A detailed analysis of protein abundance and phosphorylation changes across mitotic subphases and interphase in asynchronously growing human cells has been enabled by combining FACS with quantitative MS-based proteomics.

A comprehensive whole cell proteomic map describing expression time courses of >6,500 viral and cellular proteins during HIV infection identifies Vif-dependent antagonism of key cellular phosphatase PP2A.

Immunoisolation combined with quantitative proteomics identifies 79 proteins enriched in the tubular endoplasmic reticulum and provides useful tool for analyzing this organelle's functions.

Enriching the interactome with context-specific information from proteomics helps the identification of novel regulators of macrophage activation.

Metabolic labelling and quantitative proteomics reveal the temporal evolution of cellular and neuronal responses to global activity manipulations.

Myc-dependent induction of amino acid transporter expression in response to T cell receptor activation is essential to enable T cell proteome remodelling upon immune activation.

Identification and characterisation of proteins and processes regulated by HIV in primary human CD4+ T cells using an HIV reporter virus for one-step, antibody-free magnetic selection.

Building on previous work (Ly et al., 2014), we show that elutriated cells and arrested cells have similar patterns of DNA content and cyclin expression: however, a large fraction of the proteome changes detected in arrested cells are found to reflect arrest-specific responses rather than physiological cell cycle regulation.

Aneuploidy produces a protein expression signature characteristic of altered metabolism and redox homeostasis, and the loss of UBP6 ameliorates several aneuploidy-associated phenotypes.

Mass spectrometry exposes a post-transcriptionally regulated reduction in protein diversity in hematopoietic stem cells, including a lack of detectable Dnmt3a protein levels despite mRNA levels comparable to progenitors.