Mechanism for nucleic acid chaperone activity of HIV-1 nucleocapsid protein revealed by single molecule stretching.
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Complex interactions of HIV-1 nucleocapsid protein with oligonucleotidesStructural determinants and mechanism of HIV-1 genome packagingUnfolding of DNA quadruplexes induced by HIV-1 nucleocapsid protein.Nucleic acid binding and chaperone properties of HIV-1 Gag and nucleocapsid proteinsStructural insights into the cTAR DNA recognition by the HIV-1 nucleocapsid protein: role of sugar deoxyriboses in the binding polarity of NCA single zinc finger optimizes the DNA interactions of the nucleocapsid protein of the yeast retrotransposon Ty3.Resource Letter: LBOT-1: Laser-based optical tweezersStretched DNA investigated using molecular-dynamics and quantum-mechanical calculations.C-terminal domain modulates the nucleic acid chaperone activity of human T-cell leukemia virus type 1 nucleocapsid protein via an electrostatic mechanism.Mechanism analysis indicates that recombination events in HIV-1 initiate and complete over short distances, explaining why recombination frequencies are similar in different sections of the genomeDynamics of linker residues modulate the nucleic acid binding properties of the HIV-1 nucleocapsid protein zinc fingersSpecific zinc-finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function.Biophysical characterization of DNA binding from single molecule force measurementsSecondary structure and secondary structure dynamics of DNA hairpins complexed with HIV-1 NC proteinStructural and functional properties of the HIV-1 RNA-tRNA(Lys)3 primer complex annealed by the nucleocapsid protein: comparison with the heat-annealed complexSingle aromatic residue location alters nucleic acid binding and chaperone function of FIV nucleocapsid protein.The Interaction between tRNA(Lys) 3 and the primer activation signal deciphered by NMR spectroscopy.Nucleic acid chaperone activity of retroviral Gag proteinsSingle-molecule stretching studies of RNA chaperones.Features, processing states, and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function.Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription.Oxaliplatin and its enantiomer induce different condensation dynamics of single DNA moleculesSubtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid proteinPaired mutations abolish and restore the balanced annealing and melting activities of ORF1p that are required for LINE-1 retrotransposition.Single DNA molecule stretching measures the activity of chemicals that target the HIV-1 nucleocapsid protein.Topological rearrangement yields structural stabilization and interhelical distance constraints in the Kin.46 self-phosphorylating ribozyme.Zinc finger-dependent HIV-1 nucleocapsid protein-TAR RNA interactions.Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-mediated dimerization and isomerization of HIV-1 stemloop 1.Nucleocapsid protein-mediated maturation of dimer initiation complex of full-length SL1 stemloop of HIV-1: sequence effects and mechanism of RNA refoldingMolecular mechanism of the Zn2+-induced folding of the distal CCHC finger motif of the HIV-1 nucleocapsid proteinEffects of nucleic acid local structure and magnesium ions on minus-strand transfer mediated by the nucleic acid chaperone activity of HIV-1 nucleocapsid protein.Probing nucleation, reverse annealing, and chaperone function along the reaction path of HIV-1 single-strand transferG-quartets direct assembly of HIV-1 nucleocapsid protein along single-stranded DNA.Single-molecule spectroscopic study of dynamic nanoscale DNA bending behavior of HIV-1 nucleocapsid protein.Zinc finger function of HIV-1 nucleocapsid protein is required for removal of 5'-terminal genomic RNA fragments: a paradigm for RNA removal reactions in HIV-1 reverse transcription.Site-selective probing of cTAR destabilization highlights the necessary plasticity of the HIV-1 nucleocapsid protein to chaperone the first strand transfer.Retroviral nucleocapsid proteins display nonequivalent levels of nucleic acid chaperone activity.A single amino acid substitution in ORF1 dramatically decreases L1 retrotransposition and provides insight into nucleic acid chaperone activity.Aromatic residue mutations reveal direct correlation between HIV-1 nucleocapsid protein's nucleic acid chaperone activity and retroviral replicationOptical tweezers for single cells
P2860
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P2860
Mechanism for nucleic acid chaperone activity of HIV-1 nucleocapsid protein revealed by single molecule stretching.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Mechanism for nucleic acid cha ...... by single molecule stretching.
@ast
Mechanism for nucleic acid cha ...... by single molecule stretching.
@en
type
label
Mechanism for nucleic acid cha ...... by single molecule stretching.
@ast
Mechanism for nucleic acid cha ...... by single molecule stretching.
@en
prefLabel
Mechanism for nucleic acid cha ...... by single molecule stretching.
@ast
Mechanism for nucleic acid cha ...... by single molecule stretching.
@en
P2093
P2860
P356
P1476
Mechanism for nucleic acid cha ...... by single molecule stretching
@en
P2093
J R Wenner
K Musier-Forsyth
R J Gorelick
V A Bloomfield
P2860
P304
P356
10.1073/PNAS.101033198
P407
P577
2001-05-08T00:00:00Z