In this review we examine techniques, software, and statistical analyses used in label‐free
quantitative proteomics studies for area under the curve and spectral counting approaches …

Mass spectrometry-based proteomics has evolved as a high-throughput research field over
the past decade. Significant advances in instrumentation, and the ability to produce huge …

Stable isotope labeling is at present one of the most powerful methods in quantitative
proteomics. Stable isotope labeling has been performed at both the protein as well as the …

We present a flexible, user-friendly R package called protti for comprehensive quality
control, analysis and interpretation of quantitative bottom-up proteomics data. protti supports …

Several mass spectrometry-based assays have emerged for the quantitative profiling of
cellular tyrosine phosphorylation. Ideally, these methods should reveal the exact sites of …

Recent technological advances have made it possible to identify and quantify thousands of
proteins in a single proteomics experiment. As a result of these developments, the analysis …

Protein phosphorylation is instrumental to early signaling events. Studying system-wide
phosphorylation in relation to processes under investigation requires a quantitative …

Considerable insight into phosphoinositide-regulated cytoplasmic functions has been
gained by identifying phosphoinositide-effector proteins. Phosphoinositide-regulated …

Extracellular and cell surface proteins are generally modified with N-linked glycans and
glycopeptide enrichment is an attractive tool to analyze these proteins. The role of N-linked …

Mass spectrometry has proven to be an indispensable tool for protein identification,
characterization, and quantification. Among the possible methods in quantitative proteomics …