Richard N. Sifers, Ph.D.
Department of Pathology and Immunology
- Ph.D., University of Oklahoma Health Sciences Center
- Postdoctoral, Baylor College of Medicine
- Post-translational checkpoints
- ER-associated glycoprotein degradation
- Sifers RN. The underlying clockwork mechanics of a biosynthetic checkpoint. ASBMB Today. March 2007, pp. 22-3.
- Wu Y, Termine DJ, Swulius MT, Moremen KW, Sifers RN. Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis. J Biol Chem. 2007. 282:4841-9.
- Mast SW, Diekman K, Davis AW, Karaveg K, Sifers RN, Moremen KW. Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. Glycobiology. 2005. 15:421-36.
- Termine D, Wu Y, Liu Y, Sifers RN. Alpha1-antitrypsin as model to assess glycan function in endoplasmic reticulum. Methods. 2005. 35(4):348-53.
- Sifers RN. Insights into checkpoint capacity. Nature Struct & Mol Biol. 2004. 11:108-9.
- Sifers RN. Protein degradation unlocked. Science. 2003. 299:1330-1.
- Wu Y, Swulius MT, Moremen KW, Sifers RN. Elucidation of the molecular logic by which misfolded alpha1-antitrypsin is preferentially selected for intracellular degradation. Proc Natl Acad Sci U S A. 2003. 100:8229-34.