SUP35 Antibody

1. The role of SUP35 in protein folding in the ribosome and prion propagation PMID: 27633137
2. With the use of both segmental and specific isotopic labeling schemes in combination with dynamic nuclear polarization (DNP) NMR, the study examined an amyloid form of Sup35NM that does not have a parallel in-register structure. PMID: 28330994
3. In stressed conditions, Sup35 formed protective gels via pH-regulated liquid-like phase separation followed by gelation. PMID: 29301985
4. proteolytic cleavage of Sup35 suppresses spontaneous de novo generation of the [PSI(+)] prion. PMID: 29038292
5. we discovered a non-chromosomal factor, [NSI+], which possesses the main features of yeast prions, including cytoplasmic infectivity, reversible curability, dominance, and non-Mendelian inheritance in meiosis. This factor causes omnipotent suppression of nonsense mutations in strains of S. cerevisiae bearing a deleted or modified Sup35 N-terminal domain PMID: 28027291
6. our observations suggest that these sequence elements make complementary contributions to prion propagation, with the repeat proximal region promoting chaperone binding to and the repeats promoting chaperone processing of Sup35 amyloid PMID: 27814358
7. Sup35 becomes oxidized and aggregates during oxidative stress conditions and plays a role in [PSI+] prion formation. PMID: 28369054
8. It was found that ABF1, FKH2, and REB1 overexpression decreased the growth of strains in a prion-dependent manner and, thus, might influence [PSI;(+)] prion toxicity. PMID: 27830682
9. Autophagy therefore normally functions to remove oxidatively damaged Sup35, which accumulates in cells grown under aerobic conditions, but in the absence of autophagy, damaged/misfolded Sup35 undergoes structural transitions . PMID: 26490118
10. DnaJB6 prevented purified Sup35NM from forming amyloids at 37 degrees C, which produce predominantly weak [PSI(+)] variants when used to infect yeast PMID: 26702057
11. findings show Sup35p is secreted within extracellular vesicles (EV)released in the extracellular medium of yeast cultures; demonstrated that Sup35p within EV isolated from strong and weak [PSI(+)] cells is in an infectious prion conformation PMID: 26286691
12. Dynamic nuclear polarization of nuclear magnetic resonance of Sup35 amyloid fibers, NM, show structure in its biological context indicates that these organizing protein-protein interactions are mediated through the M domain of the protein via the adoption of a beta sheet secondary structure by the majority of this otherwise intrinsically disordered region. PMID: 26456111
13. findings show that oxidation of Sup35 is a common response to oxidative stress and results in Sup35 conversion to the [PSI+] state PMID: 25601439
14. A hybrid modelling approach is presented enabling detailed analysis of a highly ordered and hierarchically organized fibril of the GNNQQNY peptide fragment of a yeast prion protein SUP35. PMID: 25849399
15. Amino Acid Proximities in Two Sup35 Prion Strains PMID: 26265470
16. Data indicate mutations decrease amyloid formation in the prion protein Sup35. PMID: 24817093
17. The data obtained have refined a supposed organization of beta-sheets forming by different regions of Sup35p prion-forming domain within amyloid. PMID: 25850301
18. Sup35(7-13) is observed to organize into anti-parallel and parallel beta-sheet arrangements. Confinement in the sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles stabilizes extended peptide conformations and enhance peptide aggregation. PMID: 25494801
19. [PIN+] drives Pin4C into a toxic hyperphosphorylated species. PMID: 25039275
20. analysis of amino acid requirements for formation and maintenance of the [PSI] prion in yeast PMID: 25547291
21. In Saccharomyces cerevisiae the association of Pab1 with eRF3 negatively regulates translation termination. PMID: 25411355
22. the influence of SUP35 and VTS1 on [NSI+] PMID: 25474892
23. Strikingly, exposure to specific stressful environments dramatically altered the variants of Sup35 [PSI(+)] that formed de novo. PMID: 24628771
24. Lsb1 is crucial for prion maintenance during stress. PMID: 25143386
25. Sup35pC may serve as actin modulator during mitosis. PMID: 24549315
26. Sup35p is degraded in vitro by the 26S and 20S proteasomes in a ubiquitin-independent manner, generating an array of amyloidogenic peptides derived from its prion-domain. PMID: 24589377
27. Data shows that the translation termination factor Sup35 is required for premature translation termination. PMID: 25154418
28. The Sup35/Pub1 complex, which also contains TUB1 mRNA and components of translation machinery, is important for the integrity of the tubulin cytoskeleton. PMID: 24981173
29. Data indicate that the Sup35(GPI) aggregates corresponded to dense cell surface accumulations of membrane vesicle-like structures and were not fibrillar. PMID: 24627481
30. A conformation analysis of both full-length Sup35 and also from its isolated NM domain shows that Sup35NM and fragments thereof, which are often used as convenient models for prion fibril assembly, have a very different conformation of the prion domains. PMID: 24123863
31. Authors show that even within a single cell, Sup35 retains the potential to fold into more than one variant type. PMID: 22998111
32. the effect of Hofmeister ions on amyloid nucleation and strain generation by the prion domain-containing fragment (Sup35NM) of a yeast protein Sup35p. PMID: 23990463
33. Data indicate that SUP35 ORF (eRF3) affects binding between SUP45 ORF (eRF1) and the ribosome, either prior to or subsequent to peptide release. PMID: 23963452
34. This study reveals an unexpected interplay between the wild type Sup35p and proteins expressed from the sup35(KK) alleles during prionization. PMID: 23965990
35. found that over-production of C-terminally truncated multi-transmembrane (MTM) mutant proteins triggers HSR, but not UPR, and clearance of yeast prions [PSI(+)] and [URE3] PMID: 23384482
36. Mutations in a Gly58-Gly59 pair in Sup35 inhibit propagation of the [PSI+] prion. PMID: 23746351
37. We find that among the rare wild isolates containing [PSI(+)], all indistinguishably "weak" [PSI(+)], are several different variants based on their transmission efficiencies to other Sup35 alleles PMID: 23382698
38. The yeast prions [URE3] and [PSI] are not found in wild strains, suggesting they are not an advantage.Recently, we showed that the array of [PSI] and [URE3] prions includes a majority of lethal or very toxic variants. PMID: 22052353
39. Study investigated the interaction between Hsp104 and Sup35, the priongenic protein in yeast that forms the [PSI+] prion; found that a 20-amino acid segment within the highly-charged, unstructured middle domain of Sup35 contributes to the physical interaction between the middle domain and Hsp104. PMID: 22561166
40. Data indicate that the toxicity of 103 glutamines (HttQ103) in yeast containing the [PSI(+)] prion is primarily due to sequestration of the essential protein, Sup35. PMID: 22573320
41. genetic interaction is present between SKY1 and SUP35 in the presence of diamide and hydrogen peroxide in the BY background but not in the RM background. PMID: 22396662
42. SUP35 gene modulates nonsense suppression in S. cerevisiae PMID: 22215010
43. a causal link between Sup35 protein oxidation and de novo [PSI(+)] prion formation. PMID: 21832086
44. Data show that full-length New1 broke the Sup35NM amyloid fibrils in an ATP-dependent manner. PMID: 21453424
45. Class I deletions (bug1Delta, bem1Delta, arf1Delta, and hog1Delta) reduced the efficiency of [PSI+] induction, but formed rings normally. Class II deletions (las17Delta, vps5Delta, and sac6Delta) inhibited both [PSI+] induction and ring formation PMID: 21625618
46. Data report here over half of Saccharomyces cerevisiae [PSI(+)] variants are sick or lethal, and give a more realistic picture of the impact of the prion change than does focus on "mild" prion variants. PMID: 21402947
47. By negative staining, cryo-EM and scanning transmission EM (STEM), filaments of full-length Sup35p show a thin backbone fibril surrounded by a diffuse 65-nm-wide cloud of globular C-domains. PMID: 21219467
48. aggregation of Sup35p strictly depended on the presence of MgCl(2) stress in our strains PMID: 20937039
49. show that the yeast Tsa1/Tsa2 peroxiredoxins colocalize to ribosomes and function to protect the Sup35 translation termination factor against oxidative stress-induced formation of its heritable [PSI(+)] prion conformation. PMID: 20308573
50. sup35 mutations do not only decrease translation fidelity but also influence mRNA stability. PMID: 20198859

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