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We began analyzing https://link.springer.com/article/10.1007/s10719-015-9626-2, but it redirected us to https://link.springer.com/article/10.1007/s10719-015-9626-2. The analysis below is for the second page.

Title[redir]:
Human plasma protein N-glycosylation | Glycoconjugate Journal
Description:
Glycosylation is the most abundant and complex protein modification, and can have a profound structural and functional effect on the conjugate. The oligosaccharide fraction is recognized to be involved in multiple biological processes, and to affect proteins physical properties, and has consequentially been labeled a critical quality attribute of biopharmaceuticals. Additionally, due to recent advances in analytical methods and analysis software, glycosylation is targeted in the search for disease biomarkers for early diagnosis and patient stratification. Biofluids such as saliva, serum or plasma are of great use in this regard, as they are easily accessible and can provide relevant glycosylation information. Thus, as the assessment of protein glycosylation is becoming a major element in clinical and biopharmaceutical research, this review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-1-antitrypsin, alpha-1B-glycoprotein, alpha-2-HS-glycoprotein, alpha-2-macroglobulin, antithrombin-III, apolipoprotein B-100, apolipoprotein D, apolipoprotein F, beta-2-glycoprotein 1, ceruloplasmin, fibrinogen, immunoglobulin (Ig) A, IgG, IgM, haptoglobin, hemopexin, histidine-rich glycoprotein, kininogen-1, serotransferrin, vitronectin, and zinc-alpha-2-glycoprotein. In addition, the less abundant immunoglobulins D and E are included because of their major relevance in immunology and biopharmaceutical research. Where available, the glycosylation is described in a site-specific manner. In the discussion, we put the glycosylation of individual proteins into perspective and speculate how the individual proteins may contribute to a total plasma N-glycosylation profile determined at the released glycan level.

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Keywords {🔍}

pubmed, google, scholar, cas, article, asn, glycosylation, human, plasma, protein, ags, central, amino, nglycosylation, structures, analysis, glycoprotein, igg, sites, acid, glycans, site, biol, levels, found, diantennary, immunoglobulin, mass, chem, serum, acids, species, apolipoprotein, res, reported, structure, kda, iga, triantennary, chain, mgml, sequence, fags, clin, glycan, binding, cell, type, fucosylation, role,

Topics {✒️}

low-energy collision-induced dissociation obtained collision-induced dissociation electron-transfer dissociation small-angle x-ray scattering capillary hplc-esi-ms/ms ultrafiltration-based n-glycomics platform nano-lc-esi-ms combined cancer-resistant naked mole-rat asn-x-ser/thr sequon mass-selected site-specific core-fucosylation human high-molecular-mass kiniogen hplc/electrospray mass spectrometry brinkman-van der linden sequence asn87-asp-cys found called histidine-proline-rich glycoprotein article download pdf hydrophilic-interaction liquid chromatography β1-2-linked antennary n-acetylglucosamines glycopeptide lc-esi-quadrupole de la llera-moya sialic acid-linkage-specific stabilization abundance-ratio-based semiquantitative analysis serum/plasma n-glycome analysis site-specific n-glycosylation analysis n-glycosites enabling consistent tryptic glycopeptide lc-esi-ms asn-x-thr motif tf-adr versus hela uplc-esi tof ms high-throughput work flow site-specific glycoproteomics confirms asn-xaa-cys motif reducing end n-acetylglucosamine asn-x-ser/thr alpha-n-acetylneuraminyllactosyl-ceramide oxidized alpha-1-proteinase inhibitor negative acute-phase reactant asn-x-ser motif motif asn-x-ser ultraperformance liquid chromatography maldi-tof-ms analysis 400-mhz 1h-nmr spectroscopy tandem mass spectrometry rplc-esi-ms/ms h-meso-1 cell lines histidine-proline-rich glycoprotein williams-fitzgerald-flaujeac factor fat-depleting factor related β1-4-linked n-acetylglucosamine n-glycosylation consensus motif

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Interaction of mannan binding lectin with alpha2 macroglobulin via exposed oligomannose glycans: a conserved feature of the thiol ester protein family?

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WebPage:
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         headline:Human plasma protein N-glycosylation
         description:Glycosylation is the most abundant and complex protein modification, and can have a profound structural and functional effect on the conjugate. The oligosaccharide fraction is recognized to be involved in multiple biological processes, and to affect proteins physical properties, and has consequentially been labeled a critical quality attribute of biopharmaceuticals. Additionally, due to recent advances in analytical methods and analysis software, glycosylation is targeted in the search for disease biomarkers for early diagnosis and patient stratification. Biofluids such as saliva, serum or plasma are of great use in this regard, as they are easily accessible and can provide relevant glycosylation information. Thus, as the assessment of protein glycosylation is becoming a major element in clinical and biopharmaceutical research, this review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-1-antitrypsin, alpha-1B-glycoprotein, alpha-2-HS-glycoprotein, alpha-2-macroglobulin, antithrombin-III, apolipoprotein B-100, apolipoprotein D, apolipoprotein F, beta-2-glycoprotein 1, ceruloplasmin, fibrinogen, immunoglobulin (Ig) A, IgG, IgM, haptoglobin, hemopexin, histidine-rich glycoprotein, kininogen-1, serotransferrin, vitronectin, and zinc-alpha-2-glycoprotein. In addition, the less abundant immunoglobulins D and E are included because of their major relevance in immunology and biopharmaceutical research. Where available, the glycosylation is described in a site-specific manner. In the discussion, we put the glycosylation of individual proteins into perspective and speculate how the individual proteins may contribute to a total plasma N-glycosylation profile determined at the released glycan level.
         datePublished:2015-11-10T00:00:00Z
         dateModified:2015-11-10T00:00:00Z
         pageStart:309
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            Plasma
            Serum
            Glycoproteins
            Glycoproteomics
            Immunoglobulins
            Biochemistry
            general
            Pathology
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ScholarlyArticle:
      headline:Human plasma protein N-glycosylation
      description:Glycosylation is the most abundant and complex protein modification, and can have a profound structural and functional effect on the conjugate. The oligosaccharide fraction is recognized to be involved in multiple biological processes, and to affect proteins physical properties, and has consequentially been labeled a critical quality attribute of biopharmaceuticals. Additionally, due to recent advances in analytical methods and analysis software, glycosylation is targeted in the search for disease biomarkers for early diagnosis and patient stratification. Biofluids such as saliva, serum or plasma are of great use in this regard, as they are easily accessible and can provide relevant glycosylation information. Thus, as the assessment of protein glycosylation is becoming a major element in clinical and biopharmaceutical research, this review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-1-antitrypsin, alpha-1B-glycoprotein, alpha-2-HS-glycoprotein, alpha-2-macroglobulin, antithrombin-III, apolipoprotein B-100, apolipoprotein D, apolipoprotein F, beta-2-glycoprotein 1, ceruloplasmin, fibrinogen, immunoglobulin (Ig) A, IgG, IgM, haptoglobin, hemopexin, histidine-rich glycoprotein, kininogen-1, serotransferrin, vitronectin, and zinc-alpha-2-glycoprotein. In addition, the less abundant immunoglobulins D and E are included because of their major relevance in immunology and biopharmaceutical research. Where available, the glycosylation is described in a site-specific manner. In the discussion, we put the glycosylation of individual proteins into perspective and speculate how the individual proteins may contribute to a total plasma N-glycosylation profile determined at the released glycan level.
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         Glycoproteins
         Glycoproteomics
         Immunoglobulins
         Biochemistry
         general
         Pathology
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               name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
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               type:PostalAddress
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               type:PostalAddress
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      name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
      name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
      name:Department of Rheumatology, Leiden University Medical Center, Leiden, The Netherlands
      name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
      name:Division of BioAnalytical Chemistry, VU University Amsterdam, Amsterdam, The Netherlands

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