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: A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database. | Open Access Software A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database José L Jimenez Bjorn Hegemann James RA Hutchins Jan-Michael Peters and Richard Durbin Addresses Wellcome Trust Sanger Institute Genome Campus Hinxton Cambridge CB10 1SA UK. Research Institute of Molecular Pathology IMP Dr. Bohr-Gasse 7 1030 Vienna Austria. Correspondence José L Jimenez. Email j_l_jimenez71@ Published 23 May 2007 Genome Biology 2007 8 R90 doi 186 gb-2007-8-5-r90 The electronic version of this article is the complete one and can be found online at http 2007 8 5 R90 Received 3 January 2007 Revised 3 April 2007 Accepted 23 May 2007 2007 Jimenez 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 mtcPTM is an online repository of human and mouse phosphosites in which data are hierarchically organized to preserve biologically relevant experimental information thus allowing straightforward comparisons of phosphorylation patterns found under different conditions. The database also contains the largest available collection of atomic models of phosphorylatable proteins. Detailed analysis of this structural dataset reveals that phosphorylation sites are found in a heterogeneous range of structural and sequence contexts. mtcPTM is available on the web http cgi-bin mtcPTM search. Rationale In recent years several sequencing projects have revealed the complete transcriptomes and proteomes for a number of organisms including human 1 2 . The current challenge is to place this information within the dynamic context of the cell in order to elucidate how individual molecules interact to achieve the complex behavior of cellular processes
