J
John Q. Trojanowski
Researcher at University of Pennsylvania
Publications - 1538
Citations - 245534
John Q. Trojanowski is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Dementia & Alzheimer's disease. The author has an hindex of 226, co-authored 1467 publications receiving 213948 citations. Previous affiliations of John Q. Trojanowski include Vanderbilt University & University of California, San Francisco.
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Journal ArticleDOI
Multiple proteins implicated in neurodegenerative diseases accumulate in axons after brain trauma in humans.
Kunihiro Uryu,Xiao-Han Chen,Daniel Martinez,Kevin D. Browne,Victoria E. Johnson,David I. Graham,Virginia M.-Y. Lee,John Q. Trojanowski,Douglas H. Smith +8 more
TL;DR: Brain tissue from 18 cases who died after TBI and from 6 control cases was examined using immunohistochemistry to show rapid axonal accumulation of proteins implicated in neurodegenerative diseases including Alzheimer's disease and the synucleinopathies.
Journal ArticleDOI
The Microtubule-Stabilizing Agent, Epothilone D, Reduces Axonal Dysfunction, Neurotoxicity, Cognitive Deficits, and Alzheimer-Like Pathology in an Interventional Study with Aged Tau Transgenic Mice
Bin Zhang,Jenna C. Carroll,John Q. Trojanowski,Yuemang Yao,Michiyo Iba,Justin S. Potuzak,Anne-Marie L. Hogan,Sharon X. Xie,Carlo Ballatore,Amos B. Smith,Virginia M.-Y. Lee,Kurt R. Brunden +11 more
TL;DR: Data reveal that brain-penetrant MT-stabilizing drugs hold promise for the treatment of AD and related tauopathies, and that EpoD could be a candidate for clinical testing.
Journal ArticleDOI
Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies.
Kunihiro Uryu,Hanae Nakashima-Yasuda,Mark S. Forman,Linda K. Kwong,Christopher M. Clark,Murray Grossman,Bruce L. Miller,Hans A. Kretzschmar,Virginia M.-Y. Lee,John Q. Trojanowski,Manuela Neumann +10 more
TL;DR: Findings provide further insight into the burden and clinical significance of TDP-43 pathology in disorders other than FTLD-U and amyotrophic lateral sclerosis.
Journal ArticleDOI
Aging-related tau astrogliopathy (ARTAG): harmonized evaluation strategy
Gabor G. Kovacs,Isidro Ferrer,Lea T. Grinberg,Lea T. Grinberg,Irina Alafuzoff,Johannes Attems,Herbert Budka,Nigel J. Cairns,John F. Crary,Charles Duyckaerts,Bernardino Ghetti,Glenda M. Halliday,James W. Ironside,Seth Love,Ian R. A. Mackenzie,David G. Munoz,Melissa E. Murray,Peter T. Nelson,Hitoshi Takahashi,John Q. Trojanowski,Olaf Ansorge,Thomas Arzberger,Atik Baborie,Thomas G. Beach,Kevin F. Bieniek,Eileen H. Bigio,Istvan Bodi,Brittany N. Dugger,Mel B. Feany,Ellen Gelpi,Stephen M. Gentleman,Giorgio Giaccone,Kimmo J. Hatanpaa,Richard Heale,Patrick R. Hof,Monika Hofer,Tibor Hortobágyi,Kurt A. Jellinger,Gregory A. Jicha,Paul G. Ince,Julia Kofler,Eniko Veronika Kovari,Jillian J. Kril,David M. A. Mann,Radoslav Matej,Ann C. McKee,Catriona McLean,Ivan Milenkovic,Thomas J. Montine,Shigeo Murayama,Edward B. Lee,Jasmin Rahimi,Roberta Diehl Rodriguez,Annemieke J.M. Rozemuller,Julie A. Schneider,Christian Schultz,William W. Seeley,Danielle Seilhean,Colin Smith,Fabrizio Tagliavini,Masaki Takao,Dietmar Rudolf Thal,Dietmar Rudolf Thal,Jon B. Toledo,Markus Tolnay,Juan C. Troncoso,Harry V. Vinters,Serge Weis,Stephen B. Wharton,Charles L. White,Thomas Wisniewski,John Woulfe,Masahito Yamada,Dennis W. Dickson +73 more
Abstract: Pathological accumulation of abnormally phosphorylated tau protein in astrocytes is a frequent, but poorly characterized feature of the aging brain. Its etiology is uncertain, but its presence is sufficiently ubiquitous to merit further characterization and classification, which may stimulate clinicopathological studies and research into its pathobiology. This paper aims to harmonize evaluation and nomenclature of aging-related tau astrogliopathy (ARTAG), a term that refers to a morphological spectrum of astroglial pathology detected by tau immunohistochemistry, especially with phosphorylation-dependent and 4R isoform-specific antibodies. ARTAG occurs mainly, but not exclusively, in individuals over 60 years of age. Tau-immunoreactive astrocytes in ARTAG include thorn-shaped astrocytes at the glia limitans and in white matter, as well as solitary or clustered astrocytes with perinuclear cytoplasmic tau immunoreactivity that extends into the astroglial processes as fine fibrillar or granular immunopositivity, typically in gray matter. Various forms of ARTAG may coexist in the same brain and might reflect different pathogenic processes. Based on morphology and anatomical distribution, ARTAG can be distinguished from primary tauopathies, but may be concurrent with primary tauopathies or other disorders. We recommend four steps for evaluation of ARTAG: (1) identification of five types based on the location of either morphologies of tau astrogliopathy: subpial, subependymal, perivascular, white matter, gray matter; (2) documentation of the regional involvement: medial temporal lobe, lobar (frontal, parietal, occipital, lateral temporal), subcortical, brainstem; (3) documentation of the severity of tau astrogliopathy; and (4) description of subregional involvement. Some types of ARTAG may underlie neurological symptoms; however, the clinical significance of ARTAG is currently uncertain and awaits further studies. The goal of this proposal is to raise awareness of astroglial tau pathology in the aged brain, facilitating communication among neuropathologists and researchers, and informing interpretation of clinical biomarkers and imaging studies that focus on tau-related indicators.
Journal ArticleDOI
Detection of phosphorylated Ser262 in fetal tau, adult tau, and paired helical filament tau.
Peter Seubert,Madhumalti Mawal-Dewan,Robin Barbour,Ross Jakes,Michel Goedert,Gail V.W. Johnson,Joel M. Litersky,Dale Schenk,Ivan Lieberburg,John Q. Trojanowski,Virginia M.-Y. Lee +10 more
TL;DR: It is speculated that the binding of tau to microtubules is regulated by phosphorylation at multiple sites and that the generation of PHF-tau in Alzheimer's disease results from the reduced efficiency of phosphatases leading to the incremental accumulation of hyperphosphorylated tau.