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Kenneth C. Parker

Researcher at Applied Biosystems

Publications -  17
Citations -  4773

Kenneth C. Parker is an academic researcher from Applied Biosystems. The author has contributed to research in topics: Mass spectrometry & Peptide mass fingerprinting. The author has an hindex of 8, co-authored 17 publications receiving 4584 citations.

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Multiplexed Protein Quantitation in Saccharomyces cerevisiae Using Amine-reactive Isobaric Tagging Reagents

TL;DR: It is found that inactivation of Upf1p and Xrn1p causes common as well as unique effects on protein expression, and the use of 4-fold multiplexing to enable relative protein measurements simultaneously with determination of absolute levels of a target protein using synthetic isobaric peptide standards.
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Toward a high-throughput approach to quantitative proteomic analysis: expression-dependent protein identification by mass spectrometry.

TL;DR: A new software program for the automated quantification of ICAT reagent labeled peptides analyzed by microcapillary electrospray ionization time-of-flight mass spectrometry determines those peptides that differ in their abundance.
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Identification of yeast proteins from two‐dimensional gels: Working out spot cross‐contamination

TL;DR: Focusing on 14 spots in a narrow‐pH‐range gel, it is demonstrated how organizing peak‐table data and peptide match‐list data into databases enables the identification of a larger percentage of the peaks.
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Scoring methods in MALDI peptide mass fingerprinting: ChemScore, and the ChemApplex program.

TL;DR: Protein scoring based on Combined Protein Score is orthogonal to many of the commonly used probability-based scoring schemes, and makes it possible to archive a more complete set of parameters that more thoroughly characterize the validity of the database match, which increases the confidence in the identifications.
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Depth of Proteome Issues A Yeast Isotope-Coded Affinity Tag Reagent Study

TL;DR: This work sought to assess the reproducibility of peptide identification and to develop an informatics structure that characterizes the identification process as well as possible, especially with regard to tenuous identifications.