02064nas a2200253   4500008004100000022001400041245013500055210006900190260009300259300001200352490000700364520103800371653004301409653003301452653001301485653003701498100002501535700002301560700002401583700002501607700002301632700002501655856013001680       2012                        eng d  a1469-066700aZoom-in - a targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry0 aZoomin a targeted database search for identification of glycatio  a6 CHARLTON MILL, CHARLTON, CHICHESTER,, W SUSSEX PO18 0HY, ENGLANDbIM PUBLICATIONScJAN  a475-4810 v183 a<p>Post-translational modifications (PTMs) are very important to biological function, however their identification and characterization is technically challenging. In this study, we have identified glycation modifications by nano LC-MSE, a data independent acquisition work flow, followed by database search using the Protein Lynx Global Server (PLGS). PLGS search with a complete human protein database hardly identified glycation modifications in a glycated human serum albumin (HSA), which was detected to be glycated by western blotting with advanced glycation end products (AGE) antibody and fluorescence spectroscopy. To overcome this difficulty, ``Zoom-In'' approach, a targeted database search was used to identify glycation modifications in a glycated HSA, which were further manually validated. This approach was useful for identification of glycation modifications from untargeted tandem mass spectrometry workflow such as MSE, but may require the development of a new algorithm or an upgrade of the existing software.</p>10aadvanced glycation end products (AGEs)10adata independent acquisition10aDiabetes10apost-translational modifications1 aBhonsle, Hemangi, S.1 aKorwar, Arvind, M.1 aKesavan, Suresh, K.1 aBhosale, Santosh, D.1 aBansode, Sneha, B.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/zoom-targeted-database-search-identification-glycation-modifications-analyzed-untargeted-0