1 domain with a second C2 domain reduces factor VIII stability and affinity for factor IXa. The Journal of Biological Chemistry. 288: 31289-97 |
Wakabayashi H, Fay PJ. (2013) Modification of interdomain interfaces within the A3C1C2 subunit of factor VIII affects its stability and activity. Biochemistry. 52: 3921-9 |
Griffiths AE, Rydkin I, Fay PJ. (2013) Factor VIIIa A2 subunit shows a high affinity interaction with factor IXa: contribution of A2 subunit residues 707-714 to the interaction with factor IXa. The Journal of Biological Chemistry. 288: 15057-64 |