Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Francesco S, Ielasi"'
Publikováno v:
Nature. 606:1015-1020
The liver takes up bile salts from blood to generate bile, enabling absorption of lipophilic nutrients and excretion of metabolites and drugs1. Human Na+–taurocholate co-transporting polypeptide (NTCP) is the main bile salt uptake system in liver.
Autor:
Laura Mariño Pérez, Francesco S. Ielasi, Luiza M. Bessa, Damien Maurin, Jaka Kragelj, Martin Blackledge, Nicola Salvi, Guillaume Bouvignies, Andrés Palencia, Malene Ringkjøbing Jensen
Publikováno v:
Nature
Nature, 2022, ⟨10.1038/s41586-022-04417-6⟩
'Nature ', vol: 602, pages: 695-700 (2022)
Nature, 2022, ⟨10.1038/s41586-022-04417-6⟩
'Nature ', vol: 602, pages: 695-700 (2022)
Aromatic residues cluster in the core of folded proteins, where they stabilize the structure through multiple interactions. Nuclear magnetic resonance (NMR) studies in the 1970s showed that aromatic side chains can undergo ring flips—that is, 180°
Autor:
Francesco S Ielasi, Sara Ternifi, Emeline Fontaine, Domenico Iuso, Yohann Couté, Andrés Palencia
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2022, 50 (21), pp.12425-12443. ⟨10.1093/nar/gkac878⟩
Nucleic Acids Research, 2022, 50 (21), pp.12425-12443. ⟨10.1093/nar/gkac878⟩
Human pre-mRNA processing relies on multi-subunit macromolecular complexes, which recognize specific RNA sequence elements essential for assembly and activity. Canonical pre-mRNA processing proceeds via the recognition of a polyadenylation signal (PA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed141a97586fb329bf7a15f53f6fe2ff
https://hal.science/hal-04065783
https://hal.science/hal-04065783
Autor:
Francesco S. Ielasi, Mitchel Alioscha-Perez, Dagmara Donohue, Sandra Claes, Hichem Sahli, Dominique Schols, Ronnie G. Willaert
Publikováno v:
mBio, Vol 7, Iss 4 (2016)
ABSTRACT The first step in the infection of humans by microbial pathogens is their adherence to host tissue cells, which is frequently based on the binding of carbohydrate-binding proteins (lectin-like adhesins) to human cell receptors that expose gl
Externí odkaz:
https://doaj.org/article/b23f771303964066863bc08ffeb0ab0e
Autor:
Katty V. Y. Goossens, Francesco S. Ielasi, Intawat Nookaew, Ingeborg Stals, Livan Alonso-Sarduy, Luk Daenen, Sebastiaan E. Van Mulders, Catherine Stassen, Rudy G. E. van Eijsden, Verena Siewers, Freddy R. Delvaux, Sandor Kasas, Jens Nielsen, Bart Devreese, Ronnie G. Willaert
Publikováno v:
mBio, Vol 6, Iss 2 (2015)
ABSTRACT We studied the flocculation mechanism at the molecular level by determining the atomic structures of N-Flo1p and N-Lg-Flo1p in complex with their ligands. We show that they have similar ligand binding mechanisms but distinct carbohydrate spe
Externí odkaz:
https://doaj.org/article/a1816c75be7446cca3f2fd3d70437adf
Publikováno v:
Molecular microbiology. 80(6)
The opportunistic pathogen Candida albicans expresses on its surface Als (Agglutinin like sequence) proteins, which play an important role in the adhesion to host cells and in the development of candidiasis. The binding specificity of these proteins