Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Emiliano Cló"'
Autor:
Thorbjørn B. Nielsen, Rasmus P. Thomsen, Michael R. Mortensen, Jørgen Kjems, Per Franklin Nielsen, Thomas E. Nielsen, Anne Louise B. Kodal, Emiliano Cló, Kurt V. Gothelf
Publikováno v:
Angewandte Chemie. 131:9166-9170
Autor:
Milan Štengl, Emiliano Cló, Zuzana Drobňáková, Anders Märcher, Vojtěch Balšánek, Thomas E. Nielsen, Michal Hučko, Per Franklin Nielsen, Thorbjørn B. Nielsen, Charlotte Wiberg, Kurt V. Gothelf
Publikováno v:
Nielsen, T, Märcher, A, Drobňáková, Z, Hučko, M, Štengl, M, Balšánek, V, Wiberg, C, Nielsen, P F, Nielsen, T E, Gothelf, K V & Cló, E 2020, ' Disulphide-mediated site-directed modification of proteins ', Organic and Biomolecular Chemistry, vol. 18, no. 25, pp. 4717-4722 . https://doi.org/10.1039/d0ob00861c
Methods for chemical modification of native proteins in a controlled fashion are in high demand. Here, a novel protocol that exploits bifunctional reagents for transient targeting of solvent exposed disulphides to direct the introduction of a single
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::089d8488bcff0408e6478852817af22b
https://pure.au.dk/portal/da/publications/disulphidemediated-sitedirected-modification-of-proteins(fd0ae506-7b58-4c53-a66c-17e7df3310c1).html
https://pure.au.dk/portal/da/publications/disulphidemediated-sitedirected-modification-of-proteins(fd0ae506-7b58-4c53-a66c-17e7df3310c1).html
Autor:
Thomas E. Nielsen, Michael Rosholm Mortensen, Anne Louise Bank Kodal, Emiliano Cló, Jørgen Kjems, Per Franklin Nielsen, Kurt V. Gothelf, Thorbjørn B. Nielsen, Rasmus P. Thomsen
Publikováno v:
Nielsen, T B, Thomsen, R P, Mortensen, M R, Kjems, J, Nielsen, P F, Nielsen, T E, Kodal, A L B, Cló, E & Gothelf, K V 2019, ' Peptide-Directed DNA-Templated Protein Labelling for The Assembly of a Pseudo-IgM ', Angewandte Chemie International Edition, vol. 58, no. 27, pp. 9068-9072 . https://doi.org/10.1002/anie.201903134
The development of methods for conjugation of DNA to proteins is of high relevance for the integration of protein function and DNA structures. Here, we demonstrate that protein-binding peptides can direct a DNA-templated reaction, selectively furnish
Publikováno v:
Glycoconjugate Journal. 30:633-640
The Epstein-Barr virus (EBV) envelope glycoprotein 350/220 (gp350/220) is the most abundant molecule on the viral surface and it is responsible for the initial viral attachment to cell surface of the host. As many other viral envelope proteins, it is
Autor:
Ola Blixt, Sigvard Olofsson, Aaron S. Nudelman, Knud J. Jensen, Tomas Bergström, Emiliano Cló, Stjepan K. Kračun, Jan-Åke Liljeqvist
Publikováno v:
Journal of Virology. 86:6268-6278
Viral envelope proteins mediate interactions with host cells, leading to internalization and intracellular propagation. Envelope proteins are glycosylated and are known to serve important functions in masking host immunity to viral glycoproteins. How
Autor:
Nicolai V. Bovin, Emiliano Cló, Olga I Lavrova, Ola Blixt, Stjepan K. Kračun, Dmitriy Mazurov, Alexander Filatov
Publikováno v:
Glycobiology; Vol 22
CD175 or Tn antigen is a carbohydrate moiety of N-acetylgalactosamine (GalNAc)α1-O- linked to the residue of amino acid serine or threonine in a polypeptide chain. Despite the chemical simplicity of the Tn antigen, its antigenic structure is conside
Autor:
Emiliano Cló, Ola Blixt, Johannes W. Pedersen, Henrik Clausen, Morten Meldal, Hans H. Wandall, Eric P. Bennett, Steven B. Levery, Katrine T. Schjoldager, Andreas P. Holmér
Publikováno v:
The Journal of Biological Chemistry
UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (GalNAc-Ts) constitute a family of up to 20 transferases that initiate mucin-type O-glycosylation. The transferases are structurally composed of catalytic and lectin domains. Two modes have
Publikováno v:
European Journal of Organic Chemistry. 2010:540-554
Glycobiology has made very significant progress in the past decades. However, further progress will significantly depend on the establishment of novel methods for miniaturized, high-throughput analysis of glycan–protein interactions. Robust solid-p
Publikováno v:
Nielsen, M, Thomsen, A H, Clo, E, Kirpekar, F & Gothelf, K V 2004, ' Synthesis of Linear and Tripoidal Oligo(phenylene ethynylene)-Based Building Blocks for Application in Modular DNA-Programmed Assembly ', J. Org. Chem., vol. 69, pp. 2240-2250 .
Nielsen, M, Thomsen, A H, Cló, E, Kirpekar, F & Gothelf, K V 2004, ' Synthesis of Linear and Tripoidal Oligo(phenyleneethynylene)-Based Building Blocks for Application in Modular DNA-Programmed Assembly. ', Journal of Organic Chemistry, vol. 69, pp. 2240-2250 . https://doi.org/10.1021/jo035764m
Nielsen, M, Thomsen, A H, Cló, E, Kirpekar, F & Gothelf, K V 2004, ' Synthesis of Linear and Tripoidal Oligo(phenyleneethynylene)-Based Building Blocks for Application in Modular DNA-Programmed Assembly. ', Journal of Organic Chemistry, vol. 69, pp. 2240-2250 . https://doi.org/10.1021/jo035764m
Rigid linear and tripoidal organic modules based on the oligo(phenylene ethynylene) backbone having salicylaldehyde-derived termini are synthesized. A highly functionalized 5-iodosalicyl aldehyde was prepared and coupled to each ethynyl group of 1,4-
Autor:
Clive W. Ronson, Mikkel B. Thygesen, Nicolai N. Maolanon, John T. Sullivan, Kasper K. Sørensen, Mickaël Blaise, Knud J. Jensen, Jens Stougaard, Emiliano Cló, Ola Blixt
Publikováno v:
Maolanon, N N, Blaise, M, Sørensen, K K, Thygesen, M B, Cló, E, Sullivan, J T, Ronson, C W, Stougaard, J, Blixt, K O & Jensen, K J 2014, ' Lipochitin Oligosaccharides Immobilized through Oximes in Glycan Microarrays Bind LysM Proteins ', ChemBioChem, vol. 15, no. 3, pp. 425-434 . https://doi.org/10.1002/cbic.201300520
ChemBioChem
ChemBioChem, Wiley-VCH Verlag, 2014, 15 (3), pp.425-434. ⟨10.1002/cbic.201300520⟩
ChemBioChem
ChemBioChem, Wiley-VCH Verlag, 2014, 15 (3), pp.425-434. ⟨10.1002/cbic.201300520⟩
Glycan microarrays have emerged as novel tools to study carbohydrate-protein interactions. Here we describe the preparation of a covalent microarray with lipochitin oligosaccharides and its use in studying proteins containing LysM domains. The glycan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fa39a5b3e59cbae17843598a39202a9
https://pure.au.dk/ws/files/84732265/Lipochitin_Oligosaccharides_ChemBioChem_2014_Maolanon.pdf
https://pure.au.dk/ws/files/84732265/Lipochitin_Oligosaccharides_ChemBioChem_2014_Maolanon.pdf