Publicacions en què col·labora amb Jesús Jiménez Barbero (11)

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

2019

  1. Conformational Behavior of D-Lyxose in Gas and Solution Phases by Rotational and NMR Spectroscopies

    Journal of Physical Chemistry Letters, Vol. 10, Núm. 12, pp. 3339-3345

  2. Structure-Based Design of Potent Tumor-Associated Antigens: Modulation of Peptide Presentation by Single-Atom O/S or O/Se Substitutions at the Glycosidic Linkage

    Journal of the American Chemical Society, Vol. 141, Núm. 9, pp. 4063-4072

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

  2. Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4

    ACS Central Science, Vol. 4, Núm. 9, pp. 1274-1290

  3. The use of fluoroproline in MUC1 antigen enables efficient detection of antibodies inpatients with cancer

    29th International Carbohydrate Symposium - ICS2018

  4. Water Sculpts the Distinctive Shapes and Dynamics of the Tumor-Associated Carbohydrate Tn Antigens: Implications for Their Molecular Recognition

    Journal of the American Chemical Society, Vol. 140, Núm. 31, pp. 9952-9960

2017

  1. The Use of Fluoroproline in MUC1 Antigen Enables Efficient Detection of Antibodies in Patients with Prostate Cancer

    Journal of the American Chemical Society, Vol. 139, Núm. 50, pp. 18255-18261

  2. 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

2015

  1. Deciphering the Non-Equivalence of Serine and Threonine O-glycosylation Points: Implications for Molecular Recognition of the Tn Antigen by an anti-MUC1 Antibody

    Angewandte Chemie International, Vol. 54, Núm. 34, pp. 9830