M
Matthew Micsenyi
Researcher at University of Pennsylvania
Publications - 3
Citations - 5883
Matthew Micsenyi is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Frontotemporal lobar degeneration & Frontotemporal dementia. The author has an hindex of 3, co-authored 3 publications receiving 5173 citations.
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Journal ArticleDOI
Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Manuela Neumann,Deepak M. Sampathu,Linda K. Kwong,Adam C. Truax,Matthew Micsenyi,Thomas T. Chou,Jennifer Bruce,Theresa Schuck,Murray Grossman,Christopher M. Clark,Leo McCluskey,Bruce L. Miller,Eliezer Masliah,Ian R. A. Mackenzie,Howard Feldman,Wolfgang Feiden,Hans A. Kretzschmar,John Q. Trojanowski,Virginia M.-Y. Lee +18 more
TL;DR: It is shown that TDP-43 is the major disease protein in both frontotemporal lobar degeneration with ubiquitin-positive inclusions and amyotrophic lateral sclerosis.
Journal ArticleDOI
Pathological heterogeneity of frontotemporal lobar degeneration with ubiquitin-positive inclusions delineated by ubiquitin immunohistochemistry and novel monoclonal antibodies.
Deepak M. Sampathu,Manuela Neumann,Linda K. Kwong,Thomas T. Chou,Matthew Micsenyi,Adam C. Truax,Jennifer Bruce,Murray Grossman,John Q. Trojanowski,Virginia M.-Y. Lee +9 more
TL;DR: Examination of tissue sections from FTLD-U brains stained with anti-ubiquitin antibodies revealed heterogeneity in the morphological characteristics of pathological inclusions among subsets of cases, suggesting that frontotemporal lobar degeneration with ubiquitin-positive inclusions is pathologically heterogeneous.
Journal ArticleDOI
Convergence of Heat Shock Protein 90 with Ubiquitin in Filamentous α-Synuclein Inclusions of α-Synucleinopathies
Kunihiro Uryu,Christiane Richter-Landsberg,William Welch,Eveline Sun,Olaf Goldbaum,Erin H. Norris,Chi-Tuan Pham,Ikuru Yazawa,Kristen Hilburger,Matthew Micsenyi,Benoit I. Giasson,Nancy M. Bonini,Virginia M.-Y. Lee,John Q. Trojanowski +13 more
TL;DR: In this article, heat shock proteins (Hsps) facilitate refolding of denatured polypeptides, but there is limited understanding about their roles in neurodegenerative diseases characterized by misfolded proteins.