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Seong Soo A. An

Researcher at Gachon University

Publications -  237
Citations -  5778

Seong Soo A. An is an academic researcher from Gachon University. The author has contributed to research in topics: Medicine & PSEN1. The author has an hindex of 35, co-authored 208 publications receiving 4373 citations. Previous affiliations of Seong Soo A. An include Konkuk University & Carnegie Mellon University.

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Kringle 5 of plasminogen is a novel inhibitor of endothelial cell growth.

TL;DR: Kringle 5 domain of human plasminogen is a novel endothelial inhibitor that is sufficiently potent to block the growth factor-stimulated endothelial cell growth.
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Role of inflammatory molecules in the Alzheimer's disease progression and diagnosis.

TL;DR: The role or possible role of immune cells and inflammatory molecules in disease progression or prevention and how induction or inhibition of inflammatory factors could be used for AD therapies are summarized.
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Claudin-1 induces epithelial-mesenchymal transition through activation of the c-Abl-ERK signaling pathway in human liver cells.

TL;DR: It is shown that CL DN1 has a causal role in the epithelial–mesenchymal transition (EMT) in human liver cells, and that the c-Abl-Ras-Raf-1-ERK1/2 signaling axis is critical for the induction of malignant progression by CLDN1.
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Review on gold nanoparticles and their applications

TL;DR: This review addressed the use of gold nanoparticles and the surface functionalization with a wide range of molecules, expanding and improvinggold nanoparticles in targeting drugs for photothermal therapy with reduced cytotoxic effcts in various cancers, gene therapy and many other diseases.
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Heme Cofactor-Resembling Fe–N Single Site Embedded Graphene as Nanozymes to Selectively Detect H2O2 with High Sensitivity

TL;DR: Based on the high and selective peroxidase‐like activity of Fe–N‐rGO, trace amounts of H2O2 produced from the enzymatic reactions from acetylcholine and cancerous cells are successfully quantified with high sensitivity and selectivity and are expected to encourage studies on the rational design of nanozymes pursuing the active site structure of natural enzymes.