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Proteome-wide selected reaction monitoring assays for the human pathogen Streptococcus pyogenes.

Karlsson, Christofer LU ; Malmström, Lars LU ; Aebersold, Ruedi and Malmström, Johan LU (2012) In Nature Communications 3.
Abstract
Selected reaction monitoring mass spectrometry (SRM-MS) is a targeted proteomics technology used to identify and quantify proteins with high sensitivity, specificity and high reproducibility. Execution of SRM-MS relies on protein-specific SRM assays, a set of experimental parameters that requires considerable effort to develop. Here we present a proteome-wide SRM assay repository for the gram-positive human pathogen group A Streptococcus. Using a multi-layered approach we generated SRM assays for 10,412 distinct group A Streptococcus peptides followed by extensive testing of the selected reaction monitoring assays in >200 different group A Streptococcus protein pools. Based on the number of SRM assay observations we created a rule-based... (More)
Selected reaction monitoring mass spectrometry (SRM-MS) is a targeted proteomics technology used to identify and quantify proteins with high sensitivity, specificity and high reproducibility. Execution of SRM-MS relies on protein-specific SRM assays, a set of experimental parameters that requires considerable effort to develop. Here we present a proteome-wide SRM assay repository for the gram-positive human pathogen group A Streptococcus. Using a multi-layered approach we generated SRM assays for 10,412 distinct group A Streptococcus peptides followed by extensive testing of the selected reaction monitoring assays in >200 different group A Streptococcus protein pools. Based on the number of SRM assay observations we created a rule-based selected reaction monitoring assay-scoring model to select the most suitable assays per protein for a given cellular compartment and bacterial state. The resource described here represents an important tool for deciphering the group A Streptococcus proteome using selected reaction monitoring and we anticipate that concepts described here can be extended to other pathogens. (Less)
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publication status
published
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in
Nature Communications
volume
3
publisher
Nature Publishing Group
external identifiers
  • wos:000316356700068
  • pmid:23250431
  • scopus:84871791617
ISSN
2041-1723
DOI
10.1038/ncomms2297
language
English
LU publication?
yes
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a163a2b0-873b-4662-8076-f3c20d923e97 (old id 3347082)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/23250431?dopt=Abstract
date added to LUP
2013-01-06 14:16:16
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2017-11-19 03:45:20
@article{a163a2b0-873b-4662-8076-f3c20d923e97,
  abstract     = {Selected reaction monitoring mass spectrometry (SRM-MS) is a targeted proteomics technology used to identify and quantify proteins with high sensitivity, specificity and high reproducibility. Execution of SRM-MS relies on protein-specific SRM assays, a set of experimental parameters that requires considerable effort to develop. Here we present a proteome-wide SRM assay repository for the gram-positive human pathogen group A Streptococcus. Using a multi-layered approach we generated SRM assays for 10,412 distinct group A Streptococcus peptides followed by extensive testing of the selected reaction monitoring assays in >200 different group A Streptococcus protein pools. Based on the number of SRM assay observations we created a rule-based selected reaction monitoring assay-scoring model to select the most suitable assays per protein for a given cellular compartment and bacterial state. The resource described here represents an important tool for deciphering the group A Streptococcus proteome using selected reaction monitoring and we anticipate that concepts described here can be extended to other pathogens.},
  articleno    = {1301},
  author       = {Karlsson, Christofer and Malmström, Lars and Aebersold, Ruedi and Malmström, Johan},
  issn         = {2041-1723},
  language     = {eng},
  publisher    = {Nature Publishing Group},
  series       = {Nature Communications},
  title        = {Proteome-wide selected reaction monitoring assays for the human pathogen Streptococcus pyogenes.},
  url          = {http://dx.doi.org/10.1038/ncomms2297},
  volume       = {3},
  year         = {2012},
}