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Soo-Jung Kim

Researcher at University of Pennsylvania

Publications -  6
Citations -  190

Soo-Jung Kim is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Progressive supranuclear palsy & Tauopathy. The author has an hindex of 5, co-authored 5 publications receiving 102 citations. Previous affiliations of Soo-Jung Kim include National Institutes of Health.

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Transmission of tauopathy strains is independent of their isoform composition

TL;DR: A new transgenic mouse line is generated expressing 6 human tau isoforms with equal 3R and 4R ratios, recapitulate distinct human t Tau strains in mouse brains with similar isoform compositions and cell type specificities, and further show the strain transmission pattern is independent of its isoform composition.
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Characterization of tau binding by gosuranemab.

TL;DR: A detailed biochemical and biophysical characterization of the tau-binding properties of gosuranemab, a humanized monoclonal antibody directed against N-terminal tau that is currently being investigated as a treatment for AD is reported.
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Detection of Alzheimer's disease (AD) specific tau pathology with conformation-selective anti-tau monoclonal antibody in co-morbid frontotemporal lobar degeneration-tau (FTLD-tau).

TL;DR: The use of GT-38 is validated to selectively detect AD-tau pathology in the context of FTLD- tau and provides a novel tool to investigate associations of clinical phenotypes amongst co-morbid tauopathies.
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In vitro amplification of pathogenic tau conserves disease-specific bioactive characteristics.

TL;DR: In this article, a modified seeding protocol was used to template the recruitment of recombinant 2N4R (T40) tau protein in vitro, and the efficacy of the amplification reactions and the pathogenic fidelity of the amplified material to the original tau seeds using recently developed sporadic tau spreading models.
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Conformation-selective tau monoclonal antibodies inhibit tau pathology in primary neurons and a mouse model of Alzheimer’s disease

TL;DR: Findings demonstrate that conformation-selective tau mAbs, DMR7 and SKT82, inhibit tau pathology in primary neurons by preventing the uptake of tau seeds and reduce t Tau pathology in vivo, providing potential novel therapeutic candidates for the treatment of AD.