Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Jonas S. Laursen"'
Autor:
Kresten Lindorff-Larsen, Isaiah T. Arkin, Martin Willemoës, Paul Santner, Jonas S. Laursen, Christian A. Olsen, João M. Martins, Leise Riber, Lars Behrendt, Jakob R. Winther
Publikováno v:
Biochemistry. 57:5949-5956
The M2 protein is an important target for drugs in the fight against the influenza virus. Because of the emergence of resistance against antivirals directed toward the M2 proton channel, the search for new drugs against resistant M2 variants is of hi
Autor:
Paul Santner, Jonas S. Laursen, Caroline Kampmeyer, Christian A. Olsen, João M. Martins, Jakob R. Winther, Isaiah T. Arkin, Martin Willemoës, Amelie Stein, Kresten Lindorff-Larsen, Rasmus Hartmann-Petersen
Publikováno v:
Biochemistry. 57:5957-5968
The influenza M2 proton channel is a major drug target, but unfortunately, the acquisition of resistance mutations greatly reduces the functional life span of a drug in influenza treatment. New M2 inhibitors that inhibit mutant M2 channels otherwise
Autor:
Michael Bæk, Pablo Martín-Gago, Jonas S. Laursen, Julie L. H. Madsen, Saswati Chakladar, Christian Adam Olsen
Posttranslational modifications (PTMs) are important in the regulation of protein function, trafficking, localization, and marking for degradation. Here, we describe development of peptide activity-based probes for the discovery of proteins that reco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f3afe0d534fee182403b49e304dd331
https://doi.org/10.26434/chemrxiv.10315502.v1
https://doi.org/10.26434/chemrxiv.10315502.v1
Autor:
Christian A. Olsen, Andreas M. Christiansen, Isabelle Wellhöfer, Karla Frydenvang, Simona Kotesova, Jonas S. Laursen
Publikováno v:
The Journal of organic chemistry. 84(7)
Peptidomimetic foldamers adopting well-defined three-dimensional structures while being stable toward proteolysis are of interest in biomedical research, chemical biology, and biomimetic materials science. Despite their backbone flexibility, β-pepto
Autor:
Mohammad Mahdi Daoud, Ana Colaço, Christian A. Olsen, Saswati Chakladar, Peter Fristrup, Frank K. Huynh, Kristin A. Anderson, Donald S. Backos, Christian Beyschau Andersen, Matthew D. Hirschey, Jonas S. Laursen, Andreas Stahl Madsen
Publikováno v:
Journal of Biological Chemistry. 291:7128-7141
Protein lysine posttranslational modification by an increasing number of different acyl groups is becoming appreciated as a regulatory mechanism in cellular biology. Sirtuins are class III histone deacylases that use NAD(+)as a co-substrate during am
Autor:
Jonas S. Laursen, Lone Gram, Line Hein-Kristensen, Konstantin Andreev, Ivan Kuzmenko, Christian A. Olsen, Christopher Bianchi, David Gidalevitz, Linda Citterio
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838(10):2492-2502
Antimicrobial peptides or their synthetic mimics are a promising class of potential new antibiotics. Herein we assess the effect of the type of cationic side chain (i.e., guanidino vs. amino groups) on the membrane perturbing mechanism of antimicrobi
Publikováno v:
Laursen, J S, Engel-Andreasen, J, Fristrup, P, Harris, P & Olsen, C A 2013, ' Cis–Trans Amide Bond Rotamers in β-Peptoids and Peptoids: Evaluation of Stereoelectronic : Effects in Backbone and Side Chains ', Journal of the American Chemical Society, vol. 135, no. 7, pp. 2835-2844 . https://doi.org/10.1021/ja312532x
Non-natural peptide analogs have significant potential for the development of new materials and pharmacologically active ligands. One such architecture, the β-peptoids (N-alkyl-β-alanines), has found use in a variety of biologically active compound
Publikováno v:
Accounts of chemical research. 48(10)
For a long time, peptides were considered unsuitable for drug development due to their inherently poor pharmacokinetic properties and proteolytic susceptibility. However, this paradigm has changed significantly in the past decade with the approval of
Publikováno v:
Nature Communications
Laursen, J S, Harris, P, Fristrup, P & Olsen, C A 2015, ' Triangular prism-shaped β-peptoid helices as unique biomimetic scaffolds ', Nature Communications, vol. 6, 7013 . https://doi.org/10.1038/ncomms8013
Laursen, J S, Harris, P, Fristrup, P & Olsen, C A 2015, ' Triangular prism-shaped β-peptoid helices as unique biomimetic scaffolds ', Nature Communications, vol. 6, 7013 . https://doi.org/10.1038/ncomms8013
β-Peptoids are peptidomimetics based on N-alkylated β-aminopropionic acid residues (or N-alkyl-β-alanines). This type of peptide mimic has previously been incorporated in biologically active ligands and has been hypothesized to be able to exhibit
Publikováno v:
The Journal of organic chemistry. 80(11)
Peptoids constitute a class of peptidomimetics with potential as protease resistant, biologically active ligands. To harness the full potential of such compounds, however, detailed predictive insight into their propensity to adopt well-defined second