Engelbert Buxbaum
Assistant Professor, Department of Biochemistry
Biochemistry
ph: 767-255-6429
M.S. - Justus-Liebig-University
Ph.D. - Justus-Liebig-University
Dr Engelbert Buxbaum joined Ross University in 2007. Prior to that, Dr. Buxbaum held various positions in Germany, England and Kuwait, doing research on HIV, Na/K-ATPase, the Mdr1 multiple drug resistance transporter and heat shock proteins. His research interests are in the fields of enzymology and protein science.
Courses:
Biochemistry and Genetics I
Biochemistry and Genetics II
Selected Publications:
E. Buxbaum (2007)
Introduction to protein structure and function, Springer (New York)
E. Buxbaum (2003)
Cationic Electrophoresis and Electrotransfer of Membrane Glycoproteins. Anal. Biochem. 314 70-76
E. Buxbaum (1999)
Co-operating ATP sites in the Multiple Drug Resistance transporter Mdr1 Eur. J. Biochem. 265 54-63
E. Buxbaum (1999)
Co-operating binding sites for transported substrate in the Multiple Drug Resistance Transporter Mdr1. Eur. J. Biochem. 265 64-70
E. Buxbaum & P.G. Woodman (1996)
Binding of ATP and Nucleotide Analogues to Hsc70 Biochem. J. 318 923-929
E. Buxbaum & P.G. Woodman (1995)
Selective Action of Uncoating ATPase Towards Clathrin Coated Vesicles from Brain. J. Cell Sci. 108 1295-1306
E. Buxbaum (1993)
HIV und AIDS, 46 Mathem. Naturw. Untericht 105-109
E. Buxbaum & W. Schoner (1992)
Investigation of Subunit Interaction by Radiation Inactivation: The Case of Na+/K+-ATPase. J. Theor. Biol. 155 21-23
E. Buxbaum & W. Schoner (1991)
Phosphate Binding and ATP Binding Sites Coexist in Na/K-ATPase, as Demonstrated by the Inactivating MgPO4 Complex Analogue Co(NH3)4PO4. Eur. J. Biochem. 195 407-419
E. Buxbaum & W. Schoner (1990)
Blocking of Na/K-Transport by the MgPO4 Complex Analogue Co(NH3)4PO4 Leaves the Na/Na-Exchange Reaction of the Sodium Pump Unaltered and Shifts its High Affinity ATP-Binding Site to a Na-like Form. Eur. J. Biochem. 193 355-360
E. Buxbaum & P.G. Woodman (1986)
The Speed of Partial Reactions of the Uncoating ATPase Hsc70 Depends on the Source of Coated Vesicles J. Cell Sci. 109 705-711
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