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001 978-90-481-3419-9
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020 _a9789048134199
_9978-90-481-3419-9
024 7 _a10.1007/978-90-481-3419-9
_2doi
050 4 _aR-RZ
072 7 _aMBGR
_2bicssc
072 7 _aMED000000
_2bisacsh
082 0 4 _a610
_223
100 1 _aNoll, Thomas.
_eeditor.
245 1 0 _aCells and Culture
_h[electronic resource] :
_bProceedings of the 20th ESACT Meeting, Dresden, Germany, June 17-20, 2007 /
_cedited by Thomas Noll.
264 1 _aDordrecht :
_bSpringer Netherlands :
_bImprint: Springer,
_c2010.
300 _aLIV, 800p.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _aESACT Proceedings ;
_v4
520 _aIt has been predicted that nearly half of all human proteins are glycosylated indicating the significance of glycoproteins in human health and disease. For example, the glycans attached to proteins have emerged as important biomarkers in the diagnosis of diseases such as cancers and play a significant role in how pathogenic viruses gain entry into human cells. The study of glycoproteins has now become a truly proteomic science. In the last few years, technology developments including in silico methods, high throughput separation and detection techniques have accelerated the characterization of glycoproteins in cells and tissues. Glyco-engineering coupled to rapid recombinant protein production has facilitated the determination of glycoprotein structures key to exploring and exploiting their functional roles. Each chapter in this volume is written by experts in the field and together provide a review of the state of the art in the emerging field of glycoproteomics.
650 0 _aMedicine.
650 1 4 _aBiomedicine.
650 2 4 _aBiomedicine general.
710 2 _aSpringerLink (Online service)
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9789048134182
830 0 _aESACT Proceedings ;
_v4
856 4 0 _uhttp://dx.doi.org/10.1007/978-90-481-3419-9
912 _aZDB-2-SBL
999 _c113345
_d113345