Synthesis and conformational preferences of short analogues of antifreeze glycopeptides (AFGP)

Autor: Małgorzata Urbańczyk, Michał Jewgiński, Joanna Krzciuk-Gula, Jerzy Góra, Rafał Latajka, Norbert Sewald

Publikováno v: Beilstein Journal of Organic Chemistry, Vol 15, Iss 1, Pp 1581-1591 (2019)

Antifreeze glycoproteins are a class of biological agents which enable living at temperatures below the freezing point of the body fluids. Antifreeze glycopeptides usually consist of repeating tripeptide unit (-Ala-Ala-Thr*-), glycosylated at the thr

Externí odkaz: https://doaj.org/article/7a286044ae784040a11a3350617da7bd

Synthesis and conformational preferences of short analogues of antifreeze glycopeptides (AFGP)

Autor: Michał Jewgiński, Rafał Latajka, Jerzy Góra, Joanna Krzciuk-Gula, Małgorzata Urbańczyk, Norbert Sewald

Publikováno v: Beilstein Journal of Organic Chemistry, Vol 15, Iss 1, Pp 1581-1591 (2019)
Beilstein Journal of Organic Chemistry

Antifreeze glycoproteins are a class of biological agents which enable living at temperatures below the freezing point of the body fluids. Antifreeze glycopeptides usually consist of repeating tripeptide unit (-Ala-Ala-Thr*-), glycosylated at the thr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aff6ab2958ff6d1c7afac4172072753
https://pubmed.ncbi.nlm.nih.gov/31435440

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Differential Recognition Preferences of the Three Src Homology 3 (SH3) Domains from the Adaptor CD2-associated Protein (CD2AP) and Direct Association with Ras and Rab Interactor 3 (RIN3).

Autor: Rouka E; From the Weatherall Institute of Molecular Medicine, Department of Oncology, University of Oxford, Oxford OX3 9DS, United Kingdom., Simister PC; From the Weatherall Institute of Molecular Medicine, Department of Oncology, University of Oxford, Oxford OX3 9DS, United Kingdom, philip.simister@imm.ox.ac.uk., Janning M; From the Weatherall Institute of Molecular Medicine, Department of Oncology, University of Oxford, Oxford OX3 9DS, United Kingdom., Kumbrink J; the Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118., Konstantinou T; From the Weatherall Institute of Molecular Medicine, Department of Oncology, University of Oxford, Oxford OX3 9DS, United Kingdom., Muniz JR; the Structural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom., Joshi D; the Peptide Chemistry Laboratory, London Research Institute Cancer Research UK, London WC2A 3LY, United Kingdom., O'Reilly N; the Peptide Chemistry Laboratory, London Research Institute Cancer Research UK, London WC2A 3LY, United Kingdom., Volkmer R; the Institute of Medical Immunology, Charité-Universitätsmedizin Berlin, 10115 Berlin, Germany., Ritter B; the Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118., Knapp S; the Structural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom., von Delft F; the Structural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom, the Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0QX, United Kingdom, and the Department of Biochemistry, University of Johannesburg, Auckland Park 2006, South Africa., Kirsch KH; the Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118., Feller SM; From the Weatherall Institute of Molecular Medicine, Department of Oncology, University of Oxford, Oxford OX3 9DS, United Kingdom, the Institute of Molecular Medicine, Martin Luther University Halle-Wittenberg, D-06120 Halle, Germany, stephan.feller@uk-halle.de.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2015 Oct 16; Vol. 290 (42), pp. 25275-92. Date of Electronic Publication: 2015 Aug 20.