Specificity of Prion Assembly in Vivo
Specificity of Prion Assembly in Vivo
复制标题
体内朊病毒组装的特异性
DOI:
--
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发表时间:
2004
影响因子:
4.8
通讯作者:
S. Liebman
中科院分区:
文献类型:
--
作者:
Sviatoslav N. Bagriantsev;S. Liebman
The yeast prions [PSI+] and [PIN+] are self-propagating amyloid aggregates of the Gln/Asn-rich proteins Sup35p and Rnq1p, respectively. Like the mammalian PrP prion “strains,” [PSI+] and [PIN+] exist in different conformations called variants. Here, [PSI+] and [PIN+] variants were used to model in vivo interactions between co-existing heterologous amyloid aggregates. Two levels of structural organization, like those previously described for [PSI+], were demonstrated for [PIN+]. In cells with both [PSI+] and [PIN+] the two prions formed separate structures at both levels. Also, the destabilization of [PSI+] by certain [PIN+] variants was shown not to involve alterations in the [PSI+] prion size. Finally, when two variants of the same prion that have aggregates with distinct biochemical characteristics were combined in a single cell, only one aggregate type was propagated. These studies demonstrate the intracellular organization of yeast prions and provide insight into the principles of in vivo amyloid assembly.
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影响因子:
3.3
作者:
I. Derkatch;Y. Chernoff;V. Kushnirov;S. Inge-Vechtomov;S. Liebman
通讯作者:
I. Derkatch;Y. Chernoff;V. Kushnirov;S. Inge-Vechtomov;S. Liebman
DOI:
10.1073/pnas.0404968101
发表时间:
2004-08-31
影响因子:
11.1
作者:
Derkatch, IL;Uptain, SM;Liebman, SW
通讯作者:
Liebman, SW
影响因子:
16
作者:
Sondheimer, N;Lindquist, S
通讯作者:
Lindquist, S
影响因子:
3.3
作者:
Derkatch,IL;Bradley,ME;Zhou,P;Chernoff,YO;Liebman,SW
通讯作者:
Liebman,SW
影响因子:
--
作者:
Silveira,JR;Caughey,B;Baron,GS
通讯作者:
Baron,GS