J
James A. Hoxie
Researcher at University of Pennsylvania
Publications - 233
Citations - 22591
James A. Hoxie is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Virus & Antibody. The author has an hindex of 84, co-authored 230 publications receiving 21851 citations. Previous affiliations of James A. Hoxie include Memorial Sloan Kettering Cancer Center & American Red Cross.
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Journal ArticleDOI
The HIV coreceptors CXCR4 and CCR5 are differentially expressed and regulated on human T lymphocytes
TL;DR: The largely reciprocal expression of CXCR4 and CCR5 among peripheral blood T cells implies distinct susceptibility of T cell subsets to viral entry by T cell line- Tropic versus macrophage-tropic strains during the course of HIV infection.
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Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation.
TL;DR: A murine monoclonal anti-platelet antibody is developed and characterized that binds to activated platelets, but not to unstimulated platelets and inhibits fibrinogen-mediated platelet aggregation.
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Detection of activated platelets in whole blood using activation- dependent monoclonal antibodies and flow cytometry
TL;DR: It is demonstrated that activated platelets can be reliably detected in whole blood using activation-dependent monoclonal antibodies and flow cytometry and may be useful to assess the degree of platelet activation and the efficacy of antiplatelet therapy in clinical disorders.
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CD4-Independent Infection by HIV-2 Is Mediated by Fusin/CXCR4
Michael J. Endres,Paul R. Clapham,Mark Marsh,Ména Ahuja,Julie D. Turner,Áine McKnight,Jill F Thomas,Beth Stoebenau-Haggarty,Sunny Choe,Patricia J. Vance,Timothy N. C. Wells,Christine A. Power,Shaheen S Sutterwala,Robert W. Doms,Nathaniel R. Landau,James A. Hoxie +15 more
TL;DR: The finding that one chemokine receptor can function as a primary viral receptor strongly suggests that the HIV envelope glycoprotein contains a binding site for these proteins and that differences in the affinity and/or the availability of this site can extend the host range of these viruses to include a number of CD4-negative cell types.
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Interactions of Mast Cell Tryptase with Thrombin Receptors and PAR-2
Marina Molino,Elliot S. Barnathan,Robert Numerof,James D. Clark,Mark Dreyer,Albana Cumashi,James A. Hoxie,Norman Schechter,Marilyn J. Woolkalis,Lawrence F. Brass +9 more
TL;DR: Tryptase is the first protease other than trypsin that has been shown to activate human PAR-2, and in contrast, although tryptase clearly activates thrombin receptors in COS-1 cells, it does not appear to cleave endogenous throm bin receptors in platelets or CHRF-288 cells.