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Elucidating heterogeneity of IgA1 hinge-region O-glycosylation by use of MALDI-TOF/TOF mass spectrometry: Role of cysteine alkylation during sample processing

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33147879" target="_blank" >RIV/61989592:15310/13:33147879 - isvavai.cz</a>

  • Alternative codes found

    RIV/60162694:G44__/13:43875042

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.jprot.2013.07.013" target="_blank" >http://dx.doi.org/10.1016/j.jprot.2013.07.013</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.jprot.2013.07.013" target="_blank" >10.1016/j.jprot.2013.07.013</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Elucidating heterogeneity of IgA1 hinge-region O-glycosylation by use of MALDI-TOF/TOF mass spectrometry: Role of cysteine alkylation during sample processing

  • Original language description

    Determining disease-associated changes in protein glycosylation provides a better understanding of pathogenesis. This work focuses on human immunoglobulin A1 (IgA1), where aberrant O-glycosylation plays a key role in the pathogenesis of IgA nephropathy (IgAN). Normal IgA1 hinge region carries 3 to 6 O-glycans consisting of N-acetylgalactosamine (GalNAc) and galactose (Gal); both sugars may be sialylated. In IgAN patients, some O-glycans on a fraction of IgA1 molecules are Gal-deficient. Here we describea sample preparation protocol with optimized cysteine alkylation of a Gal-deficient polymeric IgA1 myeloma protein prior to in-gel digestion and analysis of the digest by MALDI-TOF/TOF mass spectrometry (MS). Following a novel strategy, IgA1 hinge-region O-glycopeptides were fractionated by reversed-phase liquid chromatography using a microgradient device and identified by MALDI-TOF/TOF tandem MS (MS/MS). The acquired MS/MS spectra were interpreted manually and by means of our own softw

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Proteomics

  • ISSN

    1874-3919

  • e-ISSN

  • Volume of the periodical

    92

  • Issue of the periodical within the volume

    OCT

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    14

  • Pages from-to

    299-312

  • UT code for WoS article

    000328518000021

  • EID of the result in the Scopus database