Search Results - "Lupisella, John A."

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    Formyl peptide receptor 2 and heart disease by Lupisella, John A., Shirude, Pravin S., Wurtz, Nicholas R., Garcia, Ricardo A.

    Published in Seminars in immunology (01-01-2022)
    “…Formyl peptide receptor type 2 (FPR2) regulates the initiation and resolution phases of the inflammatory response. In the setting of heart injury and disease,…”
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    Inhibition of disease progression by a novel retinoid antagonist in animal models of arthritis by BEEHLER, Blake C, HEI, Yong-Jiang, CHEN, Simon, LUPISELLA, John A, OSTROWSKI, Jacek, STARRETT, John E, TORTOLANI, David, TRAMPOSCH, Kenneth M, RECZEK, Peter R

    Published in Journal of rheumatology (01-02-2003)
    “…OBJECTIVE: To investigate the usefulness of a novel retinoic acid receptor (RAR) antagonist (BMS-189453) in animal models of arthritis. METHODS: BMS-189453 was…”
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    Ligand-induced Conformational Changes in the Human Retinoic Acid Receptor γ Detected Using Monoclonal Antibodies by Joyce E. Driscoll, Carrie L. Seachord, John A. Lupisella, Richard P. Darveau, Peter R. Reczek

    Published in The Journal of biological chemistry (20-09-1996)
    “…The mechanism by which the naturally occurring ligand for a nuclear hormone receptor regulates transcription remains largely unknown. One approach combines the…”
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    The Ligand Binding Domain of the Human Retinoic Acid Receptor γ Is Predominantly α-Helical with a Trp Residue in the Ligand Binding Site (∗) by Lupisella, John A., Driscoll, Joyce E., Metzler, William J., Reczek, Peter R.

    Published in The Journal of biological chemistry (20-10-1995)
    “…Retinoic acid exerts its many biological effects by interaction with a nuclear protein, the retinoic acid receptor (RAR). The details of this interaction are…”
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    The Ligand Binding Domain of the Human Retinoic Acid Receptor Is Predominantly -Helical with a Trp Residue in the Ligand Binding Site by John A. Lupisella, Joyce E. Driscoll, William J. Metzler, Peter R. Reczek

    Published in The Journal of biological chemistry (20-10-1995)
    “…Retinoic acid exerts its many biological effects by interaction with a nuclear protein, the retinoic acid receptor (RAR). The details of this interaction are…”
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    Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3 by SANDBAKEN, M. G, KUPISELLA, J. A, DIDOMENICO, B, CHAKRABURTTY, K

    Published in The Journal of biological chemistry (15-09-1990)
    “…The yeast translational elongation factor 3 (EF-3) stimulates EF-1 alpha-dependent binding of aminoacyl-tRNA by the ribosome. The requirement for EF-3 is…”
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