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Showing 1–7 of 7 results
Advanced filters: Author: Martina Mühlenhoff Clear advanced filters

  • Sialic acid O-acetylation occurs in the Golgi apparatus and is catalyzed by CASD1, a multi-pass transmembrane protein. Here, the authors reveal that SLC33A1 delivers acetyl-CoA to the luminal catalytic domain of CASD1, while a catalytic transmembrane tunnel enables SLC33A1-independent O-acetylation.

    • Malena Albers
    • Lydia Bosse
    • Martina Mühlenhoff
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-19

  • Neisseria meningitidis capsular polysaccharide (CPS) is a major virulence factor and vaccine formulations against Neisseria meningitidis serogroup A (NmA) contain O-acetylated CPS. Here, the authors provide mechanistic insights into CPS O-acetylation in NmA by determining the crystal structure of the O-acetyltransferase CsaC and NMR measurements further reveal that the CsaC-mediated reaction is regioselective for O3 and that the O4 modification results from spontaneous O-acetyl migration.

    • Timm Fiebig
    • Johannes T. Cramer
    • Martina Mühlenhoff
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • 9-O-Acetylation is one of the most common modifications of sialic acids, implicated in sialoglycan recognition and ganglioside biology. Here, the authors show that the key enzyme for the biosynthesis of 9-O-acetylated sialoglycans is CASD1, which uses CMP-activated sialic acid as acceptor substrate.

    • Anna-Maria T. Baumann
    • Mark J. G. Bakkers
    • Martina Mühlenhoff
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-12

  • Some viral proteins involved in interaction with the host cell surface adopt a very rigid and stable triple–β-helix fold. In order to attain this complex fold, these proteins contain an intramolecular chaperone domain that is auto-cleaved after assembly. Now structural work on two such chaperone domains indicates how they can promote correct folding of the β-helices.

    • Eike C Schulz
    • Achim Dickmanns
    • Ralf Ficner
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 210-215

  • The protease Atg4 mediates Atg8 lipidation, required for autophagosome biogenesis, but also triggers Atg8 release from the membranes, however is unclear how these steps are coordinated. Here the authors show that phosphorylation by Atg1 inhibits Atg4 at autophagosome formation sites.

    • Jana Sánchez-Wandelmer
    • Franziska Kriegenburg
    • Fulvio Reggiori
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-10