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PMID |
Sentence |
1 |
11447174
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Seven proteins, p76, p62, p48, p45, p41, p37, and p32, were identified as targets of the humoral response during natural infection.
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2 |
11447174
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Most of the other immunodominant proteins, including p48 and p45, were localized to the inner membrane.
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3 |
21543505
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NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62.
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4 |
21543505
|
Its NSs protein has previously been identified as a major virulence factor that suppresses host defense through three distinct mechanisms: it directly inhibits beta interferon (IFN-β) promoter activity, it promotes the degradation of double-stranded RNA-dependent protein kinase (PKR), and it suppresses host transcription by disrupting the assembly of the basal transcription factor TFIIH through sequestration of its p44 subunit.
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5 |
21543505
|
Here, we report that in addition to PKR, NSs also promotes the degradation of the TFIIH subunit p62.
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6 |
21543505
|
These data suggest that the RVFV NSs protein is able to interact with the TFIIH subunit p62 inside infected cells and promotes its degradation, which can occur directly in the nucleus.
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7 |
21543505
|
NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62.
|
8 |
21543505
|
Its NSs protein has previously been identified as a major virulence factor that suppresses host defense through three distinct mechanisms: it directly inhibits beta interferon (IFN-β) promoter activity, it promotes the degradation of double-stranded RNA-dependent protein kinase (PKR), and it suppresses host transcription by disrupting the assembly of the basal transcription factor TFIIH through sequestration of its p44 subunit.
|
9 |
21543505
|
Here, we report that in addition to PKR, NSs also promotes the degradation of the TFIIH subunit p62.
|
10 |
21543505
|
These data suggest that the RVFV NSs protein is able to interact with the TFIIH subunit p62 inside infected cells and promotes its degradation, which can occur directly in the nucleus.
|
11 |
21543505
|
NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62.
|
12 |
21543505
|
Its NSs protein has previously been identified as a major virulence factor that suppresses host defense through three distinct mechanisms: it directly inhibits beta interferon (IFN-β) promoter activity, it promotes the degradation of double-stranded RNA-dependent protein kinase (PKR), and it suppresses host transcription by disrupting the assembly of the basal transcription factor TFIIH through sequestration of its p44 subunit.
|
13 |
21543505
|
Here, we report that in addition to PKR, NSs also promotes the degradation of the TFIIH subunit p62.
|
14 |
21543505
|
These data suggest that the RVFV NSs protein is able to interact with the TFIIH subunit p62 inside infected cells and promotes its degradation, which can occur directly in the nucleus.
|
15 |
26254061
|
Autophagy is involved in oral rAAV/Aβ vaccine-induced Aβ clearance in APP/PS1 transgenic mice.
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16 |
26254061
|
In this study, we first demonstrated that oral vaccination with rAAV/Aß decreased the p62 level and up-regulated the LC3B-II/LC3B-I ratio in APP/PS1 mouse brain, suggesting enhanced autophagy.
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17 |
26254061
|
Further, inhibition of the Akt/mTOR pathway may account for autophagy enhancement.
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18 |
26254061
|
We also found increased anti-Aß antibodies in the sera of APP/PS1 mice with oral vaccination, accompanied by elevation of complement factors C1q and C3 levels in the brain.
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