Journal ArticleDOI
TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Tetsuaki Arai,Masato Hasegawa,Haruhiko Akiyama,Kenji Ikeda,Takashi Nonaka,Hiroshi Mori,David M. A. Mann,Kuniaki Tsuchiya,Mari Yoshida,Yoshio Hashizume,Tatsuro Oda +10 more
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TLDR
The common occurrence of intracellular accumulations of TDP-43 supports the hypothesis that these disorders represent a clinicopathological entity of a single disease, and suggests that they can be newly classified as a proteinopathy of T DP-43.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 2006-12-22. It has received 2263 citations till now. The article focuses on the topics: Frontotemporal lobar degeneration & TARDBP.read more
Citations
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Journal ArticleDOI
TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
Jemeen Sreedharan,Ian P. Blair,Vineeta B. Tripathi,Xun Hu,Caroline Vance,Boris Rogelj,Steven Ackerley,Steven Ackerley,Jennifer C Durnall,Kelly L. Williams,Emanuele Buratti,Francisco E. Baralle,Jacqueline de Belleroche,J. Douglas Mitchell,P. Nigel Leigh,Ammar Al-Chalabi,Christopher C.J. Miller,Christopher C.J. Miller,Garth A. Nicholson,Garth A. Nicholson,Christopher Shaw +20 more
TL;DR: The evidence suggests a pathophysiological link between TDP-43 and ALS, and neighboring mutations in a highly conserved region of TARDBP in sporadic and familial ALS cases.
Journal ArticleDOI
Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature
Peter T. Nelson,Irina Alafuzoff,Eileen H. Bigio,Constantin Bouras,Heiko Braak,Nigel J. Cairns,Rudolph J. Castellani,Barbara J. Crain,Peter Davies,Kelly Del Tredici,Charles Duyckaerts,Matthew P. Frosch,Vahram Haroutunian,Patrick R. Hof,Christine M. Hulette,Bradley T. Hyman,Takeshi Iwatsubo,Kurt A. Jellinger,Gregory A. Jicha,Eniko Veronika Kovari,Walter A. Kukull,James B. Leverenz,Seth Love,Seth Love,Ian R. A. Mackenzie,David M. A. Mann,Eliezer Masliah,Ann C. McKee,Thomas J. Montine,John C. Morris,Julie A. Schneider,Joshua A. Sonnen,Dietmar Rudolf Thal,John Q. Trojanowski,Juan C. Troncoso,Thomas Wisniewski,Randall L. Woltjer,Thomas G. Beach +37 more
TL;DR: Evidence from many independent research centers strongly supports the existence of a specific disease, as defined by the presence of A&bgr; plaques and neurofibrillary tangles.
Journal ArticleDOI
TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
Edor Kabashi,Paul N. Valdmanis,Patrick A. Dion,Dan Spiegelman,Brendan J. McConkey,Christine Vande Velde,Jean-Pierre Bouchard,Lucette Lacomblez,Ksenia Pochigaeva,François Salachas,Pierre-François Pradat,William Camu,Vincent Meininger,Nicolas Dupré,Nicolas Dupré,Guy A. Rouleau +15 more
TL;DR: Findings further corroborate that TDP-43 is involved in ALS pathogenesis and reports eight missense mutations in nine individuals—six from individuals with sporadic ALS and three from those with familial ALS (FALS)—and a concurring increase of a smaller T DP-43 product.
Journal ArticleDOI
Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis.
TL;DR: It is presented the case here that these two processes are intimately linked, with disease-initiated perturbation of either leading to further deviation of both protein and RNA homeostasis through a feedforward loop including cell-to-cell prion-like spread that may represent the mechanism for relentless disease progression.
Journal ArticleDOI
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
Magdalini Polymenidou,Clotilde Lagier-Tourenne,Kasey R. Hutt,Stephanie C. Huelga,Jacqueline T. Moran,Tiffany Y. Liang,Shuo-Chien Ling,Eveline Sun,Edward Wancewicz,Curt Mazur,Holly B. Kordasiewicz,Yalda Sedaghat,John Paul Donohue,Lily Shiue,C. Frank Bennett,Gene W. Yeo,Don W. Cleveland +16 more
TL;DR: It is found that TDP-43 autoregulates its synthesis, in part by directly binding and enhancing splicing of an intron in the 3′ untranslated region of its own transcript, thereby triggering nonsense-mediated RNA degradation.
References
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Journal ArticleDOI
Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
Matt Baker,Ian R. A. Mackenzie,Stuart Pickering-Brown,Jennifer Gass,Rosa Rademakers,Caroline Lindholm,Julie S. Snowden,Jennifer Adamson,A. Dessa Sadovnick,Sara Rollinson,Ashley Cannon,Emily Dwosh,David Neary,Stacey Melquist,Anna Richardson,Dennis W. Dickson,Zdenek Berger,Jason L. Eriksen,Todd Robinson,Cynthia Zehr,Chad A. Dickey,Richard Crook,Eileen McGowan,David M. A. Mann,Bradley F. Boeve,Howard Feldman,Mike Hutton +26 more
TL;DR: It is demonstrated that in multiple FTD families with significant evidence for linkage to the same region on chromosome 17q21, FTD is caused by mutations in progranulin (PGRN) that are likely to create null alleles and identified mutations in PGRN as a cause of neurodegenerative disease.
Journal ArticleDOI
|[alpha]|-Synuclein is phosphorylated in synucleinopathy lesions
Hideo Fujiwara,Masato Hasegawa,Naoshi Dohmae,Akiko Kawashima,Eliezer Masliah,Matthew S. Goldberg,Jie Shen,Koji Takio,Takeshi Iwatsubo +8 more
TL;DR: It is shown by mass spectrometry analysis and studies with an antibody that specifically recognizes phospho-Ser 129 of α-synuclein, that this residue is selectively and extensively phosphorylated in synucleinopathy lesions and promoted fibril formation in vitro.
Journal ArticleDOI
Clinical and Pathological Diagnosis of Frontotemporal Dementia: Report of the Work Group on Frontotemporal Dementia and Pick's Disease
Guy M. McKhann,Marilyn S. Albert,Murray Grossman,Bruce L. Miller,Dennis W. Dickson,John Q. Trojanowski +5 more
TL;DR: The goal of this meeting was to propose guidelines that would enable clinicians to recognize patients with FTD and, if appropriate, expedite their referral to a diagnostic center.
Journal ArticleDOI
Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21
Marc Cruts,Ilse Gijselinck,Julie van der Zee,Sebastiaan Engelborghs,Hans Wils,Daniel Pirici,Rosa Rademakers,Rik Vandenberghe,Bart Dermaut,Jean-Jacques Martin,Cornelia M. van Duijn,Karin Peeters,Raphael Sciot,Patrick Santens,Tim De Pooter,Maria Mattheijssens,Marleen Van den Broeck,Ivy Cuijt,Krist'l Vennekens,Peter Paul De Deyn,Samir Kumar-Singh,Christine Van Broeckhoven +21 more
TL;DR: It is demonstrated that FTDU-17 is caused by mutations in the gene coding for progranulin (PGRN), a growth factor involved in multiple physiological and pathological processes including tumorigenesis, and evidence that P GRN haploinsufficiency leads to neurodegeneration because of reduced PGRN-mediated neuronal survival is provided.
Journal ArticleDOI
Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein.
Giles D. J. Watts,Jill Wymer,Margaret J. Kovach,Sarju G. Mehta,Steven Mumm,Daniel Darvish,Alan Pestronk,Michael P. Whyte,Virginia Kimonis +8 more
TL;DR: Identification of VCP as causing IBMPFD has important implications for other inclusion-body diseases, including myopathies, dementias and Paget disease of bone (PDB), as it may define a new common pathological ubiquitin-based pathway.
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