LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 126

Search options

  1. Article ; Online: Synthesis and immunological evaluation of TLR1/2 ligand-conjugated RBDs as self-adjuvanting vaccine candidates against SARS-CoV-2.

    Manabe, Yoshiyuki / Gárate-Reyes, Brandon / Ito, Keita / Hurtado-Guerrero, Ramón / Kabayama, Kazuya / Fukase, Koichi

    Chemical communications (Cambridge, England)

    2024  Volume 60, Issue 29, Page(s) 3946–3949

    Abstract: We synthesized and evaluated ... ...

    Abstract We synthesized and evaluated Pam
    MeSH term(s) Humans ; SARS-CoV-2 ; Toll-Like Receptor 1 ; Antibodies, Viral ; COVID-19/prevention & control ; Ligands ; Viral Vaccines ; Adjuvants, Immunologic/pharmacology
    Chemical Substances Toll-Like Receptor 1 ; Antibodies, Viral ; Ligands ; Viral Vaccines ; Adjuvants, Immunologic
    Language English
    Publishing date 2024-04-04
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d4cc00462k
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) isozyme surface charge governs charge substrate preferences to modulate mucin type O-glycosylation.

    Ballard, Collin J / Paserba, Miya R / Paul Daniel, Earnest James / Hurtado-Guerrero, Ramón / Gerken, Thomas A

    Glycobiology

    2023  Volume 33, Issue 10, Page(s) 817–836

    Abstract: A large family of polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) initiate mucin type O-glycosylation transferring α-GalNAc from a UDP-GalNAc donor to the hydroxyl groups of Ser and Thr residues of peptides and proteins, thereby defining sites ...

    Abstract A large family of polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) initiate mucin type O-glycosylation transferring α-GalNAc from a UDP-GalNAc donor to the hydroxyl groups of Ser and Thr residues of peptides and proteins, thereby defining sites of O-glycosylation. Mutations and differential expression of several GalNAc-Ts are associated with many disease states including cancers. The mechanisms by which these isozymes choose their targets and their roles in disease are not fully understood. We previously showed that the GalNAc-Ts possess common and unique specificities for acceptor type, peptide sequence and prior neighboring, and/or remote substrate GalNAc glycosylation. In the present study, the role of flanking charged residues was investigated using a library of charged peptide substrates containing the central -YAVTPGP- acceptor sequence. Eleven human and one bird GalNAc-T were initially characterized revealing a range of preferences for net positive, net negative, or unique combinations of flanking N- and/or C-terminal charge, correlating to each isozyme's different electrostatic surface potential. It was further found that isoforms with high sequence identity (>70%) within a subfamily can possess vastly different charge specificities. Enzyme kinetics, activities obtained at elevated ionic strength, and molecular dynamics simulations confirm that the GalNAc-Ts differently recognize substrate charge outside the common +/-3 residue binding site. These electrostatic interactions impact how charged peptide substrates bind/orient on the transferase surface, thus modulating their activities. In summary, we show the GalNAc-Ts utilize more extended surfaces than initially thought for binding substrates based on electrostatic, and likely other hydrophobic/hydrophilic interactions, furthering our understanding of how these transferases select their target.
    MeSH term(s) Humans ; Glycosylation ; Mucins/metabolism ; Isoenzymes/chemistry ; Peptides/chemistry ; N-Acetylgalactosaminyltransferases/metabolism ; Substrate Specificity ; Polypeptide N-acetylgalactosaminyltransferase
    Chemical Substances Mucins ; Isoenzymes ; Peptides ; N-Acetylgalactosaminyltransferases (EC 2.4.1.-)
    Language English
    Publishing date 2023-08-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwad066
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3150: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Molecular Recognition of GalNAc in Mucin-Type O-Glycosylation.

    Sanz-Martinez, Ignacio / Pereira, Sandra / Merino, Pedro / Corzana, Francisco / Hurtado-Guerrero, Ramon

    Accounts of chemical research

    2023  Volume 56, Issue 5, Page(s) 548–560

    Abstract: Acetylgalactosamine (GalNAc)-type O-glycosylation is an essential posttranslational modification (PTM) that plays fundamental roles in biology. Malfunction of this PTM is exemplified by the presence of ... ...

    Abstract Acetylgalactosamine (GalNAc)-type O-glycosylation is an essential posttranslational modification (PTM) that plays fundamental roles in biology. Malfunction of this PTM is exemplified by the presence of truncated
    MeSH term(s) Mucins/chemistry ; Mucins/metabolism ; Glycosylation ; Glycopeptides/chemistry ; Lectins/chemistry ; Carbohydrates ; Polysaccharides ; Glycosyltransferases ; Sugars
    Chemical Substances Mucins ; Glycopeptides ; Lectins ; Carbohydrates ; Polysaccharides ; Glycosyltransferases (EC 2.4.-) ; Sugars
    Language English
    Publishing date 2023-02-23
    Publishing country United States
    Document type Review ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483291-4
    ISSN 1520-4898 ; 0001-4842
    ISSN (online) 1520-4898
    ISSN 0001-4842
    DOI 10.1021/acs.accounts.2c00723
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Recent structural and mechanistic insights into protein O-GalNAc glycosylation.

    Hurtado-Guerrero, Ramon

    Biochemical Society transactions

    2016  Volume 44, Issue 1, Page(s) 61–67

    Abstract: Protein O-GalNAcylation is an abundant post-translational modification and predicted to occur in over 80% of the proteins passing through the Golgi apparatus. This modification is driven by 20 polypeptide GaINAc (N-acetylgalactosamine)-transferases ( ... ...

    Abstract Protein O-GalNAcylation is an abundant post-translational modification and predicted to occur in over 80% of the proteins passing through the Golgi apparatus. This modification is driven by 20 polypeptide GaINAc (N-acetylgalactosamine)-transferases (GalNAc-Ts), which are unique in that they possess both catalytic and lectin domains. The peptide substrate specificities of GalNAc-Ts are still poorly defined and our understanding of the sequence and structural features that direct O-glycosylation of proteins is limited. Part of this may be attributed to the complex regulation by coordinated action of multiple GalNAc-T isoforms, and part of this may also be attributed to the two functional domains of GalNAc-Ts that both seems to be involved in directing the substrate specificities. Recent studies have resulted in 3D structures of GalNAc-Ts and determination of the reaction mechanism of this family of enzymes. Key advances include the trapping of binary/ternary complexes in combination with computational simulations and AFM/small-SAXS experiments, which have allowed for the dissection of the reaction coordinates and the mechanism by which the lectin domains modulate the glycosylation. These studies not only broaden our knowledge of the modes-of-action of this family of enzymes but also open up potential avenues for the rational design of effective and selective inhibitors of O-glycosylation.
    MeSH term(s) Acetylgalactosamine/chemistry ; Acetylgalactosamine/metabolism ; Animals ; Biocatalysis ; Glycosylation ; Humans ; Models, Molecular ; N-Acetylgalactosaminyltransferases/chemistry ; N-Acetylgalactosaminyltransferases/metabolism ; Protein Structure, Tertiary
    Chemical Substances N-Acetylgalactosaminyltransferases (EC 2.4.1.-) ; Acetylgalactosamine (KM15WK8O5T)
    Language English
    Publishing date 2016-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20150178
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 944: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: A Bump-and-Hole Approach to Dissect Regulation of Protein O-Glycosylation

    Schjoldager, Katrine T / Clausen, Henrik / Hurtado-Guerrero, Ramon

    Molecular cell. 2020 June 04, v. 78, no. 5

    2020  

    Abstract: In this issue of Molecular Cell, Schumann et al. (2020) present a novel strategy to dissect the regulation of protein O-glycosylation by a large family of isoenzymes in cells. They employ a bump-and-hole engineering approach to capture the specific ... ...

    Abstract In this issue of Molecular Cell, Schumann et al. (2020) present a novel strategy to dissect the regulation of protein O-glycosylation by a large family of isoenzymes in cells. They employ a bump-and-hole engineering approach to capture the specific contribution of individual isoenzymes to O-glycosylation of proteins.
    Keywords engineering ; glycosylation ; isozymes ; proteins
    Language English
    Dates of publication 2020-0604
    Size p. 803-805.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2020.05.019
    Database NAL-Catalogue (AGRICOLA)

    Full text online

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 2005/501: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  6. Article ; Online: A Bump-and-Hole Approach to Dissect Regulation of Protein O-Glycosylation.

    Schjoldager, Katrine T / Clausen, Henrik / Hurtado-Guerrero, Ramon

    Molecular cell

    2020  Volume 78, Issue 5, Page(s) 803–805

    Abstract: In this issue of Molecular Cell, Schumann et al. (2020) present a novel strategy to dissect the regulation of protein O-glycosylation by a large family of isoenzymes in cells. They employ a bump-and-hole engineering approach to capture the specific ... ...

    Abstract In this issue of Molecular Cell, Schumann et al. (2020) present a novel strategy to dissect the regulation of protein O-glycosylation by a large family of isoenzymes in cells. They employ a bump-and-hole engineering approach to capture the specific contribution of individual isoenzymes to O-glycosylation of proteins.
    MeSH term(s) Glycosylation ; Glycosyltransferases ; Isoenzymes ; Proteins
    Chemical Substances Isoenzymes ; Proteins ; Glycosyltransferases (EC 2.4.-)
    Language English
    Publishing date 2020-06-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2020.05.019
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: The Essential Role of Water Molecules in the Reaction Mechanism of Protein O-Fucosyltransferase 2.

    Sanz-Martínez, Ignacio / García-García, Ana / Tejero, Tomás / Hurtado-Guerrero, Ramón / Merino, Pedro

    Angewandte Chemie (International ed. in English)

    2022  Volume 61, Issue 48, Page(s) e202213610

    Abstract: Protein O-fucosyltransferase 2 (PoFUT2) is an inverting glycosyltransferase (GT) that fucosylates thrombospondin repeats (TSRs) from group 1 and 2. PoFUT2 recognizes a large and diverse number of TSRs through a dynamic network of water-mediated ... ...

    Abstract Protein O-fucosyltransferase 2 (PoFUT2) is an inverting glycosyltransferase (GT) that fucosylates thrombospondin repeats (TSRs) from group 1 and 2. PoFUT2 recognizes a large and diverse number of TSRs through a dynamic network of water-mediated interactions. By X-ray structural studies of C. elegans PoFUT2 complexed to a TSR of group 2, we demonstrate that this GT recognizes similarly the 3D structure of TSRs from both groups 1 and 2. Its active site is highly exposed to the solvent, suggesting that water molecules might also play an essential role in the fucosylation mechanism. We applied QM/MM methods using human PoFUT2 as a model, and found that HsPoFUT2 follows a classical S
    MeSH term(s) Humans ; Animals ; Fucose/chemistry ; Water ; Caenorhabditis elegans/metabolism ; Glycosylation ; Galactoside 2-alpha-L-fucosyltransferase
    Chemical Substances Fucose (28RYY2IV3F) ; Water (059QF0KO0R)
    Language English
    Publishing date 2022-11-10
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.202213610
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Author Correction: Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase.

    Piniello, Beatriz / Macías-León, Javier / Miyazaki, Shun / García-García, Ana / Compañón, Ismael / Ghirardello, Mattia / Taleb, Víctor / Veloz, Billy / Corzana, Francisco / Miyagawa, Atsushi / Rovira, Carme / Hurtado-Guerrero, Ramon

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 1322

    Language English
    Publishing date 2024-02-13
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-45708-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: A perspective on structural and mechanistic aspects of protein O-fucosylation.

    Lira-Navarrete, Erandi / Hurtado-Guerrero, Ramon

    Acta crystallographica. Section F, Structural biology communications

    2018  Volume 74, Issue Pt 8, Page(s) 443–450

    Abstract: Protein O-fucosylation is an important post-translational modification (PTM) found in cysteine-rich repeats in proteins. Protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this PTM and selectively glycosylate ... ...

    Abstract Protein O-fucosylation is an important post-translational modification (PTM) found in cysteine-rich repeats in proteins. Protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this PTM and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs), respectively. Within the past six years, crystal structures of both enzymes have been reported, revealing important information on how they recognize protein substrates and achieve catalysis. Here, the structural information available today is summarized and how PoFUT1 and PoFUT2 employ different catalytic mechanisms is discussed.
    MeSH term(s) Animals ; Fucosyltransferases/chemistry ; Fucosyltransferases/metabolism ; Humans ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Galactoside 2-alpha-L-fucosyltransferase
    Chemical Substances Fucosyltransferases (EC 2.4.1.-)
    Language English
    Publishing date 2018-07-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 2053-230X
    ISSN (online) 2053-230X
    DOI 10.1107/S2053230X18004788
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  10. Article: Systematic Strategy for the Development of Glycosyltransferase Inhibitors: Diversity-Oriented Synthesis of FUT8 Inhibitors

    Manabe, Yoshiyuki / Hizume, Koki / Takakura, Yohei / Takamatsu, Shinji / Miyoshi, Eiji / Kamada, Yoshihiro / Hurtado-Guerrero, Ramón / Fukase, Koichi

    Synlett

    2023  

    Abstract: Glycans control various biological processes, depending on their structures. Particularly, core fucose, formed by α1,6-fucosyltransferase (FUT8), has a substantial influence on multiple biological processes. In this study, we investigated the development ...

    Abstract Glycans control various biological processes, depending on their structures. Particularly, core fucose, formed by α1,6-fucosyltransferase (FUT8), has a substantial influence on multiple biological processes. In this study, we investigated the development of FUT8 inhibitors with structural elements encompassing both the glycosyl donor (GDP-fucose) and acceptor ( N -glycan) of FUT8. To efficiently optimize the structure of FUT8 inhibitors, we employed a strategy involving fragmentation of the target structure, followed by a structure optimization using a diversity-oriented synthesis approach. This study proposes an efficient strategy to accelerate the structural optimization of middle molecules.
    Keywords compound libraries ; diversity-oriented synthesis ; glycosyltransferase ; enzyme inhibitor ; diversity-oriented synthesis
    Language English
    Publishing date 2023-12-04
    Publisher Georg Thieme Verlag KG
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 2042012-2
    ISSN 1437-2096 ; 0936-5214
    ISSN (online) 1437-2096
    ISSN 0936-5214
    DOI 10.1055/a-2221-9096
    Database Thieme publisher's database

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top