Ramón Hurtado Guerrero-rekin lankidetzan egindako argitalpenak (13)

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. 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

  2. Mucin Architecture behind the Immune Response: Design and Evaluation of an Antitumor Vaccine Derived from an Unnatural MUC1 Fragment

    Chemical Science, Vol. 7, Núm. 3, pp. 2294

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

  2. Detection of tumor-associated glycopeptides by Lectins: The peptide context modulates carbohydrate recognition

    ACS chemical biology, Vol. 10, Núm. 3, pp. 747-756

2014

  1. Serine versus Threonine Glycosylation witha-O-GalNAc: Unexpected Selectivity in Their Molecular Recognition with Lectins

    Chemistry - A European Journal, Vol. 20, Núm. 39, pp. 12616-12627