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Computational prediction of proteotypic peptides for quantitative proteomics

Article Abstract:

The characteristic physicochemical properties of proteolytic peptides are used to build a computational tool that can predict proteolytic peptides for any protein from any organism, for a given platform, with greater than 85% cumulative accuracy. The applications of proteolytic peptides have included the validation of protein identifications, absolute quantification of proteins, and annotation of coding sequences in genomes and characterization of the physical principles governing key elements of mass spectrometric workflows.

Author: Aebersold, Ruedi, Martin, Daniel, Raught, Brian, Kuster, Bernhard, Mallick, Parag, Schirle, Markus, Chen, Sharon S., Flory, Mark R., Hookeun Lee, Ranish, Jeffrey, Schmitt, Robert, Werner, Thilo
Publisher: Nature Publishing Co.
Publication Name: Nature Biotechnology
Subject: Business
ISSN: 1087-0156
Year: 2007
Polypeptides, Amino acid sequence, Amino acid sequencing, Properties, Chemical properties

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Identification of post-translational modifications by blind search of mass spectra

Article Abstract:

An unrestrictive post-translational modifications (PTMs) search algorithm, Mass spectrometry (MS)-alignment, that searches for all types of PTMs at once in a blind mode, that is, without knowing which PTMs exist in nature is described. Blind PTM identification makes it possible to study the extent and frequency of different types of PTMs and application of this approach to lens proteins resulted in the largest set of PTMs reported in human crystallins.

Author: Tsur, Dekel, Tanner, Stephen, Zandi, Ebrahim, Bafna, Vineet, Pevzner, Pavel A.
Publisher: Nature Publishing Co.
Publication Name: Nature Biotechnology
Subject: Business
ISSN: 1087-0156
Year: 2005
United States, Protein research

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Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor

Article Abstract:

Mass spectrometry (MS) analysis is applicable to a broad range of biological analytes and has the important advantage that it does not require analytes to be labeled. This method is used to screen a chemical library against protese activity of anthrax lethal factor and report a compound that inhibits lethal factor activity with a K(Sub i) of 1.1 muM and blocks the cleavage of MEK1 in 293 cells.

Author: Min, Dal-Hee, Tang, Wei-Jen, Mrksich, Milan
Publisher: Nature Publishing Co.
Publication Name: Nature Biotechnology
Subject: Business
ISSN: 1087-0156
Year: 2004
Lethal mutation, Anthrax

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Subjects list: Analysis, Mass spectrometry, Proteomics, Research
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