Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Christos Tsiamantas"'
Publikováno v:
Angewandte Chemie (International Ed. in English)
Derivatives of 4‐aminomethyl‐l‐phenylalanine with aromatic oligoamide foldamers as sidechain appendages were successfully charged on tRNA by means of flexizymes. Their subsequent incorporation both at the C‐terminus of, and within, peptide se
Publikováno v:
Chemical Communications. 56:4265-4272
Ribosomal peptide synthesis begins almost exclusively with the amino acid methionine, across all domains of life. The ubiquity of methionine initiation raises the question; to what extent could polypeptide synthesis be realized with other amino acids
Autor:
Sebastian Dengler, Ryan T. Howard, Vasily Morozov, Christos Tsiamantas, Zhiwei Liu, Christopher Dobrzanski, Vojislava Pophristic, Sophie Brameyer, Céline Douat, Hiroaki Suga, Ivan Huc
A helical aromatic foldamer was identified that undergoes tRNA acylation by a flexizyme and ribosomal peptide initiation with yields sufficiently high to perform an mRNA display selection of macrocyclic foldamer-peptide hybrids. A hybrid macrocyle bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::761abc8ad402295a08324d7487ed7cd7
https://doi.org/10.26434/chemrxiv-2022-5rlmv
https://doi.org/10.26434/chemrxiv-2022-5rlmv
Publikováno v:
Chemical Communications. 55:7366-7369
The tolerance of ribosomal peptide translation for helical aromatic oligoamide foldamers appended as initiators has been investigated. Small cationic foldamer side-chains were shown to expand the range of foldamer-peptide hybrids that can be produced
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2001
Flexizymes, highly flexible tRNA aminoacylation ribozymes, have enabled charging of virtually any amino acid (including non-proteogenic ones) onto tRNA molecules. Coupling to a custom-made in vitro translation system, namely the flexible in vitro tra
Publikováno v:
Methods in Molecular Biology ISBN: 9781493995035
Flexizymes, highly flexible tRNA aminoacylation ribozymes, have enabled charging of virtually any amino acid (including non-proteogenic ones) onto tRNA molecules. Coupling to a custom-made in vitro translation system, namely the flexible in vitro tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::62d6997a41e259e2552c22ddede09e7b
https://doi.org/10.1007/978-1-4939-9504-2_14
https://doi.org/10.1007/978-1-4939-9504-2_14
Autor:
Nils Metzler-Nolte, Céline Douat, Makoto Takafuji, Ivan Huc, Christos Tsiamantas, Brice Kauffmann, Victor Maurizot, Hirotaka Ihara, Xavier de Hatten
Publikováno v:
Angewandte Chemie. 128:6962-6966
Disulfide bridge formation was investigated in helical aromatic oligoamide foldamers. Depending on the position of thiol-bearing side chains, exclusive intramolecular or intermolecular disulfide bridging may occur. The two processes are capable of se
Publikováno v:
Current opinion in biotechnology. 58
Ribosomal incorporation of non-proteinogenic amino acids (NPaa) into peptides have made significant progress in recent years. These non-standard peptides have been utilized for a plethora of applications in the fields of chemical biology and therapeu
Publikováno v:
Polymer Journal. 45:1216-1223
Model asymmetric miktoarm star copolymers of the type AA′B, where A and A′ are polyisoprenes (PIs) and B is deuterated polystyrene (PS), were synthesized by anionic polymerization high-vacuum techniques. Their micellization behavior was studied i
Publikováno v:
Comptes Rendus. Chimie
Comptes Rendus. Chimie, Académie des sciences (Paris), 2016, 19 (1-2), pp.132-142. ⟨10.1016/j.crci.2015.06.007⟩
Comptes Rendus. Chimie, Académie des sciences (Paris), 2016, 19 (1-2), pp.132-142. ⟨10.1016/j.crci.2015.06.007⟩
International audience; A series of octameric quinoline oligoamide foldamers has been synthesized consisting exclusively of monomers which display mono-, di-, tri- or tetraethylene glycol side-chains. These oligomers adopt stable helical conformation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99cf37f163dc312cdfb7bcc70e403f45
https://hal.archives-ouvertes.fr/hal-01509473
https://hal.archives-ouvertes.fr/hal-01509473