In the last decade, single-cell RNA sequencing routinely performed on large numbers of
single cells has greatly advanced our understanding of the underlying heterogeneity of …

The data‐independent acquisition mass spectrometry (DIA‐MS) has rapidly evolved as a
powerful alternative for highly reproducible proteome profiling with a unique strength of …

Current mass spectrometry methods enable high-throughput proteomics of large sample
amounts, but proteomics of low sample amounts remains limited in depth and throughput. To …

Single‐cell proteomics aims to characterize biological function and heterogeneity at the
level of proteins in an unbiased manner. It is currently limited in proteomic depth, throughput …

The proteome, or collection of proteoforms expressed in a biological system, is dynamic and
heterogeneous. As our appreciation for the complexity of the proteome has evolved, so have …

Data-independent acquisition (DIA) mass spectrometry (MS) has emerged as a powerful
technology for high-throughput, accurate, and reproducible quantitative proteomics. This …

Protein post-translational modifications (PTMs), which are usually enzymatically catalyzed,
are major regulators of protein activity and involved in almost all celluar processes …

The analysis of proteins that are newly synthesized upon a cellular perturbation can provide
detailed insight into the proteomic response that is elicited by specific cues. This can be …

Recent advances in methodology have made phosphopeptide analysis a tractable problem
for many proteomics researchers. There are now a wide variety of robust and accessible …

Accurate protein quantification is key to identifying protein markers, regulatory relationships
between proteins, and pathophysiological mechanisms. Realizing this potential requires …