Zobrazeno 1 - 10
of 10
pro vyhledávání: '"G E Gilbert"'
Publikováno v:
Diseases of Aquatic Organisms. 121:173-188
The objective of this study was to assess the extent and describe the nature of a multi-species marine finfish and crustacean disease event that occurred in Gladstone Harbour, Australia, 2011-2012. Finfish were examined for this study in January to A
Publikováno v:
Vox sanguinis. 100(2)
Annexin V, the long established standard method of measuring phosphatidylserine (PS) exposure, is not the most suitable probe for the study of stored platelets because of calcium dependence and low sensitivity under 8% PS exposure. The aim of this st
Publikováno v:
Family medicine. 32(5)
Several experts have emphasized the need to respond to a patient's emotions as an essential component of effective medical interviewing. This study examined the relationship of faculty observers' scores of students' performance in standardized patien
Publikováno v:
Blood. 92(2)
von Willebrand factor (vWF) is a multimeric adhesive glycoprotein with one factor VIII binding site/subunit. Prior reports suggest that posttranslational modifications of vWF, including formation of N-terminal intersubunit disulfide bonds and subsequ
Publikováno v:
The Journal of biological chemistry. 268(12)
Factor VIII functions as a component of the tenase enzyme complex upon phospholipid membranes. Factor VIII binds to phosphatidylserine-containing membranes and apparently provides high affinity binding sites for factor IXa upon these membranes. We ha
Publikováno v:
The Journal of biological chemistry. 267(22)
Factor VIII functions in an enzyme complex upon the activated platelet membrane where phosphatidylserine exposure correlates with expression of receptors for factor VIII. To evaluate the specificity of phosphatidylserine-containing membrane binding s
Publikováno v:
The Journal of biological chemistry. 266(26)
Factor VIII is a cofactor in the tenase enzyme complex which assembles on the membrane of activated platelets. A critical step in tenase assembly is membrane binding of factor VIII. Platelet membrane factor VIII-binding sites were characterized by fl
Publikováno v:
The Journal of biological chemistry. 265(2)
Factor VIII, a protein cofactor involved in blood coagulation, functions in vitro on a phospholipid membrane surface to greatly increase the rate of factor X activation by factor IXa. Using gel filtration, rapid sedimentation, and resonance energy tr
Autor:
G. R. de Foliart, L. C. Bliss, S. C. Kendeigh, A. A. Lindsey, R. F. Daubenmire, H. G. Baker, F. E. Smith, Jean H. Langenheim, M. W. Weller, Bryon Blair, W. Hilsenhoff, James H. Zimmerman, O. L. Loucks, R. Horrall, F. Stearns, F. C. Evans, Katharina Lettau, G. E. Gilbert
Publikováno v:
BioScience. 17:712-714
Publikováno v:
Health physics. 55(3)