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10.2183/pjab.93.005 http://scihub22266oqcxt.onion/10.2183/pjab.93.005 C5422628!5422628 !28190870     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28190870 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Proc+Jpn+Acad+Ser+B+Phys+Biol+Sci 2017 ; 93 (2 ): 64-86 Nephropedia Template TP {{tp|p=28190870 |t=2017. The complexity of glycoprotein-derived glycans |pdf=|usr=}}{{28190870 }} gab.com Text The complexity of glycoprotein-derived glycans JO: Proc Jpn Acad Ser B Phys Biol Sci http://www.kidney.de/pget.php?&tw=1&pmid=28190870 #FOAvip A brief review is presented of our studies on the structure of glycoprotein-derived glycans. The emphasis is on the introduction of high-resolution (1)H-NMR spectroscopy for the unambiguous determination of primary structures. For this purpose, we developed the structural reporter group concept. Structural reporters are defined as unique markers of structural elements in the NMR spectra. Application of this concept led to the discovery of numerous new structures. Furthermore, a number of structures presented in the literature could be corrected. The results are relevant for insight in the various steps in glycan metabolism in health and disease, for the function and mode of action of glycans in vivo and for the interpretation of structural information obtained through other techniques. The strength of the approach is further shown for several highly complex glycoproteins, carrying very heterogeneous and complicated glycans. Twit Text FOAVip The complexity of glycoprotein-derived glycans ????Proc Jpn Acad Ser B Phys Biol Sci http://www.kidney.de/pget.php?&tw=1&pmid=28190870 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28190870 #FOAvip English Wikipedia <ref>{{Cite pmid|28190870 }}</ref> The complexity of glycoprotein-derived glycans #MMPMID28190870 Vliegenthart JF Proc Jpn Acad Ser B Phys Biol Sci 2017[]; 93 (2 ): 64-86 PMID28190870 show ga A brief review is presented of our studies on the structure of glycoprotein-derived glycans. The emphasis is on the introduction of high-resolution (1)H-NMR spectroscopy for the unambiguous determination of primary structures. For this purpose, we developed the structural reporter group concept. Structural reporters are defined as unique markers of structural elements in the NMR spectra. Application of this concept led to the discovery of numerous new structures. Furthermore, a number of structures presented in the literature could be corrected. The results are relevant for insight in the various steps in glycan metabolism in health and disease, for the function and mode of action of glycans in vivo and for the interpretation of structural information obtained through other techniques. The strength of the approach is further shown for several highly complex glycoproteins, carrying very heterogeneous and complicated glycans. |Animals [MESH] |Glycoproteins/*chemistry [MESH] |Humans [MESH] |Magnetic Resonance Spectroscopy [MESH] |Mass Spectrometry [MESH] |Polysaccharides/*chemistry [MESH]The complexity of glycoprotein-derived glycans (epmc).pdf DeepDyve Pubget Overpricing