GPM #: Keyword: # GPM # proteins Description 1. GPM33080000351 peptide model gel aaa go mh 1123 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastGluC_Dtree2. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 2. GPM33080000364 peptide model gel aaa go mh 1158 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastGluC_Dtree3. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 3. GPM33080000376 peptide model gel aaa go mh 1277 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastGluC_Dtree. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 4. GPM33080000389 peptide model gel aaa go mh 1099 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastArgC_Dtree. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 5. GPM33080000402 peptide model gel aaa go mh 1299 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastArgC_Dtree2. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 6. GPM33080000415 peptide model gel aaa go mh 1326 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastArgC_Dtree3. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 7. GPM33080000428 peptide model gel aaa go mh 1322 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastAspN_Dtree. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 8. GPM33080000441 peptide model gel aaa go mh 1369 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastAspN_Dtree2. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 9. GPM33080000467 peptide model gel aaa go mh 1381 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastAspN_Dtree3. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 10. GPM33080000480 peptide model gel aaa go mh 1492 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastLysC_Dtree. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 11. GPM33080000494 peptide model gel aaa go mh 1502 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastLysC_Dtree2. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 12. GPM33080000507 peptide model gel aaa go mh 1510 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastLysC_Dtree3. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 13. GPM33080000519 peptide model gel aaa go mh 1266 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastTryp2_Dtree. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 14. GPM33080000532 peptide model gel aaa go mh 1365 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastTryp2_Dtree2. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. 15. GPM33080000545 peptide model gel aaa go mh 1376 BRENDA cell culture: none BRENDA tissue: none CELL cell type: none GO subcellular: GO:0005623  email: institution: University of Wisconson name: Danielle Swaney, Josh Coon, et al. project: The value of using multiple proteases for large-scale mass spectrometry-based proteomics project comment: Tranche  Large-scale protein sequencing methods rely on enzymatic digestion of complex protein mixtures to generate a collection of peptides for mass spectrometric analysis. Here we examine the use of multiple proteases (trypsin, LysC, ArgC, AspN, and GluC) to improve both protein identification and characterization in the model organism Saccharomyces cerevisiae. Data set: yeastTryp2_Dtree3. PubMed, J. Proteome Research (2009) DOI: 10.1021/pr900863u. Page 1 of 1 | 1 | Key word(s): 20113005 Total protein ids = 19865 If you do not see a red dot in the square brackets [], you will need Adobe's SVG plugin to view this site properly.

dblist_gpmnotes.pl, v. 2010.07.06