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Barbara C. Furie
Researcher at Beth Israel Deaconess Medical Center
Publications - 135
Citations - 9851
Barbara C. Furie is an academic researcher from Beth Israel Deaconess Medical Center. The author has contributed to research in topics: Thrombus & Platelet. The author has an hindex of 49, co-authored 135 publications receiving 9397 citations. Previous affiliations of Barbara C. Furie include Harvard University & Icahn School of Medicine at Mount Sinai.
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Journal ArticleDOI
Localization of the affinity peptide-substrate inactivator site on recombinant vitamin K-dependent carboxylase.
Athan Kuliopulos,Noele P. Nelson,M. Yamada,Christopher T. Walsh,Bruce Furie,Barbara C. Furie,D A Roth +6 more
TL;DR: The inactivated His6-carboxylase-Ac-FLEEL-125I-Y, purified under denaturing conditions by Ni-chelation chromatography followed by preparative polyacrylamide gel electrophoresis, was subjected to proteolytic digestions with either Glu-C or Lys-C endoproteinases.
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The Gla Domain of Factor IXa Binds to Factor VIIIa in the Tenase Complex
TL;DR: Results suggest that the factor IXa Gla domain contacts factor VIIIa in the tenase complex through a contact site that includes phenylalanine 25 and perhaps valine 46.
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The Gla Domain of Human Prothrombin Has a Binding Site for Factor Va
TL;DR: Results indicate that the N-terminal Gla domain of human prothrombin is a functional unit that has a binding site for factor Va, which is important for interaction of the substrate with the pro thirdrombinase complex.
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Structure determination of two conotoxins from Conus textile by a combination of matrix-assisted laser desorption/ionization time-of-flight and electrospray ionization mass spectrometry and biochemical methods.
Dário E. Kalume,Dário E. Kalume,Johan Stenflo,Johan Stenflo,Eva Czerwiec,Eva Czerwiec,Björn Hambe,Barbara C. Furie,Barbara C. Furie,Bruce Furie,Bruce Furie,Peter Roepstorff +11 more
TL;DR: Two highly modified conotoxins from the mollusc Conus textile, epsilon-TxIX and Gla(1)-TxVI, were characterized by matrix-assisted laser desorption/ionization and electrospray mass spectrometry and also by electrosPRay ionization tandem and triple mass Spectrometry in combination with enzymatic cleavage and chemical modification reactions.
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Rapid phosphorylation and selective dephosphorylation of P-selectin accompanies platelet activation
TL;DR: The rapid phosphorylation and selective dephosphorylation of specific amino acids in P- selectin following platelet activation may be important for P-selectin function and signal transduction within platelets.