Cargando…

Origins and Evolution of the HET-s Prion-Forming Protein: Searching for Other Amyloid-Forming Solenoids

The HET-s prion-forming domain from the filamentous fungus Podospora anserina is gaining considerable interest since it yielded the first well-defined atomic structure of a functional amyloid fibril. This structure has been identified as a left-handed beta solenoid with a triangular hydrophobic core...

Descripción completa

Detalles Bibliográficos
Autores principales:	Gendoo, Deena M. A., Harrison, Paul M.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2011
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3214033/ https://www.ncbi.nlm.nih.gov/pubmed/22096554 http://dx.doi.org/10.1371/journal.pone.0027342

Ejemplares similares

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)

PrionHome: A Database of Prions and Other Sequences Relevant to Prion Phenomena
por: Harbi, Djamel, 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)

The Landscape of the Prion Protein's Structural Response to Mutation Revealed by Principal Component Analysis of Multiple NMR Ensembles
por: Gendoo, Deena M. A., et al.
Publicado: (2012)

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)

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

Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion
por: Sabaté, Raimon, et al.
Publicado: (2009)

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

Variable absorption of mutational trends by prion-forming domains during Saccharomycetes evolution
por: Harrison, Paul M.
Publicado: (2020)

UV-Light Exposed Prion Protein Fails to Form Amyloid Fibrils
por: Thakur, Abhay Kumar, et al.
Publicado: (2008)

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

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

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

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

Emergence and evolution of yeast prion and prion-like proteins
por: An, Lu, et al.
Publicado: (2016)

Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
por: Macedo, Bruno, et al.
Publicado: (2015)

HetL, HetR and PatS form a reaction-diffusion system to control pattern formation in the cyanobacterium nostoc PCC 7120
por: Xu, Xiaomei, et al.
Publicado: (2020)

Prion Protein: The Molecule of Many Forms and Faces
por: Kovač, Valerija, et al.
Publicado: (2022)

Comparing the Folds of Prions and Other Pathogenic Amyloids
por: Flores-Fernández, José Miguel, et al.
Publicado: (2018)

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

Ex vivo mammalian prions are formed of paired double helical prion protein fibrils
por: Terry, Cassandra, et al.
Publicado: (2016)

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

Glycoform-Selective Prion Formation in Sporadic and Familial Forms of Prion Disease
por: Xiao, Xiangzhu, et al.
Publicado: (2013)

Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion
por: Abskharon, Romany, et al.
Publicado: (2019)

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

Correction: Glycoform-Selective Prion Formation in Sporadic and Familial Forms of Prion Disease
por: Xiao, Xiangzhu, et al.
Publicado: (2013)

MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
por: Batlle, Cristina, et al.
Publicado: (2021)

Amyloid Core Formed of Full-Length Recombinant Mouse Prion Protein Involves Sequence 127–143 but Not Sequence 107–126
por: Chatterjee, Biswanath, et al.
Publicado: (2013)

Tor forms a dimer through an N-terminal helical solenoid with a complex topology
por: Baretić, Domagoj, et al.
Publicado: (2016)

The RHIM of the Immune Adaptor Protein TRIF Forms Hybrid Amyloids with Other Necroptosis-Associated Proteins
por: Baker, Max O. D. G., et al.
Publicado: (2022)

Porcine prion protein amyloid
por: Hammarström, Per, et al.
Publicado: (2015)

Distinct patterns of spread of prion infection in brains of mice expressing anchorless or anchored forms of prion protein
por: Rangel, Alejandra, et al.
Publicado: (2014)

PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions
por: Barron, Rona M., et al.
Publicado: (2016)

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)

Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae
por: Keefer, Kathryn M., et al.
Publicado: (2017)

Bioinformatics and computational approaches for analyzing patient-derived disease models in cancer research
por: Gendoo, Deena M.A.
Publicado: (2020)

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

In het kort
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_s3hrkrurkg537432dh0darjmja