Recognition of the HIV capsid by the TRIM5α restriction factor is mediated by a subset of pre-existing conformations of the TRIM5α SPRY domain.
about
Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5α.Ring finger protein 39 genetic variants associate with HIV-1 plasma viral loads and its replication in cell culture.A putative SUMO interacting motif in the B30.2/SPRY domain of rhesus macaque TRIM5α important for NF-κB/AP-1 signaling and HIV-1 restrictionDynamic conformational changes in the rhesus TRIM5α dimer dictate the potency of HIV-1 restriction.The therapeutic landscape of HIV-1 via genome editingQuarterly intrinsic disorder digest (January-February-March, 2014).A general model for retroviral capsid pattern recognition by TRIM5 proteins.The three-fold axis of the HIV-1 capsid lattice is the species-specific binding interface for TRIM5α.
P2860
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P2860
Recognition of the HIV capsid by the TRIM5α restriction factor is mediated by a subset of pre-existing conformations of the TRIM5α SPRY domain.
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2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2014 թվականի փետրվարին հրատարակված գիտական հոդված
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年论文
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name
Recognition of the HIV capsid ...... ons of the TRIM5α SPRY domain.
@ast
Recognition of the HIV capsid ...... ons of the TRIM5α SPRY domain.
@en
type
label
Recognition of the HIV capsid ...... ons of the TRIM5α SPRY domain.
@ast
Recognition of the HIV capsid ...... ons of the TRIM5α SPRY domain.
@en
prefLabel
Recognition of the HIV capsid ...... ons of the TRIM5α SPRY domain.
@ast
Recognition of the HIV capsid ...... ons of the TRIM5α SPRY domain.
@en
P2860
P356
P1433
P1476
Recognition of the HIV capsid ...... ons of the TRIM5α SPRY domain.
@en
P2093
Dmitri N Ivanov
Dmytro B Kovalskyy
P2860
P304
P356
10.1021/BI4014962
P407
P577
2014-02-24T00:00:00Z