Literature DB >> 28150244

Bioinformatics Analysis of Functional Associations of PTMs.

Pablo Minguez1, Peer Bork2,3.   

Abstract

Post-translational modifications (PTMs) are an important source of protein regulation; they fine-tune the function, localization, and interaction with other molecules of the majority of proteins and are partially responsible for their multifunctionality. Usually, proteins have several potential modification sites, and their patterns of occupancy are associated with certain functional states. These patterns imply cross talk among PTMs within and between proteins, the majority of which are still to be discovered. Several methods detect associations between PTMs; these have recently combined into a global resource, the PTMcode database, which contains already known and predicted functional associations between pairs of PTMs from more than 45,000 proteins in 19 eukaryotic species.

Keywords:  Post-translational modifications; Protein regulation; Protein–protein interactions; Proteomics; Systems biology

Mesh:

Substances:

Year:  2017        PMID: 28150244     DOI: 10.1007/978-1-4939-6783-4_14

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  2 in total

Review 1.  Proteomics of Long-Lived Mammals.

Authors:  Gregory Tombline; Jonathan Gigas; Nicholas Macoretta; Max Zacher; Stephan Emmrich; Yang Zhao; Andrei Seluanov; Vera Gorbunova
Journal:  Proteomics       Date:  2020-01-09       Impact factor: 3.984

2.  Identification of Urinary Biomarkers for Exercise-Induced Immunosuppression by iTRAQ Proteomics.

Authors:  Guoqin Xu; Wentao Lin; Andrew J McAinch; Xu Yan; Xiquan Weng
Journal:  Biomed Res Int       Date:  2020-01-23       Impact factor: 3.411

  2 in total

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