S. Hung

A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin

Nolan H. Sigal, N. Sigal, J. Siekierka, 1989, Nature.

FK-506, a potent novel immunosuppressive agent, binds to a cytosolic protein which is distinct from the cyclosporin A-binding protein, cyclophilin.

N. Sigal, J. Siekierka, S. Hung, 1989, Journal of immunology.

Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex.

N. Sigal, R. Kincaid, M. Martin, 1992, The Journal of biological chemistry.

The Mechanism of Action of FK‐506 and Cyclosporin A

N. Sigal, G. Wiederrecht, S. Hung, 1993, Annals of the New York Academy of Sciences.

FKBP, the binding protein for the immunosuppressive drug, FK-506, is not an inhibitor of protein kinase C activity.

N. Sigal, G. Wiederrecht, J. Siekierka, 1991, Biochemical and biophysical research communications.

Hybrid baculovirus-mediated prolonged hemagglutinin expression and secretion in vivo enhances the vaccine efficacy

Yu-Chen Hu, S. Hung, M. Cheng, 2018, Journal of the Taiwan Institute of Chemical Engineers.

Alkyl ether derivatives of the FK-506 related, immunosuppressive macrolide L-683,742 (C31-O-desmethyl ascomycin)

F. Dumont, J. Siekierka, S. Hung, 1994 .

The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase.

N. Sigal, H. Greulich, G. Wiederrecht, 1990, The Journal of biological chemistry.

Inhibition of calcineurin by a novel FK-506-binding protein.

P. Griffin, J. Weidner, J. Leszyk, 1994, The Journal of biological chemistry.