Surachai Supattapone, MD, PhD
Professor of Biochemistry and Cell Biology
Professor of Medicine
Biochemistry and Cell Biology
Johns Hopkins University School of Medicine, Ph.D. 1992
Johns Hopkins University School of Medicine, M.D. 1992, Oxford University Ph.D. 1991
Molecular and Cellular Biology Graduate Programs
Molecular Pathogenesis Program
Neuroscience Center at Dartmouth
Dartmouth Medical School
Hanover NH 03755
Office: 311 Vail Building
Surachai joined the Dartmouth faculty in 2001, and has enjoyed teaching in the Year One Metabolism and Scientific Basis of Medicine courses for medical students, as well as the Core Course for Molecular and Cellular Biology graduate students. He has also greatly enjoyed having the opportunity to mentor students conducting laboratory research projects on the pathogenesis of prion disease. Surachai has also served as director for the Clinical Translational Science Masters Program, a co-director for the Cellular and Molecular Basis of Disease course, and member of the Medical Education Committee and the Committee for Student Performance and Conduct. He has won teaching awards at Geisel and at the University of California at San Francisco.
Surachai would be happy to mentor faculty on integrating basic science in medical education.
CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins.
Interallelic Transcriptional Enhancement as an in Vivo Measure of Transvection in Drosophila melanogaster.
The effect of reducing agents on challenge of rainbow trout with Aeromonas salmonicida.
Dissociation of recombinant prion autocatalysis from infectivity.
Expanding the prion disease repertoire.
A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.
Requirements for mutant and wild-type prion protein misfolding in vitro.
Synthesis of high titer infectious prions with cofactor molecules.
Elucidating the role of cofactors in mammalian prion propagation.
Prion nucleation site unmasked by transient interaction with phospholipid cofactor.