Suchergebnisse

Filtern nach

Letzte Suchanfragen

Ergebnisse für *

Es wurden 3 Ergebnisse gefunden.

Zeige Ergebnisse 1 bis 3 von 3.

Sortieren

NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice

Autor*in: Léger, Psylvia ; Nachman, Eliana ; Richter, Karsten ; Tamietti, Carole ; Koch, Jana ; Burk, Robin ; Kummer, Susann ; Xin, Qilin ; Stanifer, Megan ; Bouloy, Michèle ; Boulant, Steeve ; Kräusslich, Hans-Georg ; Montagutelli, Xavier ; Flamand, Marie ; Nussbaum-Krammer, Carmen ; Lozach, Pierre-Yves

Erschienen: 2020

Verlag: HAL CCSD ; Nature Publishing Group

Volltext:	https://hal-pasteur.archives-ouvertes.fr/pasteur-02949167 https://hal-pasteur.archives-ouvertes.fr/pasteur-02949167/document https://hal-pasteur.archives-ouvertes.fr/pasteur-02949167/file/s41467-020-17101-y.pdf
Zitierfähiger Link:	https://doi.org/10.1038/s41467-020-17101-y

International audience ; Amyloid fibrils result from the aggregation of host cell-encoded proteins, many giving rise to specific human illnesses such as Alzheimer's disease. Here we show that the major virulence factor of Rift Valley fever virus, the protein NSs, forms filamentous structures in the brain of mice and affects mortality. NSs assembles into nuclear and cytosolic disulfide bond-dependent fibrillary aggregates in infected cells. NSs structural arrangements exhibit characteristics typical for amyloids, such as an ultrastructure of 12 nm-width fibrils, a strong detergent resistance, and interactions with the amyloid-binding dye Thioflavin-S. The assembly dynamics of viral amyloid-like fibrils can be visualized in real-time. They form spontaneously and grow in an amyloid fashion within 5 hours. Together, our results demonstrate that viruses can encode amyloid-like fibril-forming proteins and have strong implications for future research on amyloid aggregation and toxicity in general.

Export in Literaturverwaltung

RIS-Format
BibTeX-Format

Quelle:	BASE Fachausschnitt Germanistik
Sprache:	Englisch
Medientyp:	Aufsatz aus einer Zeitschrift
Format:	Online
Übergeordneter Titel:	ISSN: 2041-1723 ; EISSN: 2041-1723 ; Nature Communications ; https://hal-pasteur.archives-ouvertes.fr/pasteur-02949167 ; Nature Communications, 2020, 11 (1), pp.3281. ⟨10.1038/s41467-020-17101-y⟩
Schlagworte:	MESH: Amyloid; MESH: Amyloidogenic Proteins; MESH: Animals; MESH: Cell Line; Tumor; MESH: Cell Nucleus; MESH: Chlorocebus aethiops; MESH: HeLa Cells; MESH: Humans; MESH: Mice; MESH: Microscopy; Confocal; Electron; Transmission; MESH: Protein Aggregation; Pathological; MESH: Rift Valley Fever; MESH: Rift Valley fever virus; MESH: Vero Cells; MESH: Viral Nonstructural Proteins; MESH: Virulence; MESH: Virulence Factors; [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
Lizenz:	creativecommons.org/licenses/by/ ; info:eu-repo/semantics/OpenAccess

Observations on fungus haematodes or soft cancer, in several of the most important organs of the human body

containing also a comparative view of the structure of fungus haematodes and cancer

Autor*in: Wardrop, James

Erschienen: 1809

Verlag: Constable [u.a.], Edinburgh

Berlin: Staatsbibliothek zu Berlin - Preußischer Kulturbesitz, Haus Potsdamer Straße

Standort:

Staatsbibliothek zu Berlin - Preußischer Kulturbesitz, Haus Potsdamer Straße

Signatur:

8"Jx 7325

Fernleihe:

keine Fernleihe

Link zum Verbundkatalog:

Quelle:	Herzog August Bibliothek Wolfenbüttel
Sprache:	Englisch
Medientyp:	Buch (Monographie)
Format:	Druck
Schlagworte:	Markschwamm; Krebs <Medizin>; Tumor; Krankheit; Medizin;
Umfang:	XIII, 205 S, 8°

Filtern nach

Aktive Filter

Kategorien:

Bereich

Quelle

Format

Beteiligt

Medientyp

Sprache

Jahr

Letzte Suchanfragen

Ergebnisse für *

NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice

Observations on fungus haematodes or soft cancer, in several of the most important organs of the human body

Viruses and tumours