Cargando…

Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion

The formation of amyloid aggregates is related to the onset of a number of human diseases. Recent studies provide compelling evidence for the existence of related fibrillar structures in bacterial inclusion bodies (IBs). Bacteria might thus provide a biologically relevant and tuneable system to stud...

Descripción completa

Detalles Bibliográficos
Autores principales:	Sabaté, Raimon, Espargaró, Alba, Saupe, Sven J, Ventura, Salvador
Formato:	Texto
Lenguaje:	English
Publicado:	BioMed Central 2009
Materias:	Research
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2774669/ https://www.ncbi.nlm.nih.gov/pubmed/19863787 http://dx.doi.org/10.1186/1475-2859-8-56

Ejemplares similares

Yeast prions form infectious amyloid inclusion bodies in bacteria
por: Espargaró, Alba, et al.
Publicado: (2012)

Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors
por: Villar-Piqué, Anna, et al.
Publicado: (2012)

Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion
por: Espargaró, Alba, et al.
Publicado: (2016)

The [Het-s] Prion, an Amyloid Fold as a Cell Death Activation Trigger
por: Saupe, Sven J., et al.
Publicado: (2012)

The Mechanism of Toxicity in HET-S/HET-s Prion Incompatibility
por: Seuring, Carolin, et al.
Publicado: (2012)

Signal Transduction by a Fungal NOD-Like Receptor Based on Propagation of a Prion Amyloid Fold
por: Daskalov, Asen, et al.
Publicado: (2015)

Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability
por: Daskalov, Asen, et al.
Publicado: (2014)

Theme and variations: evolutionary diversification of the HET-s functional amyloid motif
por: Daskalov, Asen, et al.
Publicado: (2015)

Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?
por: Busquets, Maria Antònia, et al.
Publicado: (2015)

Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
por: Espargaró, Alba, et al.
Publicado: (2015)

Ultra rapid in vivo screening for anti-Alzheimer anti-amyloid drugs
por: Espargaró, Alba, et al.
Publicado: (2016)

PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores
por: Zambrano, Rafael, et al.
Publicado: (2015)

Amyloid-Like Protein Inclusions in Tobacco Transgenic Plants
por: Villar-Piqué, Anna, et al.
Publicado: (2010)

What Makes a Protein Sequence a Prion?
por: Sabate, Raimon, et al.
Publicado: (2015)

Dual Inhibitors of Amyloid-β and Tau Aggregation with Amyloid-β Disaggregating Properties: Extended In Cellulo, In Silico, and Kinetic Studies of Multifunctional Anti-Alzheimer’s Agents
por: Pasieka, Anna, et al.
Publicado: (2021)

Genomic Clustering and Homology between HET-S and the NWD2 STAND Protein in Various Fungal Genomes
por: Daskalov, Asen, et al.
Publicado: (2012)

Evolutionary link between metazoan RHIM motif and prion-forming domain of fungal heterokaryon incompatibility factor HET-s/HET-s
por: Kajava, Andrey V., et al.
Publicado: (2014)

Partial Prion Cross-Seeding between Fungal and Mammalian Amyloid Signaling Motifs
por: Bardin, Thierry, et al.
Publicado: (2021)

Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
por: Álvarez-Berbel, Irene, et al.
Publicado: (2022)

The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria
por: Navarro, Susanna, et al.
Publicado: (2015)

Origins and Evolution of the HET-s Prion-Forming Protein: Searching for Other Amyloid-Forming Solenoids
por: Gendoo, Deena M. A., et al.
Publicado: (2011)

Characterization of Amyloid Cores in Prion Domains
por: Sant’Anna, Ricardo, et al.
Publicado: (2016)

Magnetic Nanoparticles Cross the Blood-Brain Barrier: When Physics Rises to a Challenge
por: Busquets, Maria Antònia, et al.
Publicado: (2015)

All-atom simulation of the HET-s prion replication
por: Terruzzi, Luca, et al.
Publicado: (2020)

Azobioisosteres of Curcumin with Pronounced Activity against Amyloid Aggregation, Intracellular Oxidative Stress, and Neuroinflammation
por: Hofmann, Julian, et al.
Publicado: (2021)

Evidence of Protein Adsorption in Pegylated Liposomes: Influence of Liposomal Decoration
por: Sangrà, Marc, et al.
Publicado: (2017)

Characterization of Soft Amyloid Cores in Human Prion-Like Proteins
por: Batlle, Cristina, et al.
Publicado: (2017)

Ribosomal RNA Modulates Aggregation of the Podospora Prion Protein HET-s
por: Pang, Yanhong, et al.
Publicado: (2020)

Functionalized Prion-Inspired Amyloids for Biosensor Applications
por: Díaz-Caballero, Marta, et al.
Publicado: (2021)

Fiber Diffraction of the Prion-Forming Domain HET-s(218–289) Shows Dehydration-Induced Deformation of a Complex Amyloid Structure
por: Wan, William, et al.
Publicado: (2014)

Bacterial Inclusion Bodies Contain Amyloid-Like Structure
por: Wang, Lei, et al.
Publicado: (2008)

Analyzing the Birth and Propagation of Two Distinct Prions, [PSI(+)] and [Het-s](y), in Yeast
por: Mathur, Vidhu, et al.
Publicado: (2010)

Amyloid Fibrils Formed by Short Prion-Inspired Peptides Are Metalloenzymes
por: Navarro, Susanna, et al.
Publicado: (2023)

Natural Variation of Heterokaryon Incompatibility Gene het-c in Podospora anserina Reveals Diversifying Selection
por: Bastiaans, Eric, et al.
Publicado: (2014)

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective
por: Daskalov, Asen, et al.
Publicado: (2021)

En zo rommelt het in het gekkenhuis verder!
Publicado: (2010)

'Het sociale isolement door corona is het ergste'
por: Overduin, Carla
Publicado: (2020)

Kan het helpen, of kan het ook schaden?
por: de Graaf, Toine
Publicado: (2020)

The expanding scope of amyloid signalling
por: Daskalov, Asen, et al.
Publicado: (2021)

Het Behandelpaspoort
por: Bertholet, Ester
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_k67gcsdbemtd5chumqlv1bshkr