Publications by authors named "Mallorie Boron"

Thrombomodulin (TM) is a type-I transmembrane protein that is mainly expressed on endothelial cells and plays important roles in many biological processes. Circulating TM of different forms are also present in biofluids, such as blood and urine. Soluble TM (sTM), comprised of several domains of TM, is the major circulating TM which is generated by either enzymatic or chemical cleavage of the intact protein under different conditions.

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The use of cadmium to produce inexpensive jewelry has recently been documented. Governments have adopted varying standards, with US states focused on either total cadmium content or extractable cadmium from children's jewelry, while the European Union has adopted a limit of 100 mg/kg cadmium for all jewelry. This study evaluated 80 items purchased at a discount jewelry store.

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Thrombomodulin (TM) is an endothelial cell membrane protein that plays essential roles in controlling vascular haemostatic balance. The 4, 5, 6 EGF-like domain of TM (TM) has cofactor activity for thrombin binding and subsequently protein C activation. Therefore, recombinant TM is a promising anticoagulant candidate but has a very short half-life.

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Introduction of selectively chemical reactive groups at the cell surface enables site-specific cell surface labeling and modification opportunity, thus facilitating the capability to study the cell surface molecular structure and function and the molecular mechanism it underlies. Further, it offers the opportunity to change or improve a cell's functionality for interest of choice. In this study, two chemical reactive anchor lipids, phosphatidylethanolamine-poly(ethylene glycol)-dibenzocyclooctyne (DSPE-PEG-DBCO) and cholesterol-PEG-dibenzocyclooctyne (CHOL-PEG-DBCO) were synthesized and their potential application for cell surface re-engineering via lipid fusion were assessed with RAW 264.

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