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Yoonjung Kho

Researcher at University of Texas Southwestern Medical Center

Publications -  5
Citations -  2028

Yoonjung Kho is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Proteomics & Protein farnesylation. The author has an hindex of 4, co-authored 5 publications receiving 1917 citations.

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Journal ArticleDOI

Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

TL;DR: This study reveals previously unappreciated roles for lysine acetylation in the regulation of diverse cellular pathways outside of the nucleus, including many longevity regulators and metabolism enzymes.
Journal ArticleDOI

A tagging-via-substrate technology for detection and proteomics of farnesylated proteins

TL;DR: TAS technology can be extended to other posttranslational modifications, such as geranylgeranylation and myristoylation, thus providing powerful tools for detection, quantification, and proteomic analysis of posttranslationally modified proteins.
Journal ArticleDOI

Proteomic Analysis of Integral Plasma Membrane Proteins

TL;DR: A biotin-directed affinity purification (BDAP) method for the preparation of integral plasma membrane proteins, which involves biotinylation of cell surface membrane proteins in viable cells, affinity enrichment using streptavidin beads, and depletion of plasma membrane-associated cytosolic proteins by harsh washes with high-salt and high-pH buffers is reported.
Journal ArticleDOI

Broad spectrum identification of SUMO substrates in melanoma cells.

TL;DR: It is found that epidermal growth factor (EGF) stimulation evokes a rapid alteration in small ubiquitin modifier (SUMO) target selection, while oncogene expression alters steady‐state SUMO‐protein profiles.
Book ChapterDOI

A tagging-via-substrate technology for genome-wide detection and identification of farnesylated proteins.

TL;DR: This chapter describes the principle of TAS technology and details the method for detection and enrichment of farnesylated proteins.