L
Linda K. Kwong
Researcher at University of Pennsylvania
Publications - 47
Citations - 15248
Linda K. Kwong is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Frontotemporal lobar degeneration & Amyotrophic lateral sclerosis. The author has an hindex of 38, co-authored 47 publications receiving 13370 citations. Previous affiliations of Linda K. Kwong include National Institutes of Health.
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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.
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Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
Ian R. A. Mackenzie,Eileen H. Bigio,Paul G. Ince,Felix Geser,Manuela Neumann,Nigel J. Cairns,Linda K. Kwong,Mark S. Forman,John Ravits,Heather Stewart,Andrew Eisen,Leo McClusky,Hans A. Kretzschmar,Camelia M. Monoranu,J. Robin Highley,Janine Kirby,Teepu Siddique,Pamela J. Shaw,Virginia M.-Y. Lee,John Q. Trojanowski +19 more
TL;DR: This study investigated TDP‐43 in a larger series of ALS cases, including familial cases with and without SOD1 mutations, and identified it as the major pathological protein in sporadic ALS.
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Stages of pTDP‐43 pathology in amyotrophic lateral sclerosis
Johannes Brettschneider,Kelly Del Tredici,Jon B. Toledo,John L. Robinson,David J. Irwin,Murray Grossman,EunRan Suh,Vivianna M. Van Deerlin,Elisabeth M. Wood,Young Min Baek,Linda K. Kwong,Edward B. Lee,Lauren Elman,Leo McCluskey,Lubin Fang,Simone Feldengut,Albert C. Ludolph,Virginia M.-Y. Lee,Heiko Braak,John Q. Trojanowski +19 more
TL;DR: To see whether the distribution patterns of phosphorylated 43kDa TAR DNA‐binding protein (pTDP‐43) intraneuronal inclusions in amyotrophic lateral sclerosis (ALS) permit recognition of neuropathological stages, a chiral model is constructed.
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Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons
Jing L. Guo,Dustin J. Covell,Joshua P. Daniels,Michiyo Iba,Anna Stieber,Bin Zhang,Dawn M. Riddle,Linda K. Kwong,Yan Xu,John Q. Trojanowski,Virginia M.-Y. Lee +10 more
TL;DR: It is speculated that distinct strains of pathological α-synuclein likely exist in neurodegenerative disease brains and may underlie the tremendous heterogeneity of synucleinopathies.
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The acetylation of tau inhibits its function and promotes pathological tau aggregation
Todd J. Cohen,Jing L. Guo,David E. Hurtado,Linda K. Kwong,Ian P. Mills,John Q. Trojanowski,Virginia M.-Y. Lee +6 more
TL;DR: It is demonstrated that tau acetylation inhibits tau function via impaired tau-microtubule interactions and promotes pathological tau aggregation, and suggests tau K280 acetylations is a potential target for drug discovery and biomarker development for AD and related tauopathies.