We are analyzing https://link.springer.com/article/10.1007/s10719-015-9626-2.

Title:
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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

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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

Questions {❓}

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

Schema {🗺️}

WebPage:
      mainEntity:
         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
         pageEnd:343
         sameAs:https://doi.org/10.1007/s10719-015-9626-2
         keywords:
             N-glycosylation
            Plasma
            Serum
            Glycoproteins
            Glycoproteomics
            Immunoglobulins
            Biochemistry
            general
            Pathology
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                        type:PostalAddress
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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.
      datePublished:2015-11-10T00:00:00Z
      dateModified:2015-11-10T00:00:00Z
      pageStart:309
      pageEnd:343
      sameAs:https://doi.org/10.1007/s10719-015-9626-2
      keywords:
          N-glycosylation
         Plasma
         Serum
         Glycoproteins
         Glycoproteomics
         Immunoglobulins
         Biochemistry
         general
         Pathology
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         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs10719-015-9626-2/MediaObjects/10719_2015_9626_Fig1_HTML.gif
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            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
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      author:
            name:Florent Clerc
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                     type:PostalAddress
                  type:Organization
            type:Person
            name:Karli R. Reiding
            affiliation:
                  name:Leiden University Medical Center
                  address:
                     name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Bas C. Jansen
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                  name:Leiden University Medical Center
                  address:
                     name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
                     type:PostalAddress
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            type:Person
            name:Guinevere S. M. Kammeijer
            affiliation:
                  name:Leiden University Medical Center
                  address:
                     name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
                     type:PostalAddress
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            type:Person
            name:Albert Bondt
            affiliation:
                  name:Leiden University Medical Center
                  address:
                     name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
                     type:PostalAddress
                  type:Organization
                  name:Leiden University Medical Center
                  address:
                     name:Department of Rheumatology, Leiden University Medical Center, Leiden, The Netherlands
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Manfred Wuhrer
            affiliation:
                  name:Leiden University Medical Center
                  address:
                     name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
                     type:PostalAddress
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                  name:VU University Amsterdam
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         type:PostalAddress
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         name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
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      address:
         name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
         type:PostalAddress
      name:Leiden University Medical Center
      address:
         name:Department of Rheumatology, Leiden University Medical Center, Leiden, The Netherlands
         type:PostalAddress
      name:Leiden University Medical Center
      address:
         name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
         type:PostalAddress
      name:VU University Amsterdam
      address:
         name:Division of BioAnalytical Chemistry, VU University Amsterdam, Amsterdam, The Netherlands
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Person:
      name:Florent Clerc
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            name:Leiden University Medical Center
            address:
               name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
               type:PostalAddress
            type:Organization
      name:Karli R. Reiding
      affiliation:
            name:Leiden University Medical Center
            address:
               name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
               type:PostalAddress
            type:Organization
      name:Bas C. Jansen
      affiliation:
            name:Leiden University Medical Center
            address:
               name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
               type:PostalAddress
            type:Organization
      name:Guinevere S. M. Kammeijer
      affiliation:
            name:Leiden University Medical Center
            address:
               name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
               type:PostalAddress
            type:Organization
      name:Albert Bondt
      affiliation:
            name:Leiden University Medical Center
            address:
               name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
               type:PostalAddress
            type:Organization
            name:Leiden University Medical Center
            address:
               name:Department of Rheumatology, Leiden University Medical Center, Leiden, The Netherlands
               type:PostalAddress
            type:Organization
      name:Manfred Wuhrer
      affiliation:
            name:Leiden University Medical Center
            address:
               name:Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands
               type:PostalAddress
            type:Organization
            name:VU University Amsterdam
            address:
               name:Division of BioAnalytical Chemistry, VU University Amsterdam, Amsterdam, The Netherlands
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      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: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: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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