Benoit I. Giasson, Ph.D.

Pharmacology University of Pennsylvania, Philadelphia, PA, United States 
 Neuroscience University of Florida, Gainesville, Gainesville, FL, United States 
Neurodegeneration ,Parkinson’s disease, Neuronal Damage, Protein Aggregation,Kinases, Alpha-synuclein, Tau
"Benoit Giasson"

Post-Doc, Pathology and Laboratory Medicine (John Trojanowski), University of Pennsylvania, 2001-2003
Post-Doc, Pathology and Laboratory Medicine (Virginia Lee), University of Pennsylvania, 1998-2001
Ph.D., Biochemistry, McGill University, Canada- 1997

My research is focused on understanding the cellular mechanisms and molecular interactions involved as underlying causes of neurodegenerative diseases. A primary research interest is to expand the understanding of the regulation of protein levels, function, interactions and folding that affect protein aggregation in the nervous system.

Mean distance: 15.49 (cluster 24)
Cross-listing: Chemistry Tree


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Walter E. Mushynski grad student 1991-1997 McGill
Virginia Man-Yee Lee post-doc 1998-2001 Penn
John Q. Trojanowski post-doc 2001-2003 Penn


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Jason P. Covy grad student 2004-2010 Penn
Chenere P. Ramsey grad student 2004-2010 Penn
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Sorrentino ZA, Goodwin MS, Riffe CJ, et al. (2019) Unique α-synuclein pathology within the amygdala in Lewy body dementia: implications for disease initiation and progression. Acta Neuropathologica Communications. 7: 142
Tayebi N, Parisiadou L, Berhe B, et al. (2017) Glucocerebrosidase haploinsufficiency in A53T α-synuclein mice impacts disease onset and course. Molecular Genetics and Metabolism. 122: 198-208
Sacino AN, Brooks MM, Chakrabarty P, et al. (2016) Proteolysis of α-Synuclein Fibrils in the Lysosomal Pathway Limits Induction of Inclusion Pathology. Journal of Neurochemistry
Uchihara T, Giasson BI, Paulus W. (2015) Propagation of Aβ, tau and α-synuclein pathology between experimental models and human reality: prions, propagons and propaganda. Acta Neuropathologica
Sacino AN, Ayers JI, Brooks MM, et al. (2015) Non-prion-type transmission in A53T α-synuclein transgenic mice: a normal component of spinal homogenates from naïve non-transgenic mice induces robust α-synuclein pathology. Acta Neuropathologica
Uchihara T, Giasson BI. (2015) Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies. Acta Neuropathologica
Hamm M, Bailey R, Shaw G, et al. (2015) Physiologically relevant factors influence tau phosphorylation by leucine-rich repeat kinase 2. Journal of Neuroscience Research
Chakrabarty P, Hudson Iii VJ, Sacino AN, et al. (2015) Inefficient induction and spread of seeded tau pathology in P301L mouse model of tauopathy suggests inherent physiological barriers to transmission. Acta Neuropathologica. 130: 303-5
Rutherford NJ, Giasson BI. (2015) The A53E α-synuclein pathological mutation demonstrates reduced aggregation propensity in vitro and in cell culture. Neuroscience Letters. 597: 43-8
Fishbein I, Kuo YM, Giasson BI, et al. (2014) Augmentation of phenotype in a transgenic Parkinson mouse heterozygous for a Gaucher mutation. Brain : a Journal of Neurology. 137: 3235-47
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