The effect of mutations in the HIV-1 nucleocapsid protein on strand transfer in cell-free reverse transcription reactions
about
Ty5 gag mutations increase retrotransposition and suggest a role for hydrogen bonding in the function of the nucleocapsid zinc finger.Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transferUtilization of nonviral sequences for minus-strand DNA transfer and gene reconstitution during retroviral replication.Human immunodeficiency virus type 1 nucleocapsid zn(2+) fingers are required for efficient reverse transcription, initial integration processes, and protection of newly synthesized viral DNA.The N-terminal zinc finger and flanking basic domains represent the minimal region of the human immunodeficiency virus type-1 nucleocapsid protein for targeting chaperone function.The HIV-1 repeated sequence R as a robust hot-spot for copy-choice recombination.Two basic regions of NCp7 are sufficient for conformational conversion of HIV-1 dimerization initiation site from kissing-loop dimer to extended-duplex dimer.Differing roles of the N- and C-terminal zinc fingers in human immunodeficiency virus nucleocapsid protein-enhanced nucleic acid annealing.
P2860
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P2860
The effect of mutations in the HIV-1 nucleocapsid protein on strand transfer in cell-free reverse transcription reactions
description
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name
The effect of mutations in the ...... everse transcription reactions
@en
The effect of mutations in the ...... verse transcription reactions.
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type
label
The effect of mutations in the ...... everse transcription reactions
@en
The effect of mutations in the ...... verse transcription reactions.
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prefLabel
The effect of mutations in the ...... everse transcription reactions
@en
The effect of mutations in the ...... verse transcription reactions.
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P2093
P2860
P356
P1476
The effect of mutations in the ...... everse transcription reactions
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P2093
P2860
P304
P356
10.1093/NAR/28.8.1724
P407
P577
2000-04-01T00:00:00Z