Mass spectrometry in the postgenomic era.

@article{Chait2011MassSI,
  title={Mass spectrometry in the postgenomic era.},
  author={Brian T. Chait},
  journal={Annual review of biochemistry},
  year={2011},
  volume={80},
  pages={
          239-46
        }
}
  • B. Chait
  • Published 2011
  • Biology, Medicine
  • Annual review of biochemistry
Mass spectrometry (MS) is rapidly becoming an essential tool for biologists and biochemists in their efforts to throw light on molecular mechanisms within cellular systems. Used in unison with genome sequence data, MS has developed into the method of choice for identifying proteins, elucidating their posttranslational modifications, and reading out their functional interactions. Variations of the method have even begun to enable accurate mass determination of intact protein complexes, allowing… Expand
A mass spectrometry view of stable and transient protein interactions.
TLDR
An overview of workflows that incorporate immunoaffinity purifications and quantitative mass spectrometry (frequently abbreviated as IP-MS or AP-MS) for characterizing protein-protein interactions is provided. Expand
Ion Dissociation Methods in Proteomics
This article serves as a review of polypeptide ion dissociation methods in the context of mass spectrometry (MS)-based proteomic analysis. Given the many tandem mass spectrometry (MS/MS) instrumentExpand
Recent advances in peptide separation by multidimensional liquid chromatography for proteome analysis.
TLDR
This review attempts to provide a historical perspective to separations in proteomics as well as indicate the principles of their operation and rationales for their implementation and provides a guide on what are the possibilities for combining different separation in order to increase peak capacity and proteome coverage. Expand
Middle-down approaches for mass spectrometry-based protein identification and characterization
Mass spectrometry (MS) has emerged over the last two decades as the analytical technique of choice in systems-level protein studies, known as proteomics. Two are the MS-based approaches generallyExpand
Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions.
TLDR
An understanding of protein functions cannot be fully accomplished without knowledge of its interactions, and characterizing these interactions is critical to understanding the biology of health and disease systems. Expand
Purification of a specific native genomic locus for proteomic analysis
TLDR
The TAL-ChAP-MS approach allows the biochemical isolation of a specific native genomic locus for proteomic studies and will provide for unprecedented objective insight into protein and epigenetic mechanisms regulating site-specific chromosome metabolism. Expand
Taming the Huntington's Disease Proteome: What Have We Learned?
TLDR
This review summarizes the data from most of the MS studies done in the HD field in the last 20 years and compares it to the protein data reported before the use of MS technology, to validate early findings in the field and identify new changes. Expand
Trends in ultrasensitive proteomics.
Here we review recent developments and trends in sample preparation, pre-fractionation, chromatography and mass spectrometry contributing towards the ultra-sensitive global analysis of proteins.Expand
Mass spectrometry and animal science: protein identification strategies and particularities of farm animal species.
TLDR
The main methodologies available for protein identification using mass spectrometry are summarized, with particular reference to experiments using animal species poorly described in public databases, providing a case study of specific applications in the field of animal science. Expand
A Pipeline for Determining Protein–Protein Interactions and Proximities in the Cellular Milieu*
TLDR
Stabilized Affinity Capture Mass Spectrometry allows us to stabilize and elucidate local, distant, and transient protein interactions within complex cellular milieux, many of which are not observed in the absence of chemical stabilization. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 333 REFERENCES
Phosphoproteomics for the masses.
TLDR
An overview of how in vivo phosphorylation technology came to be and is currently applied, as well as future challenges for the field are presented. Expand
The role of mass spectrometry in structure elucidation of dynamic protein complexes.
TLDR
The applications described herein not only confirm the status of mass spectrometry as a structural biology approach to complement X-ray analysis or electron microscopy, but also highlight unique attributes of the methodology. Expand
Advances in the mass spectrometry of membrane proteins: from individual proteins to intact complexes.
TLDR
Exciting possibilities now exist to go beyond primary and secondary structure to reveal the tertiary and quaternary interactions of soluble and membrane subunits within intact assemblies of more than 700 kDa. Expand
Quantitative, high-resolution proteomics for data-driven systems biology.
  • J. Cox, M. Mann
  • Biology, Medicine
  • Annual review of biochemistry
  • 2011
TLDR
The principles of analysis and the areas of biology where proteomics can make unique contributions are described and the large-scale nature of proteomics data and its high accuracy pose special opportunities as well as challenges in systems biology that have been largely untapped so far. Expand
Mass spectrometry–based proteomics turns quantitative
TLDR
Two recently developed methodologies offer the opportunity to obtain quantitative proteomic information by comparing the signals from the same peptide under different conditions, and stable isotope labels facilitates direct quantification from the mass spectra. Expand
Proteomics by mass spectrometry: approaches, advances, and applications.
TLDR
This review dissects the overall framework of the MS experiment into its key components, and highlights both the inherent strengths and limitations of protein MS and offer a rough guide for selecting an experimental design based on the goals of the analysis. Expand
The utility of ETD mass spectrometry in proteomic analysis.
TLDR
The utility of electron transfer dissociation (ETD) mass spectrometry for sequence analysis of post-translationally modified and/or highly basic peptides is reviewed to illustrate the utility of ETD as an advantageous tool in proteomic research by readily identifying peptides resistant to analysis by CAD. Expand
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
TLDR
Comparison of the HMS-PCI data set with interactions reported in the literature revealed an average threefold higher success rate in detection of known complexes compared with large-scale two-hybrid studies. Expand
The emerging process of Top Down mass spectrometry for protein analysis: biomarkers, protein-therapeutics, and achieving high throughput.
TLDR
Together with steadily advancing commercial MS instrumentation and data processing, a high-throughput workflow covering intact proteins and polypeptides up to 70 kDa is directly visible in the near future. Expand
Applications of mass spectrometry to lipids and membranes.
TLDR
Deuterium exchange mass spectrometry is being used to investigate the association of lipids and membranes with proteins and enzymes, and imaging mass Spectrometry (IMS) is being applied to the in situ analysis oflipids in tissues. Expand
...
1
2
3
4
5
...