Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Sebastian Kiehstaller"'
Autor:
Sebastian Kiehstaller, George H. Hutchins, Alessia Amore, Alan Gerber, Mohamed Ibrahim, Sven Hennig, Saskia Neubacher, Tom N. Grossmann
Publikováno v:
Kiehstaller, S, Hutchins, G H, Amore, A, Gerber, A, Ibrahim, M, Hennig, S, Neubacher, S & Grossmann, T N 2023, ' Bicyclic Engineered Sortase A Performs Transpeptidation under Denaturing Conditions ', Bioconjugate chemistry, vol. 34, no. 6, pp. 1114-1121 . https://doi.org/10.1021/acs.bioconjchem.3c00151
Bioconjugate chemistry. American Chemical Society
Bioconjugate chemistry. American Chemical Society
Enzymes are of central importance to many biotechnological and biomedical applications. However, for many potential applications, the required conditions impede enzyme folding and therefore function. The enzyme Sortase A is a transpeptidase that is w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::900073b38c8c7146288c8df4ea14297a
https://hdl.handle.net/1871.1/ce68c81f-f931-4ebd-93ed-e2d4861cf034
https://hdl.handle.net/1871.1/ce68c81f-f931-4ebd-93ed-e2d4861cf034
Autor:
Mathias Wendt, Sven Hennig, Arne Kuepper, Nicole Pospiech, Diego Brancaccio, Sadasivam Jeganathan, Tom N. Grossmann, Ettore Novellino, Alfonso Carotenuto, Sebastian Kiehstaller
Publikováno v:
Angewandte Chemie (International Ed. in English)
Jeganathan, S, Wendt, M, Kiehstaller, S, Brancaccio, D, Kuepper, A, Pospiech, N, Carotenuto, A, Novellino, E, Hennig, S & Grossmann, T N 2019, ' Constrained Peptides with Fine-Tuned Flexibility Inhibit NF-Y Transcription Factor Assembly ', Angewandte Chemie. International Edition, vol. 58, no. 48, pp. 17351-17358 . https://doi.org/10.1002/anie.201907901
Angewandte Chemie
Jeganathan, S, Wendt, M, Kiehstaller, S, Brancaccio, D, Kuepper, A, Pospiech, N, Carotenuto, A, Novellino, E, Hennig, S & Grossmann, T N 2019, ' Constrained Peptides with Fine-Tuned Flexibility Inhibit NF-Y Transcription Factor Assembly ', Angewandte Chemie. International Edition, vol. 58, no. 48, pp. 17351-17358 . https://doi.org/10.1002/anie.201907901
Angewandte Chemie
Protein complex formation depends on the interplay between preorganization and flexibility of the binding epitopes involved. The design of epitope mimetics typically focuses on stabilizing a particular bioactive conformation, often without considerin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b3c6498df6c55ad6a3fb51bf57bd5e
https://doi.org/10.1002/ange.201907901
https://doi.org/10.1002/ange.201907901
Publikováno v:
Journal of Biological Chemistry, 295(52), 18266-18275. American Society for Biochemistry and Molecular Biology Inc.
The Journal of Biological Chemistry
Kiehstaller, S, Ottmann, C & Hennig, S 2020, ' MMP activation associated Aminopeptidase N reveals a bivalent 14-3-3 binding motif ', Journal of Biological Chemistry, vol. 295, no. 52, pp. 18266-18275 . https://doi.org/10.1074/jbc.RA120.014708
The Journal of Biological Chemistry
Kiehstaller, S, Ottmann, C & Hennig, S 2020, ' MMP activation associated Aminopeptidase N reveals a bivalent 14-3-3 binding motif ', Journal of Biological Chemistry, vol. 295, no. 52, pp. 18266-18275 . https://doi.org/10.1074/jbc.RA120.014708
Aminopeptidase N (APN, CD13) is a trans-membrane ectopeptidase involved in many crucial cellular functions. Besides its role as a peptidase, APN also mediates signal transduction, and is involved in the activation of Matrix Metalloproteinases (MMPs).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32758ffec530b68b835f708122e5d50c
https://research.tue.nl/nl/publications/7271e282-d705-4152-9fba-f2808793ff76
https://research.tue.nl/nl/publications/7271e282-d705-4152-9fba-f2808793ff76