ProteoModlR for functional proteomic analysis.

ABSTRACT:

Background

High-accuracy mass spectrometry enables near comprehensive quantification of the components of the cellular proteomes, increasingly including their chemically modified variants. Likewise, large-scale libraries of quantified synthetic peptides are becoming available, enabling absolute quantification of chemically modified proteoforms, and therefore systems-level analyses of changes of their absolute abundance and stoichiometry. Existing computational methods provide advanced tools for mass spectral analysis and statistical inference, but lack integrated functions for quantitative analysis of post-translationally modified proteins and their modification stoichiometry.

Results

Here, we develop ProteoModlR, a program for quantitative analysis of abundance and stoichio

SUBMITTER: Cifani P 

PROVIDER: S-EPMC5336658 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature