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1 in yeast are infectious when introduced into Podospora.
2 nt independent discovery of ST production in Podospora [1], suggest that this HGT event probably resu
4 four prions of Saccharomyces cerevisiae and Podospora anserina affect diverse biological processes:
5 ls of recombinant prion proteins from yeast, Podospora anserina and mammals can induce prion phenotyp
7 MAGA, and CPG-2 from the saprophytic fungus Podospora anserina and the pathogenic fungi Magnaporthe
8 sidues 218-289 of the HET-s prion protein of Podospora anserina by factors of three or more, indicati
9 4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradati
11 glutamine/asparagine (Q/N)-rich regions, the Podospora anserina HET-s and PrP prion proteins lack suc
12 GLTP, we recently showed that HET-C2 GLTP of Podospora anserina is organized conformationally as a GL
13 s are plainly diseases, the [Het-s] prion of Podospora anserina may be a functional amyloid, with imp
15 e mitochondria from the aging model organism Podospora anserina revealed profound age-dependent chang
17 iscovered that a complete ST gene cluster in Podospora anserina was horizontally transferred from Asp
18 identified in this fashion, PODANSg2158 from Podospora anserina was selected for expression and chara
20 han that of their homologs in another fungus Podospora anserina with a well-characterized senescence.
22 to Het-E1 (vegetative incompatibility) from Podospora anserina, acylaminoacyl-peptidase from Bacillu
23 e.g., mammalian PrP and the [Het-s] prion of Podospora anserina, although still able to form infectio
24 l amyloid aggregate in the filamentous fungi Podospora anserina, and is involved in mediating heterok
25 o fungi models, Saccharomyces cerevisiae and Podospora anserina, previously transformed to express Ab
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