Philip J Fay
Overview
Explore the profile of Philip J Fay including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
51
Citations
628
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Leong L, Sim D, Patel C, Tran K, Liu P, Ho E, et al.
Blood
. 2014 Oct;
125(2):392-8.
PMID: 25331117
An important negative regulator of factor VIIIa (FVIIIa) cofactor activity is A2 subunit dissociation. FVIII molecules with stabilized activity have been generated by elimination of charged residues at the A1-A2...
2.
Kosloski M, Shetty K, Wakabayashi H, Fay P, Balu-Iyer S
AAPS J
. 2014 Jun;
16(5):1038-45.
PMID: 24934295
Proteolytic cleavage of factor VIII (FVIII) to activated FVIIIa is required for participation in the coagulation cascade. The A2 domain is no longer covalently bound in the resulting activated heterotrimer...
3.
Wakabayashi H, Monaghan M, Fay P
J Biol Chem
. 2014 Apr;
289(20):14020-9.
PMID: 24692542
The factor VIII (FVIII) crystal structure suggests a possible bonding interaction of His(281) (A1 domain) with Ser(524) (A2 domain), although the resolution of the structure (∼4 Å) does not firmly...
4.
Griffiths A, Wintermute J, Newell-Caito J, Fay P
Biochemistry
. 2013 Oct;
52(45):8060-8.
PMID: 24128092
Factor Xa (FXa) proteolytically activates Factor VIII (FVIII) by cleaving P1 residues Arg(372), Arg(740), and Arg(1689). The Arg(372) site represents the rate-limiting step for procofactor activation, whereas cleavage at Arg(740)...
5.
Wakabayashi H, Fay P
J Biol Chem
. 2013 Sep;
288(43):31289-97.
PMID: 24030831
Factor VIII (FVIII) consists of a heavy chain (A1(a1)A2(a2)B domains) and light chain ((a3)A3C1C2 domains). To gain insights into a role of the FVIII C domains, we eliminated the C1...
6.
Wakabayashi H, Fay P
Biochemistry
. 2013 May;
52(22):3921-9.
PMID: 23659383
Factor (F)VIII consists of a heavy chain [A1(a1)A2(a2)B domains] and a light chain [(a3)A3C1C2 domains]. Several reports have shown significant changes in FVIII stability and/or activity following selected mutations at...
7.
Griffiths A, Rydkin I, Fay P
J Biol Chem
. 2013 Apr;
288(21):15057-64.
PMID: 23580639
Factor (F) VIIIa forms a number of contacts with FIXa in assembling the FXase enzyme complex. Surface plasmon resonance was used to examine the interaction between immobilized biotinylated active site-modified...
8.
Wakabayashi H, Fay P
Biochem J
. 2013 Mar;
452(2):293-301.
PMID: 23521092
F (Factor) VIIIa binds to phospholipid membranes during formation of the FXase complex. Free thiols from cysteine residues of isolated FVIIIa A1 and A2 subunits and the A3 domain of...
9.
Takeyama M, Wintermute J, Manithody C, Rezaie A, Fay P
Biochemistry
. 2013 Mar;
52(13):2228-35.
PMID: 23480827
Basic residues contained in the 39-, 60-, and 70-80-loops of activated protein C (APC) comprise an exosite that contributes to the binding and subsequent proteolytic inactivation of factor (F) VIIIa....
10.
Yada K, Nogami K, Wakabayashi H, Fay P, Shima M
Thromb Haemost
. 2013 Mar;
109(6):1007-15.
PMID: 23467620
The clinical severity in some patients with haemophilia A appears to be unrelated to the levels of factor (F)VIII activity (FVIII:C), but mechanisms are poorly understood. We have investigated a...