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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
Accumulation of Tissue Factor into Developing Thrombi In Vivo Is Dependent upon Microparticle P-Selectin Glycoprotein Ligand 1 and Platelet P-Selectin
Shahrokh Falati,Qingde Liu,Peter L. Gross,Glenn Merrill-Skoloff,Janet Ing-Yuh Chou,Erik Vandendries,Alessandro Celi,Kevin Croce,Barbara C. Furie,Bruce Furie +9 more
TL;DR: It is proposed that PSGL-1 plays a role in blood coagulation in addition to its known role in leukocyte trafficking by examining thrombus formation in the microcirculation of wild-type and genetically altered mice by real-time in vivo microscopy.
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Real-time in vivo imaging of platelets, tissue factor and fibrin during arterial thrombus formation in the mouse.
TL;DR: This system provides high-speed, near-simultaneous acquisition of images of multiple fluorescent probes and of a brightfield channel that observed platelet deposition, tissue factor accumulation and fibrin generation after laser-induced endothelial injury in a single developing thrombus.
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PADGEM (GMP140) is a component of Weibel-Palade bodies of human endothelial cells
TL;DR: In endothelial cells treated with secretagogues that stimulate vWf release the elongated structures positive for PADGEM disappeared, and this observation extends the parallels between Weibel-Palade bodies and alpha-granules and suggests a possible functional association between vWF and P ADGEM.
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Vitamin K-Dependent Biosynthesis of γ-Carboxyglutamic Acid
TL;DR: VITAMin K, an essential vitamin, is a cofactor for a single known enzymatic reaction: the conversion of glutamic acid to γ-carboxyglutamic acid in vitamin K-dependent proteins during their biosynthesis.
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Localization of labile posttranslational modifications by electron capture dissociation: The case of γ-carboxyglutamic acid
Neil L. Kelleher,Roman A. Zubarev,Kristine Bush,Bruce Furie,Barbara C. Furie,Fred W. McLafferty,Christopher T. Walsh +6 more
TL;DR: ECD is a unique complement to conventional methods for MS/MS, causing less undesirable loss of side-chain functionalities as well as more desirable backbone cleavages.