Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Mateusz Imiołek"'
Publikováno v:
Journal of Chromatography Open, Vol 6, Iss , Pp 100187- (2024)
With this work, we present a comprehensive tutorial for the analysis of oligonucleotides (ONs, 5 to 100 mer) using ion-pair reversed-phase liquid chromatography (IP-RPLC) on ultra-short columns (20 × 2.1 mm). We explore the impact of ion-pairing (IP
Externí odkaz:
https://doaj.org/article/7091a7b2a27c48a698281f30664c32bf
Autor:
Mateusz Imiołek, Patrick G. Isenegger, Wai-Lung Ng, Aziz Khan, Véronique Gouverneur, Benjamin G. Davis
Publikováno v:
ACS Central Science, Vol 7, Iss 1, Pp 145-155 (2021)
Externí odkaz:
https://doaj.org/article/891c31bca4b745b8931fa54f6ed10163
Autor:
Mateusz Imiołek, Nicolas Winssinger
Peptidic motifs folded in a defined conformation are able to inhibit protein-protein interactions (PPIs) covering large interfaces and as such they are biomedical molecules of interest. Mimicry of such natural structures with synthetically tractable
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0761f5fada91d2fe72c03cf671796e2f
Autor:
Szabolcs Fekete, Megane K. Aebischer, Mateusz Imiołek, Tobias Graf, Raphael Ruppert, Matthew Lauber, Valentina D’Atri, Davy Guillarme
Publikováno v:
TrAC Trends in Analytical Chemistry. 164:117088
Autor:
Véronique Gouverneur, Mateusz Imiołek, Benjamin G. Davis, Aziz Khan, Patrick G. Isenegger, Wai-Lung Ng
Publikováno v:
ACS Central Science
ACS Central Science, Vol 7, Iss 1, Pp 145-155 (2021)
ACS Central Science, Vol 7, Iss 1, Pp 145-155 (2021)
The carbonyl group is now a widely useful, nonproteinogenic functional group in chemical biology, yet methods for its generation in proteins have relied upon either cotranslational incorporation of unnatural amino acids bearing carbonyls or oxidative
Stapled peptides with an enforced α-helical conformation have been shown to overcome major limitations in the development of short peptides targeting protein-protein interactions (PPI). While the growing arsenal of methodologies to staple peptides f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fb9c719d4d775220c0f152c11814912
Publikováno v:
Journal of the American Chemical Society, Vol. 143, No 45 (2021) pp. 18932-18940
Stapled peptides with an enforced α-helical conformation have been shown to overcome major limitations in the development of short peptides targeting protein-protein interactions (PPIs). While the growing arsenal of methodologies to staple peptides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc59cf7d34ae878a754bebb259d7cf67
https://archive-ouverte.unige.ch/unige:156465
https://archive-ouverte.unige.ch/unige:156465
Autor:
Stefan Verhoog, Thomas C. Wilson, Jane K. Sosabowski, Véronique Gouverneur, Giulia Boscutti, Christophe Plisson, Florian Guibbal, Jan Passchier, Sharon Ashworth, Mateusz Imiołek, Michael J. Tilby, Sven Macholl, Benjamin G. Davis, Choon Wee Kee, Adeline W. J. Poh, Bart Cornelissen, Osman Tack, Juliette Chupin, Michael C. Willis, Patrick G. Isenegger, Roxana Kashani
Publikováno v:
Journal of the American Chemical Society
18F labeling strategies for unmodified peptides with [18F]fluoride require 18F-labeled prosthetics for bioconjugation more often with cysteine thiols or lysine amines. Here we explore selective radical chemistry to target aromatic residues applying C
Autor:
Wai-Lung Ng, Andrew Baldwin, Benjamin G. Davis, Mateusz Imiołek, Gogulan Karunanithy, Véronique Gouverneur
Publikováno v:
Journal of the American Chemical Society
The incorporation of fluorine can not only significantly facilitate the study of proteins but also potentially modulate their function. Though some biosynthetic methods allow global residue-replacement, post-translational fluorine incorporation would