Vinzenz Lange

TL;DR: This tutorial explains the application of SRM for quantitative proteomics, including the selection of proteotypic peptides and the optimization and validation of transitions, and normalization and various factors affecting sensitivity and accuracy are discussed.

TL;DR: This work presents a mass-spectrometry-based strategy to determine the absolute quantity, that is, the average number of protein copies per cell in a cell population, for a large fraction of the proteome in genetically unperturbed cells and expects it to become a cornerstone of quantitative biology and systems biology.

TL;DR: The unprecedented sensitivity of the mass spectrometric analysis of minimally fractionated plasma samples is the result of the significantly reduced sample complexity of the isolated N-glycosites compared with whole plasma proteome digests and the selectivity of the MRM process.

TL;DR: The workflow presented proved to be a cost-efficient alternative to Sanger sequencing for high-throughput HLA typing and “neXtype” for streamlined data analysis and HLA allele assignment was developed.

TL;DR: Applying this approach, low abundance virulence factors from cultures of the human pathogen Streptococcus pyogenes exposed to increasing amounts of plasma were reliably quantified and clearly defined the subset of virulence proteins that is regulated upon plasma exposure.