Thaysen-Andersen et al., 2013 - Google Patents
Structural analysis of glycoprotein sialylation–Part I: pre-LC-MS analytical strategiesThaysen-Andersen et al., 2013
View HTML- Document ID
- 11278141248296390728
- Author
- Thaysen-Andersen M
- Larsen M
- Packer N
- Palmisano G
- Publication year
- Publication venue
- Rsc Advances
External Links
Snippet
Sialic acids are carried by glycoproteins, proteoglycans and glycolipids as terminal entities of larger glycan structures and form a heterogeneous group of important monosaccharides in a wide range of biological systems in nature. Spatial and temporal structural …
- 102000003886 Glycoproteins 0 title abstract description 109
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
- G01N33/5308—Immunoassay; Biospecific binding assay for analytes not provided for elsewhere, e.g. nucleic acids, uric acid, worms, mites
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Thaysen-Andersen et al. | Structural analysis of glycoprotein sialylation–Part I: pre-LC-MS analytical strategies | |
Xiao et al. | Global and site‐specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry | |
Narimatsu et al. | Current technologies for complex glycoproteomics and their applications to biology/disease-driven glycoproteomics | |
Suttapitugsakul et al. | Recent advances in glycoproteomic analysis by mass spectrometry | |
Woo et al. | Development of IsoTaG, a chemical glycoproteomics technique for profiling intact N-and O-glycopeptides from whole cell proteomes | |
Halim et al. | Assignment of saccharide identities through analysis of oxonium ion fragmentation profiles in LC–MS/MS of glycopeptides | |
Palaniappan et al. | Chemical glycoproteomics | |
Shah et al. | Mass spectrometric analysis of sialylated glycans with use of solid-phase labeling of sialic acids | |
Chandler et al. | Glycomics and glycoproteomics of membrane proteins and cell‐surface receptors: Present trends and future opportunities | |
Fanayan et al. | Using lectins to harvest the plasma/serum glycoproteome | |
Miura et al. | Glycoblotting-assisted O-glycomics: ammonium carbamate allows for highly efficient O-glycan release from glycoproteins | |
Chen et al. | A universal chemical enrichment method for mapping the yeast N-glycoproteome by mass spectrometry (MS) | |
Jensen et al. | Mucin‐type O‐glycosylation–putting the pieces together | |
Kita et al. | Quantitative glycomics of human whole serum glycoproteins based on the standardized protocol for liberating N-glycans | |
Qin et al. | Proteomics analysis of O-GalNAc glycosylation in human serum by an integrated strategy | |
Brooks | Strategies for analysis of the glycosylation of proteins: current status and future perspectives | |
Dai et al. | Lectin‐based glycoproteomics to explore and analyze hepatocellular carcinoma‐related glycoprotein markers | |
Lazar et al. | Recent advances in the MS analysis of glycoproteins: Theoretical considerations | |
Brandi et al. | Advances in enrichment methods for mass spectrometry-based proteomics analysis of post-translational modifications | |
Yang et al. | Modification of sialic acids on solid phase: accurate characterization of protein sialylation | |
Wang et al. | Simultaneous release and labeling of O-and N-glycans allowing for rapid glycomic analysis by online LC-UV-ESI-MS/MS | |
Waniwan et al. | Glycoproteomic alterations in drug-resistant nonsmall cell lung cancer cells revealed by lectin magnetic nanoprobe-based mass spectrometry | |
Shajahan et al. | Tool for rapid analysis of glycopeptide by permethylation via one-pot site mapping and glycan analysis | |
Li et al. | Characterization of cell glycocalyx with mass spectrometry methods | |
Chen et al. | Highly efficient enrichment of O-GlcNAc glycopeptides based on chemical oxidation and reversible hydrazide chemistry |