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Structural and site-specific characterization of distinctiveNglycans with heavy fucosylation in human semen

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F25%3A43910164" target="_blank" >RIV/60076658:12520/25:43910164 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1016/j.carpta.2025.100941" target="_blank" >https://doi.org/10.1016/j.carpta.2025.100941</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.carpta.2025.100941" target="_blank" >10.1016/j.carpta.2025.100941</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural and site-specific characterization of distinctiveNglycans with heavy fucosylation in human semen

  • Original language description

    Heavy fucosylation (fucose residues &gt;= 6 per glycan) has been previously reported in human semen with unclear precise site-specific glycan structures. In current study, we characterized heavily fucosylated glycoproteins as a distinctive feature of human spermatozoa (HS) and seminal plasma (HSP), with a precise definition of glycan structural features at the glycosite-specific level. There were 49 unique heavily fucosylated intact glycopeptides (IGPs) at 15 N-glycosites from 12 glycoproteins identified in HS, and 188 unique heavily fucosylated IGPs at 58 N-glycosites from 37 glycoproteins in HSP. Among these heavily fucosylated glycoproteins, 10 were shared in HS and HSP, 2 were detected only in HS and 17 only in HSP. Almost all heavily fucosylated glycans were complex Nglycans with core fucosylation and Lewis antennary, among which CLU were glycosylated by ten and nine fucoses per glycan in HS and HSP, respectively. Moreover, these heavily fucosylated glycans varied from tri- to hexa-antennas. Notably, the N-glycan structures on shared heavily fucosylated glycoproteins were more complex in HSP than in HS. These heavily fucosylated glycoproteins identified in human semen represent a valuable and distinctive resource for glycopeptide studies, offering significant potential for advancing glycoproteomic methodologies and clinical research into male infertility.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10601 - Cell biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Carbohydrate Polymer Technologies and Applications

  • ISSN

    2666-8939

  • e-ISSN

    2666-8939

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    neuvedeno

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    11

  • Pages from-to

    nestránkováno

  • UT code for WoS article

    001539168300001

  • EID of the result in the Scopus database

    2-s2.0-105010588191