ProMoST (Protein Modification Screening Tool): a web-based tool for mapping protein modifications on two-dimensional gels Export

@article{citeulike:4948430, abstract = {ProMoST is a flexible web tool that calculates the effect of single or multiple posttranslational modifications (PTMs) on protein isoelectric point (pI) and molecular weight and displays the calculated patterns as two-dimensional (2D) gel images. PTMs of proteins control many biological regulatory and signaling mechanisms and 2D gel electrophoresis is able to resolve many PTM-induced isoforms, such as those due to phosphorylation, acetylation, deamination, alkylation, cysteine oxidation or tyrosine nitration. These modifications cause changes in the pI of the protein by adding, removing or changing titratable groups. Proteins differ widely in buffering capacity and pI and therefore the same PTMs may give rise to quite different patterns of pI shifts in different proteins. It is impossible by visual inspection of a pattern of spots on a gel to determine which modifications are most likely to be present. The patterns of PTM shifts for different proteins can be calculated and are often quite distinctive. The theoretical gel images produced by ProMoST can be compared to the experimental 2D gel results to implicate probable PTMs and focus efforts on more detailed study of modified proteins. ProMoST has been implemented as cgi script in Perl available on a WWW server at http://proteomics.mcw.edu/promost. 10.1093/nar/gkh356}, author = {Halligan, Brian D. and Ruotti, Victor and Jin, Weihong and Laffoon, Scott and Twigger, Simon N. and Dratz, Edward A.}, citeulike-article-id = {4948430}, citeulike-linkout-0 = {http://dx.doi.org/10.1093/nar/gkh356}, citeulike-linkout-1 = {http://nar.oxfordjournals.org/cgi/content/abstract/32/suppl_2/W638}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/15215467}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=15215467}, day = {1}, doi = {10.1093/nar/gkh356}, journal = {Nucl. Acids Res.}, keywords = {h, method}, month = {July}, number = {suppl\_2}, pages = {W638--644}, posted-at = {2009-06-24 23:24:00}, priority = {2}, title = {ProMoST (Protein Modification Screening Tool): a web-based tool for mapping protein modifications on two-dimensional gels}, url = {http://dx.doi.org/10.1093/nar/gkh356}, volume = {32}, year = {2004} }

TY - JOUR ID - citeulike:4948430 L3 - citeulike-article-id:4948430 N2 - ProMoST is a flexible web tool that calculates the effect of single or multiple posttranslational modifications (PTMs) on protein isoelectric point (pI) and molecular weight and displays the calculated patterns as two-dimensional (2D) gel images. PTMs of proteins control many biological regulatory and signaling mechanisms and 2D gel electrophoresis is able to resolve many PTM-induced isoforms, such as those due to phosphorylation, acetylation, deamination, alkylation, cysteine oxidation or tyrosine nitration. These modifications cause changes in the pI of the protein by adding, removing or changing titratable groups. Proteins differ widely in buffering capacity and pI and therefore the same PTMs may give rise to quite different patterns of pI shifts in different proteins. It is impossible by visual inspection of a pattern of spots on a gel to determine which modifications are most likely to be present. The patterns of PTM shifts for different proteins can be calculated and are often quite distinctive. The theoretical gel images produced by ProMoST can be compared to the experimental 2D gel results to implicate probable PTMs and focus efforts on more detailed study of modified proteins. ProMoST has been implemented as cgi script in Perl available on a WWW server at http://proteomics.mcw.edu/promost. 10.1093/nar/gkh356 IS - suppl_2 JF - Nucl. Acids Res. EP - 644 TI - ProMoST (Protein Modification Screening Tool): a web-based tool for mapping protein modifications on two-dimensional gels VL - 32 SP - W638 KW - h KW - method AU - Halligan, Brian AU - Ruotti, Victor AU - Jin, Weihong AU - Laffoon, Scott AU - Twigger, Simon AU - Dratz, Edward PY - 2004/07/01/ UR - http://dx.doi.org/10.1093/nar/gkh356 ER -