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- W2169142034 abstract "Glycosylation is one of the most common and structurally diverse posttranslational modifications of proteins. Given that protein glycosylation is involved in various cellular processes, the characterization of site-specific Nand O-linked glycosylations is becoming increasingly important. However, current mass spectrometry-based technologies, i.e. proteomics and glycomics, are unable to resolve the site-specific glycosylation pattern of glycoproteins. The primary aim of this thesis was to develop glycoproteomic techniques for mass spectrometric analysis of glycoproteins. A sialic acid captureand-release method, based on hydrazide chemistry, for selective enrichment of Nand O-linked glycopeptides from complex biological samples was developed. Enriched glycopeptides were separated by reversed phase liquid chromatography and analyzed by Fourier transform ion cyclotron mass spectrometry (FTICR MS) utilizing collision induced dissociation (CID) and electron capture dissociation (ECD) fragmentation techniques. Initially, both Nand O-glycopeptides from sialylated glycoproteins of human cerebrospinal fluid (CSF) were enriched and characterized. Subsequently, a targeted O-glycoproteomics approach was developed, allowing for sequence analysis of preferred O-glycosylation sites of glycoproteins. The applicability of the sialic acid capture-and-release strategy was further demonstrated for human urine, a technically more challenging biological fluid. The LC-MS/MS analyses revealed unique Nand O-glycosylations, many of which were previously unknown, both for CSF and urinary glycoproteins. In e.g. CSF, a series of O-glycopeptides with Thr linked O-glycans in the vicinity of the β-secretase cleavage site of the amyloid precursor protein (APP) were identified. Additionally, amyloid beta (Aβ) peptides, originating from APP, were immunoprecipitated from CSF samples for a targeted glycoproteomic analysis. These analyses revealed that a series of Aβ peptides were uniquely modified with sialylated O-glycans at a specific Tyr residue. A relative increase of such Tyr O-glycosylated Aβ peptides was observed in CSF samples from Alzheimer’s disease (AD) patients compared to nonAD patients, suggesting that these Aβ glycopeptides may potentially be used as biomarkers of AD." @default.
- W2169142034 created "2016-06-24" @default.
- W2169142034 creator A5049912825 @default.
- W2169142034 date "2012-02-10" @default.
- W2169142034 modified "2023-09-27" @default.
- W2169142034 title "Targeting the human glycoproteome New enrichment protocols and mass spectrometric analyses reveal unique and novel glycosylation sites" @default.
- W2169142034 cites W126606941 @default.
- W2169142034 cites W1418975799 @default.
- W2169142034 cites W145329232 @default.
- W2169142034 cites W1495926848 @default.
- W2169142034 cites W1505123947 @default.
- W2169142034 cites W1520029826 @default.
- W2169142034 cites W1529465329 @default.
- W2169142034 cites W1548285478 @default.
- W2169142034 cites W1566087596 @default.
- W2169142034 cites W1585241254 @default.
- W2169142034 cites W1604340849 @default.
- W2169142034 cites W1618025150 @default.
- W2169142034 cites W163727811 @default.
- W2169142034 cites W1835800556 @default.
- W2169142034 cites W1870828328 @default.
- W2169142034 cites W1943949390 @default.
- W2169142034 cites W1947454816 @default.
- W2169142034 cites W1957424016 @default.
- W2169142034 cites W1964850706 @default.
- W2169142034 cites W1967772572 @default.
- W2169142034 cites W1968896304 @default.
- W2169142034 cites W1969869303 @default.
- W2169142034 cites W1970052428 @default.
- W2169142034 cites W1971907885 @default.
- W2169142034 cites W1971983473 @default.
- W2169142034 cites W1972084678 @default.
- W2169142034 cites W1973632433 @default.
- W2169142034 cites W1973753936 @default.
- W2169142034 cites W1974732006 @default.
- W2169142034 cites W1974830441 @default.
- W2169142034 cites W1976115853 @default.
- W2169142034 cites W1976645829 @default.
- W2169142034 cites W1976897287 @default.
- W2169142034 cites W1976985227 @default.
- W2169142034 cites W1978268623 @default.
- W2169142034 cites W1979274827 @default.
- W2169142034 cites W1979474533 @default.
- W2169142034 cites W1979543098 @default.
- W2169142034 cites W1981447099 @default.
- W2169142034 cites W1981593008 @default.
- W2169142034 cites W1982655905 @default.
- W2169142034 cites W1982977832 @default.
- W2169142034 cites W1984596349 @default.
- W2169142034 cites W1988621302 @default.
- W2169142034 cites W1990350348 @default.
- W2169142034 cites W1991787417 @default.
- W2169142034 cites W1992066825 @default.
- W2169142034 cites W1992778614 @default.
- W2169142034 cites W1993000555 @default.
- W2169142034 cites W1993063472 @default.
- W2169142034 cites W1997292282 @default.
- W2169142034 cites W1997374000 @default.
- W2169142034 cites W2003148857 @default.
- W2169142034 cites W2003885329 @default.
- W2169142034 cites W2003926613 @default.
- W2169142034 cites W2004291187 @default.
- W2169142034 cites W2004627688 @default.
- W2169142034 cites W2004858523 @default.
- W2169142034 cites W2005093408 @default.
- W2169142034 cites W2007378287 @default.
- W2169142034 cites W2007646072 @default.
- W2169142034 cites W2007731313 @default.
- W2169142034 cites W2009605886 @default.
- W2169142034 cites W2010925911 @default.
- W2169142034 cites W2016870770 @default.
- W2169142034 cites W2017288068 @default.
- W2169142034 cites W2022754675 @default.
- W2169142034 cites W2023096047 @default.
- W2169142034 cites W2024191848 @default.
- W2169142034 cites W2025069411 @default.
- W2169142034 cites W2031119708 @default.
- W2169142034 cites W2031884770 @default.
- W2169142034 cites W2032179964 @default.
- W2169142034 cites W2032194486 @default.
- W2169142034 cites W2032920422 @default.
- W2169142034 cites W2033492963 @default.
- W2169142034 cites W2035347203 @default.
- W2169142034 cites W2036288989 @default.
- W2169142034 cites W2040484264 @default.
- W2169142034 cites W2040947654 @default.
- W2169142034 cites W2044340366 @default.
- W2169142034 cites W2044943436 @default.
- W2169142034 cites W2046847750 @default.
- W2169142034 cites W2051258411 @default.
- W2169142034 cites W2053697292 @default.
- W2169142034 cites W2055537573 @default.
- W2169142034 cites W2056181922 @default.
- W2169142034 cites W2058570072 @default.
- W2169142034 cites W2059282001 @default.
- W2169142034 cites W2060813860 @default.
- W2169142034 cites W2062311239 @default.
- W2169142034 cites W2062734474 @default.
- W2169142034 cites W2064140463 @default.
- W2169142034 cites W2064347820 @default.