A5066772511- Hemophilia Treatment and Research
- Blood Coagulation and Thrombosis Mechanisms
- Platelet Disorders and Treatments
- Cell Adhesion Molecules Research
- Coagulation, Bradykinin, Polyphosphates, and Angioedema
- Monoclonal and Polyclonal Antibodies Research
- Hemostasis and retained surgical items
- Myeloproliferative Neoplasms: Diagnosis and Treatment
- Blood properties and coagulation
- Chronic Myeloid Leukemia Treatments
- Heparin-Induced Thrombocytopenia and Thrombosis
- Genomics and Rare Diseases
- Protease and Inhibitor Mechanisms
- Cystic Fibrosis Research Advances
- Virus-based gene therapy research
- Wnt/β-catenin signaling in development and cancer
- Cancer-related gene regulation
- Gene expression and cancer classification
- Protein purification and stability
- Connexins and lens biology
Bayer (United States)
2011-2018
Thomas Jefferson University
2000
Scripps Research Institute
1995-1996
Scripps Institution of Oceanography
1995
Torrey Pines Institute For Molecular Studies
1995
Scripps (United States)
1995
University of Vermont
1992-1994
Summary Patients with haemophilia ( PWH ) are usually monitored by the one‐stage activated partial thromboplastin time (aPTT) factor VIII (FVIII) assay. Different aPTT activators may affect clotting CT and FVIII:C levels in patients treated PEGylated FVIII. To evaluate characteristics of FVIII (BAY 94‐9027) various assays, to identify suitable reagents for monitoring BAY 94‐9027 during treatment , World Health Organization WHO 8th standards ‐8) were spiked into pooled individual severe A...
Factor VIII (FVIII) replacement is standard of care for patients with hemophilia A (HemA); however, patient response does not always correlate FVIII levels. We hypothesize this may be in part due to the physical properties clots and contributions fibrin, platelets, erythrocytes, which important hemostasis.To understand how contributes effective hemostasis terms clot structure mechanical properties.In vitro HemA human plasma or whole blood were analyzed using turbidity waveform analysis,...
ABSTRACT pp125FAK (focal adhesion kinase) a protein tyrosine kinase that may mediate cellular responses to adhesion, is activated and tyrosine-phosphorylated when platelets adhere fibrinogen via the integrin, αIIbβ3. To determine whether either of cytoplasmic tails αIIbβ3 regulates FAK phosphorylation, CHO cells were stably transfected with or various tail truncation mutants. Cells expressing wild-type lacked COOH-terminal 13 18 residues 20 residue αIIb adhered spread on an anti-αIIb...
PEGylation of B-domain deleted factor VIII (PEG-FVIII-BDD) prolongs the half-life molecule by approximately twofold in animals (Mei et al., Blood 2010; 116: 270). To investigate role von Willebrand (vWF) catabolism PEG-FVIII-BDD vivo, a FVIII-BDD mutant (F8V), which is incapable binding vWF, was generated deleting vWF-binding region a3 domain FVIIII-BDD. F8V expressed, purified and PEGylated site-specific conjugation. The biochemical biological properties (PEG-F8V) were evaluated vitro vivo....
Discrepancies in the measurement of modified factor VIII (FVIII) products have been recognized, highlighting need for adjustments clinical laboratory practices to ensure effective monitoring patients treated with these products, particularly using one-stage (activated partial thromboplastin time [aPTT]) assay.To assess ability laboratories measure activity BAY 94-9027, a PEGylated extended half-life FVIII product, routine (predominantly one-stage) assays METHODS: Blinded samples...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe thrombin high-affinity binding site on platelets is a negative regulator of thrombin-induced platelet activation. Structure-function studies using two mutant thrombins, Quick I and IILilley Leong, Ruth A. Henriksen, John C. Kermode, Susan E. Rittenhouse, Paula B. TracyCite this: Biochemistry 1992, 31, 9, 2567–2576Publication Date (Print):March 10, 1992Publication History Published online1 May 2002Published inissue 10 March...
Prior studies using the mutant thrombin, thrombin Quick I, indicate that this protease induces maximum platelet aggregation and intraplatelet [Ca2+] fluxes at agonist concentrations where dissociable, equilibrium binding is undetectable led to conclusion interaction with its receptor best described kinetically by formation of an enzyme-substrate complex. This was substantiated further in present demonstrating both I mimicked peptide induction activation-dependent events required for...