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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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Mass spectral investigations on microorganisms

TL;DR: The identity of few bacterial cells present in unknown samples can be easily, rapidly and accurately established by adopting a procedure involving simple sample processing followed by direct mass spectral analysis and data processing.
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Mango: A General Tool for Collision Induced Dissociation-Cleavable Cross-Linked Peptide Identification

TL;DR: Mango is an open source software tool that extracts precursor masses from chimeric spectra generated using cleavable cross-linkers that provides an avenue to perform whole proteome cross-linking experiments without specialized instrumentation or access to nonstandard methods.
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Visualization of Host-Polerovirus Interaction Topologies Using Protein Interaction Reporter Technology.

TL;DR: It is shown that PLRV virions have hot spots of protein interaction and multifunctional surface topologies, revealing how these plant viruses maximize their use of binding interfaces and demonstrating the usefulness of PIR technology for precision mapping of functional host-pathogen protein interaction topologies.
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Characterizing the connectivity of poly-ubiquitin chains by selected reaction monitoring mass spectrometry

TL;DR: A set of specific and quantitative targeted mass spectrometry assays are developed to determine the frequency of different types of inter-ubiquitin linkages in poly-ubsitin chains relative to the total ubiquitin concentration.
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Quantification of the Compositional Information Provided by Immonium Ions on a Quadrupole-Time-of-Flight Mass Spectrometer

TL;DR: This work has created the largest database to date of high-confidence sequence assignments to characterize the appearance of immonium ions in CID spectra using a QTOF instrument under "typical" operating conditions and clearly demonstrated a positional effect whereby the proximity of the amino acid generating theImmonium ion to the amino terminal of the peptide correlates with the strength of the immonia ion peak.