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10.1021/ac400398s http://scihub22266oqcxt.onion/10.1021/ac400398s C3713787!3713787!23682733     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Anal+Chem 2013 ; 85 (12): 5827-34 Nephropedia Template TP {{tp|p=23682733|t=2013. Using Glycinylation, a Chemical Derivatization Technique, for the Quantitation of Ubiquitinated Proteins |pdf=|usr=}}{{23682733}} gab.com Text Using Glycinylation, a Chemical Derivatization Technique, for the Quantitation of Ubiquitinated Proteins JO: Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=23682733 #FOAvip The quantitation of lysine post-translational modifications (PTMs) by bottom-up mass spectrometry is convoluted by the need for analogous derivatives and the production of different tryptic peptides from the unmodified and modified versions of a protein. Chemical derivatization of lysines prior to enzymatic digestion circumvents these problems and has proven to be a successful method for lysine PTM quantitation. The most notable example is the use of deuteroacetylation to quantitate lysine acetylation. In this work, levels of lysine ubiquitination were quantitated using a structurally homologous label that is chemically similar to the di-glycine (GlyGly)-tag, which is left at the ubiquitination site upon trypsinolysis. The LC-MS analysis of a chemically equivalent mono-glycine (Gly)-tag that is analogous to the corresponding GlyGly-tag proved that the mono-glycine tag can be used for the quantitation of ubiquitination. A glycinylation protocol was then established for the derivatization of proteins to label unmodified lysine residues with a single glycine tag. Ubiquitin multimers were used to show that after glycinylation and tryptic digestion, the mass spectrometric response from the corresponding analogous tagged peptides could be compared for relative quantitation. For a proof of principle regarding the applicability of this technique to the analysis of ubiquitination in biological samples, the glycinylation technique was used to quantitate the increase in mono-ubiquitinated histone H2B that is observed in yeast which lack the enzyme responsible for deubiquitinating H2B-K123, compared to wild-type yeast. Twit Text FOAVip Using Glycinylation, a Chemical Derivatization Technique, for the Quantitation of Ubiquitinated Proteins ????Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=23682733 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23682733 #FOAvip English Wikipedia <ref>{{Cite pmid|23682733}}</ref> Using Glycinylation, a Chemical Derivatization Technique, for the Quantitation of Ubiquitinated Proteins #MMPMID23682733 Fiedler KL; Cotter RJ Anal Chem 2013[Jun]; 85 (12): 5827-34 PMID23682733show ga The quantitation of lysine post-translational modifications (PTMs) by bottom-up mass spectrometry is convoluted by the need for analogous derivatives and the production of different tryptic peptides from the unmodified and modified versions of a protein. Chemical derivatization of lysines prior to enzymatic digestion circumvents these problems and has proven to be a successful method for lysine PTM quantitation. The most notable example is the use of deuteroacetylation to quantitate lysine acetylation. In this work, levels of lysine ubiquitination were quantitated using a structurally homologous label that is chemically similar to the di-glycine (GlyGly)-tag, which is left at the ubiquitination site upon trypsinolysis. The LC-MS analysis of a chemically equivalent mono-glycine (Gly)-tag that is analogous to the corresponding GlyGly-tag proved that the mono-glycine tag can be used for the quantitation of ubiquitination. A glycinylation protocol was then established for the derivatization of proteins to label unmodified lysine residues with a single glycine tag. Ubiquitin multimers were used to show that after glycinylation and tryptic digestion, the mass spectrometric response from the corresponding analogous tagged peptides could be compared for relative quantitation. For a proof of principle regarding the applicability of this technique to the analysis of ubiquitination in biological samples, the glycinylation technique was used to quantitate the increase in mono-ubiquitinated histone H2B that is observed in yeast which lack the enzyme responsible for deubiquitinating H2B-K123, compared to wild-type yeast. äUsing Glycinylation, a Chemical Derivatization Technique, for the Quan(epmc).pdf DeepDyve Pubget Overpricing