tailieunhanh - Báo cáo y học: " PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. | Open Access PHOSIDA phosphorylation site database management structural and evolutionary investigation and prediction of phosphosites Florian Gnad Shubin Ren Juergen Cox Jesper V Olsen Boris Macek Mario Oroshi and Matthias Mann Address Department for Proteomics and Signal Transduction Max-Planck Institute for Biochemistry Am Klopferspitz D-82152 Martinsried Germany. Correspondence Matthias Mann. Email mmann@ Published 26 November 2007 Genome Biology 2007 8 R250 doi gb-2007-8- 11-r250 The electronic version of this article is the complete one and can be found online at http 2007 8 ll R250 Received 29 June 2007 Revised 8 August 2007 Accepted 26 November 2007 2007 Gnad et al. licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract PHOSIDA http a phosphorylation site database integrates thousands of high-confidence in vivo phosphosites identified by mass spectrometry-based proteomics in various species. For each phosphosite PHOSIDA lists matching kinase motifs predicted secondary structures conservation patterns and its dynamic regulation upon stimulus. Using support vector machines PHOSIDA also predicts phosphosites. Rationale Protein phosphorylation is a ubiquitous and important post-translational modification responsible for modulating protein function localization interaction and stability 1-4 . High-throughput experimental studies such as our recent large scale analysis of the human phosphoproteome by quantitative mass spectrometry in which we measured the time courses of more than 6 600 phosphorylation sites in response to growth factor stimulation 5 enable us to study biological systems from a global perspective. Those sites were identified by high resolution mass