scispace - formally typeset
N

Nathan A. Yates

Researcher at University of Pittsburgh

Publications -  71
Citations -  3051

Nathan A. Yates is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Mass spectrometry & Proteomics. The author has an hindex of 26, co-authored 68 publications receiving 2518 citations. Previous affiliations of Nathan A. Yates include Merck & Co. & Northwestern University.

Papers
More filters
Journal ArticleDOI

How many human proteoforms are there

Ruedi Aebersold, +53 more
TL;DR: This work frames central issues regarding determination of protein-level variation and PTMs, including some paradoxes present in the field today, and uses this framework to assess existing data and ask the question, "How many distinct primary structures of proteins (proteoforms) are created from the 20,300 human genes?"
Journal ArticleDOI

Differential mass spectrometry: a label-free LC-MS method for finding significant differences in complex peptide and protein mixtures.

TL;DR: An automated, label-free method for finding differences in complex mixtures using complete LC-MS data sets, rather than subsets of extracted peaks or features, which is more sensitive and gives fewer false positives than subtractive methods that ignore signal variability.
Patent

Mass spectrometry data analysis techniques

TL;DR: In this article, the statistical significance of changes to signals associated with mass-to-charge ratios (m/z intensity pairs) between individual samples and sample sets is determined based on changes likely to indicate analyte level differences are identified.
Journal ArticleDOI

Lysine 63-linked polyubiquitination is required for EGF receptor degradation

TL;DR: Mass spectrometry-based targeted proteomics is used to show that activated epidermal growth factor receptor (EGFR) is ubiquitinated by one to two short polyubiquitin chains mainly linked via lysine 63 (K63) or conjugated with a single monoubiquit in.
Journal ArticleDOI

Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation.

TL;DR: Electron capture dissociation (ECD) and collision-induced Dissociation (CID) are demonstrated to be effective in the detection and localization of the methionine sulfoxide residues in peptides using Fourier transform ion cyclotron resonance (FTICR) mass spectrometry.