Virus-specific effects of TRIM5α(rh) RING domain functions on restriction of retroviruses.
about
Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid latticePrimate TRIM5 proteins form hexagonal nets on HIV-1 capsids.The human antiviral factor TRIM11 is under the regulation of HIV-1 Vpr.Ring finger protein 39 genetic variants associate with HIV-1 plasma viral loads and its replication in cell culture.Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies.Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction.Prospects in Innate Immune Responses as Potential Control Strategies against Non-Primate Lentiviruses
P2860
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P2860
Virus-specific effects of TRIM5α(rh) RING domain functions on restriction of retroviruses.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Virus-specific effects of TRIM ...... n restriction of retroviruses.
@en
type
label
Virus-specific effects of TRIM ...... n restriction of retroviruses.
@en
prefLabel
Virus-specific effects of TRIM ...... n restriction of retroviruses.
@en
P2093
P2860
P50
P356
P1433
P1476
Virus-specific effects of TRIM5α(rh) RING domain functions on restriction of retroviruses
@en
P2093
Byeongwoon Song
Jonghwa Kim
P2860
P304
P356
10.1128/JVI.00620-13
P407
P577
2013-05-01T00:00:00Z