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Jimmy K. Eng

Researcher at University of Washington

Publications -  171
Citations -  37832

Jimmy K. Eng is an academic researcher from University of Washington. The author has contributed to research in topics: Mass spectrometry & Proteome. The author has an hindex of 77, co-authored 168 publications receiving 35701 citations. Previous affiliations of Jimmy K. Eng include Oregon Health & Science University & Fred Hutchinson Cancer Research Center.

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Journal ArticleDOI

Proteomic analyses using Grifola frondosa metalloendoprotease Lys-N.

TL;DR: A relatively obscure basidomycete-derived zinc metalloendopeptidase, Lys-N, that selectively cleaves the amide bond N-terminal of lysine residues is benchmarked and it is found that Lys- N digestion yields peptides with easily assigned CID spectra.
Book ChapterDOI

Characterization of proteome of human cerebrospinal fluid.

TL;DR: To identify as many CSF proteins in well-characterized healthy young subjects as possible, sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE) was used to prefractionate theCSF proteins before further separation by multidimensional liquid chromatography and analyzed with LCQ or LTQ-FT mass spectrometry (MS).
Journal ArticleDOI

Protein Kinase PKN1 Represses Wnt/β-Catenin Signaling in Human Melanoma Cells

TL;DR: This study identifies a kinase that inhibits Wnt/β-catenin signaling, a pathway critical to melanoma cell viability, and sensitizes melanoma cells to cell death stimulated by WNT3A.
Journal ArticleDOI

In vivo application of photocleavable protein interaction reporter technology.

TL;DR: Three proteins or protein complexes with detailed crystallography structures are compared to the cross-linking results obtained from in vivo application of pcPIR technology.
Journal ArticleDOI

Tools for 3D Interactome Visualization

TL;DR: New informatics capabilities are developed, the first to enable 3D visualization of multiple quantitative interactome data sets, acquired over time or with varied perturbation levels, to reveal relevant dynamic interactome changes.