192 related articles for article (PubMed ID: 22677387)
1. Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold.
Wan W; Wille H; Stöhr J; Baxa U; Prusiner SB; Stubbs G
Biophys J; 2012 May; 102(10):2339-44. PubMed ID: 22677387
[TBL] [Abstract][Full Text] [Related]
2. Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).
Wan W; Bian W; McDonald M; Kijac A; Wemmer DE; Stubbs G
J Biol Chem; 2013 Oct; 288(41):29604-12. PubMed ID: 23986444
[TBL] [Abstract][Full Text] [Related]
3. Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry.
Nazabal A; Maddelein ML; Bonneu M; Saupe SJ; Schmitter JM
J Biol Chem; 2005 Apr; 280(14):13220-8. PubMed ID: 15647259
[TBL] [Abstract][Full Text] [Related]
4. Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold.
Daskalov A; Habenstein B; Martinez D; Debets AJ; Sabaté R; Loquet A; Saupe SJ
PLoS Biol; 2015 Feb; 13(2):e1002059. PubMed ID: 25671553
[TBL] [Abstract][Full Text] [Related]
5. The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility.
Saupe SJ
Semin Cell Dev Biol; 2011 Jul; 22(5):460-8. PubMed ID: 21334447
[TBL] [Abstract][Full Text] [Related]
6. Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomes.
Daskalov A; Paoletti M; Ness F; Saupe SJ
PLoS One; 2012; 7(4):e34854. PubMed ID: 22493719
[TBL] [Abstract][Full Text] [Related]
7. The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo.
Balguerie A; Dos Reis S; Coulary-Salin B; Chaignepain S; Sabourin M; Schmitter JM; Saupe SJ
J Cell Sci; 2004 May; 117(Pt 12):2599-610. PubMed ID: 15159455
[TBL] [Abstract][Full Text] [Related]
8. Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.
Daskalov A; Gantner M; Wälti MA; Schmidlin T; Chi CN; Wasmer C; Schütz A; Ceschin J; Clavé C; Cescau S; Meier B; Riek R; Saupe SJ
PLoS Pathog; 2014 Jun; 10(6):e1004158. PubMed ID: 24945274
[TBL] [Abstract][Full Text] [Related]
9. Prion and non-prion amyloids of the HET-s prion forming domain.
Sabaté R; Baxa U; Benkemoun L; Sánchez de Groot N; Coulary-Salin B; Maddelein ML; Malato L; Ventura S; Steven AC; Saupe SJ
J Mol Biol; 2007 Jul; 370(4):768-83. PubMed ID: 17532341
[TBL] [Abstract][Full Text] [Related]
10. The mechanism of toxicity in HET-S/HET-s prion incompatibility.
Seuring C; Greenwald J; Wasmer C; Wepf R; Saupe SJ; Meier BH; Riek R
PLoS Biol; 2012; 10(12):e1001451. PubMed ID: 23300377
[TBL] [Abstract][Full Text] [Related]
11. Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity.
Benkemoun L; Sabaté R; Malato L; Dos Reis S; Dalstra H; Saupe SJ; Maddelein ML
Methods; 2006 May; 39(1):61-7. PubMed ID: 16750391
[TBL] [Abstract][Full Text] [Related]
12. Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids.
Gendoo DM; Harrison PM
PLoS One; 2011; 6(11):e27342. PubMed ID: 22096554
[TBL] [Abstract][Full Text] [Related]
13. Infectious fold and amyloid propagation in Podospora anserina.
Maddelein ML
Prion; 2007; 1(1):44-7. PubMed ID: 19164904
[TBL] [Abstract][Full Text] [Related]
14. Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis.
Daskalov A; Habenstein B; Sabaté R; Berbon M; Martinez D; Chaignepain S; Coulary-Salin B; Hofmann K; Loquet A; Saupe SJ
Proc Natl Acad Sci U S A; 2016 Mar; 113(10):2720-5. PubMed ID: 26903619
[TBL] [Abstract][Full Text] [Related]
15. Amyloids and yeast prion biology.
Wickner RB; Edskes HK; Bateman DA; Kelly AC; Gorkovskiy A; Dayani Y; Zhou A
Biochemistry; 2013 Mar; 52(9):1514-27. PubMed ID: 23379365
[TBL] [Abstract][Full Text] [Related]
16. The HET-S/s Prion Motif in the Control of Programmed Cell Death.
Riek R; Saupe SJ
Cold Spring Harb Perspect Biol; 2016 Sep; 8(9):. PubMed ID: 27352624
[TBL] [Abstract][Full Text] [Related]
17. Amyloid aggregates of the HET-s prion protein are infectious.
Maddelein ML; Dos Reis S; Duvezin-Caubet S; Coulary-Salin B; Saupe SJ
Proc Natl Acad Sci U S A; 2002 May; 99(11):7402-7. PubMed ID: 12032295
[TBL] [Abstract][Full Text] [Related]
18. Correlation of structural elements and infectivity of the HET-s prion.
Ritter C; Maddelein ML; Siemer AB; Lührs T; Ernst M; Meier BH; Saupe SJ; Riek R
Nature; 2005 Jun; 435(7043):844-8. PubMed ID: 15944710
[TBL] [Abstract][Full Text] [Related]
19. Structural and molecular basis of cross-seeding barriers in amyloids.
Daskalov A; Martinez D; Coustou V; El Mammeri N; Berbon M; Andreas LB; Bardiaux B; Stanek J; Noubhani A; Kauffmann B; Wall JS; Pintacuda G; Saupe SJ; Habenstein B; Loquet A
Proc Natl Acad Sci U S A; 2021 Jan; 118(1):. PubMed ID: 33443172
[TBL] [Abstract][Full Text] [Related]
20. Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity.
Wasmer C; Zimmer A; Sabaté R; Soragni A; Saupe SJ; Ritter C; Meier BH
J Mol Biol; 2010 Sep; 402(2):311-25. PubMed ID: 20600104
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]