Publications en collaboration avec des chercheurs de University of Copenhagen (14)

2024

  1. A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases

    Nature Catalysis, Vol. 7, Núm. 4, pp. 386-400

  2. Correction to: Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase (Nature Communications, (2023), 14, 1, (5785), 10.1038/s41467-023-41238-1)

    Nature Communications

  3. Rational Design of Dual-Domain Binding Inhibitors for N-Acetylgalactosamine Transferase 2 with Improved Selectivity over the T1 and T3 Isoforms

    JACS Au, Vol. 4, Núm. 9, pp. 3649-3656

2023

  1. Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase

    Nature Communications, Vol. 14, Núm. 1

2022

  1. Atomic and Specificity Details of Mucin 1 O-Glycosylation Process by Multiple Polypeptide GalNAc-Transferase Isoforms Unveiled by NMR and Molecular Modeling

    JACS AU, Vol. 2, Núm. 3, pp. 631-645

  2. Structural and mechanistic insights into the cleavage of clustered O-glycan patches-containing glycoproteins by mucinases of the human gut

    Nature Communications, Vol. 13, Núm. 1

  3. Structural basis for the synthesis of the core 1 structure by C1GalT1

    Nature Communications, Vol. 13, Núm. 1

2020

  1. Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3

    Nature Chemical Biology, Vol. 16, Núm. 3, pp. 351-360

  2. Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody

    Chemical Communications, Vol. 56, Núm. 96, pp. 15137-15140

2018

  1. Structural Analysis of a GalNAc-T2 Mutant Reveals an Induced-Fit Catalytic Mechanism for GalNAc-Ts

    Chemistry - A European Journal, Vol. 24, Núm. 33, pp. 8382-8392

2017

  1. The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences

    Nature Communications, Vol. 8, Núm. 1

2016

  1. Design of α-S-Neoglycopeptides Derived from MUC1 with a Flexible and Solvent-Exposed Sugar Moiety

    Journal of Organic Chemistry, Vol. 81, Núm. 14, pp. 5929-5941

2014

  1. Combined structural snapshots and metadynamics reveal a substrate-guided SNi-type reaction for polypeptide GalNAc transferaseT2

    XI Carbohydrate Symposium

  2. Substrate-guided front-face reaction revealed by combined structural snapshots and metadynamics for the polypeptide N-acetylgalactosaminyltransferase 2

    Angewandte Chemie International, Vol. 53, Núm. 31, pp. 8206-8210