O
Oenick Marsha Denise Bale
Researcher at University of Rochester
Publications - 4
Citations - 201
Oenick Marsha Denise Bale is an academic researcher from University of Rochester. The author has contributed to research in topics: Ligand (biochemistry) & Cancer. The author has an hindex of 2, co-authored 4 publications receiving 174 citations. Previous affiliations of Oenick Marsha Denise Bale include Johnson & Johnson.
Papers
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Journal ArticleDOI
VEGF, PF4 and PDGF are elevated in platelets of colorectal cancer patients
Jon E. Peterson,David Zurakowski,Joseph E. Italiano,Joseph E. Italiano,Lea Vacca Michel,Lea Vacca Michel,Susan L. Connors,Oenick Marsha Denise Bale,Robert J. D'Amato,Giannoula Klement,Judah Folkman +10 more
TL;DR: Platelets sequester angiogenesis regulatory proteins which suggests an avenue for developing biomarkers to monitor disease and Multivariable logistic regression analysis indicated that PDGF, PF4 and VEGF were independent predictors of colorectal carcinoma and as a set provided statistically significant discrimination.
Journal ArticleDOI
Studies on fibrin polymerization and fibrin structure--a retrospective.
Patent
Immunoassay element containing a diaryl telluride compound to increase its stability
Carol Anne Decann,Logan Margaret Elizabeth,Oenick Marsha Denise Bale,Gary Louis Snodgrass,Roy Euegene Snoke +4 more
TL;DR: In this paper, a support bearing is used for assaying a ligand, comprising of a spreading zone, an enzyme labeled ligand or an enzyme-labeled receptor zone, and a receptor zone containing a fixed concentration of an immobilized receptor for the ligand and the labelled ligand when present.
Patent
Reduction in first slide bias and improved enzyme stability by the incorporation of diaryl tellurides in thin-film immunoassay elements
Logan Margaret Elizabeth,Carol Anne Decann,Oenick Marsha Denise Bale,Gary Louis Snodgrass,Roy Euegene Snoke +4 more
TL;DR: In this article, a support bearing is used for assaying a ligand, comprising of a spreading zone, an enzyme labeled ligand or an enzyme-labeled receptor zone, and a receptor zone containing a fixed concentration of an immobilized receptor for the ligand and the labelled ligand when present.