pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils

Autor: Christin Pohl, Gregory Effantin, Eaazhisai Kandiah, Sebastian Meier, Guanghong Zeng, Werner Streicher, Dorotea Raventos Segura, Per H. Mygind, Dorthe Sandvang, Line Anker Nielsen, Günther H. J. Peters, Guy Schoehn, Christoph Mueller-Dieckmann, Allan Noergaard, Pernille Harris

Publikováno v: Pohl, C, Effantin, G, Kandiah, E, Meier, S, Zeng, G, Streicher, W, Segura, D R, Mygind, P H, Sandvang, D, Nielsen, L A, Peters, G H J, Schoehn, G, Mueller-Dieckmann, C, Noergaard, A & Harris, P 2022, ' pH-and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils ', Nature Communications, vol. 13, no. 1, 3162 . https://doi.org/10.1038/s41467-022-30462-w
Nature Communications
Nature Communications, 2022, 13 (1), pp.3162. ⟨10.1038/s41467-022-30462-w⟩
Pohl, C, Effantin, G, Kandiah, E, Meier, S, Zeng, G, Streicher, W, Segura, D R, Mygind, P H, Sandvang, D, Nielsen, L A, Peters, G H J, Schoehn, G, Mueller-Dieckmann, C, Noergaard, A & Harris, P 2022, ' pH-and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils ', Nature Communications, vol. 13, 3162 . https://doi.org/10.1038/s41467-022-30462-w

Self-assembly and fibril formation play important roles in protein behaviour. Amyloid fibril formation is well-studied due to its role in neurodegenerative diseases and characterized by refolding of the protein into predominantly β-sheet form. Howev

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::851a084e8130b607038ba7cd1f92e2da
https://curis.ku.dk/portal/da/publications/ph-and-concentrationdependent-supramolecular-assembly-of-a-fungal-defensin-plectasin-variant-into-helical-nonamyloid-fibrils(6e7a7c21-6712-4738-81d8-e42e8d3e7670).html

Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation

Autor: Romain Linares, Charles-Adrien Arnaud, Grégory Effantin, Claudine Darnault, Nathan Hugo Epalle, Elisabetta Boeri Erba, Guy Schoehn, Cécile Breyton

Publikováno v: Science Advances
Science Advances, 2023, 9 (12), pp.eade9674. ⟨10.1126/sciadv.ade9674⟩

The vast majority of bacteriophages (phages) - bacterial viruses - present a tail that allows host recognition, cell wall perforation and safe channelling of the viral DNA from the capsid to the cytoplasm of the infected bacterium. The majority of ta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14528f8d4381b813e2cb5f48bb2495fa
https://doi.org/10.1101/2022.09.20.507954

Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying $Peribunyaviridae$ replication and transcription

Autor: Benoît Arragain, Quentin Durieux Trouilleton, Florence Baudin, Jan Provaznik, Nayara Azevedo, Stephen Cusack, Guy Schoehn, Hélène Malet

Publikováno v: Nature Communications
Nature Communications, 2022, 13 (1), pp.902. ⟨10.1038/s41467-022-28428-z⟩

Segmented negative-strand RNA bunyaviruses encode a multi-functional polymerase that performs genome replication and transcription. Here, we establish conditions for in vitro activity of La Crosse virus polymerase and visualize its conformational dyn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b438e563a5d7aaea928db9dd1675e661
https://hal.univ-grenoble-alpes.fr/hal-03641463/file/arr1.pdf

Nucleation of protein mesocrystals via oriented attachment

Autor: Nani Van Gerven, Rick R. M. Joosten, Wai Li Ling, Alexander E. S. Van Driessche, Nico A. J. M. Sommerdijk, Mike Sleutel, Maria Bacia

Publikováno v: Nature Communications
Nature Communications, 2021, 12, pp.3902. ⟨10.1038/s41467-021-24171-z⟩
Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-021-24171-z⟩
Nature Communications, 2021, 12 (1), ⟨10.1038/s41467-021-24171-z⟩
Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
Nature Communications, 12
Nature Communications, 12, 1
Nature Communications, Nature Publishing Group, 2021, 12, pp.3902. ⟨10.1038/s41467-021-24171-z⟩
Nature Communications, 12(1):3902. Nature Publishing Group

Self-assembly of proteins holds great promise for the bottom-up design and production of synthetic biomaterials. In conventional approaches, designer proteins are pre-programmed with specific recognition sites that drive the association process towar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9d193043e542523da268f8ea4f42202
https://hal.univ-grenoble-alpes.fr/hal-03358785/file/alex1.pdf

Cysteine oxidation and disulfide formation in the ribosomal exit tunnel

Autor: Schulte, Linda, Mao, Jiafei, Reitz, Julian, Sreeramulu, Sridhar, Kudlinzki, Denis, Hodirnau, Victor-Valentin, Meier-Credo, Jakob, Saxena, Krishna, Buhr, Florian, Langer, Julian D., Blackledge, Martin, Frangakis, Achilleas S., Glaubitz, Clemens, Schwalbe, Harald

Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.5569. ⟨10.1038/s41467-020-19372-x⟩
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Nature Communications, 2020, 11 (1), pp.5569. ⟨10.1038/s41467-020-19372-x⟩

Understanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nascent c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56a2fecabdb0052809f19c3a012a7acd
https://hal.univ-grenoble-alpes.fr/hal-03119733