Fundamental differences between the nucleic acid chaperone activities of HIV-1 nucleocapsid protein and Gag or Gag-derived proteins: biological implications (Q34237075)

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English	Fundamental differences between the nucleic acid chaperone activities of HIV-1 nucleocapsid protein and Gag or Gag-derived proteins: biological implications	scientific article

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8 February 2020

Fundamental differences between the nucleic acid chaperone activities of HIV-1 nucleocapsid protein and Gag or Gag-derived proteins: biological implications (English)

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8 February 2020

molecular chaperones

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viral nucleocapsid

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based on heuristic

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Siddhartha A.K. Datta

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8 February 2020

Robert J Gorelick

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Robert J Gorelick

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8 February 2020

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Tiyun Wu

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8 February 2020

Mithun Mitra

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8 February 2020

Alan Rein

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8 February 2020

Judith G Levin

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23 July 2010

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8 February 2020

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8 February 2020

405

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8 February 2020

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8 February 2020

556-567

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8 February 2020

The capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation

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Coronavirus nucleocapsid protein facilitates template switching and is required for efficient transcription

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HIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity.

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A strongly transdominant mutation in the human immunodeficiency virus type 1 gag gene defines an Achilles heel in the virus life cycle

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Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) Annealing to viral RNA in human immunodeficiency virus type 1

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Divergent Bro1 domains share the capacity to bind human immunodeficiency virus type 1 nucleocapsid and to enhance virus-like particle production

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28 July 2018

The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL late domains to recruit the cellular machinery necessary for viral budding

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APOBEC3G inhibits elongation of HIV-1 reverse transcripts

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Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription

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RNA chaperones, RNA annealers and RNA helicases

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Strand transfer events during HIV-1 reverse transcription

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Nucleocapsid protein function in early infection processes

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Measuring the binding stoichiometry of HIV-1 Gag to very-low-density oligonucleotide surfaces using surface plasmon resonance spectroscopy.

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Effects of nucleic acid local structure and magnesium ions on minus-strand transfer mediated by the nucleic acid chaperone activity of HIV-1 nucleocapsid protein

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Interactions between HIV-1 Gag molecules in solution: an inositol phosphate-mediated switch

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Conformation of the HIV-1 Gag protein in solution.

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Interactions of HIV-1 Gag with assembly cofactors

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28 July 2018

Nucleic acid binding and chaperone properties of HIV-1 Gag and nucleocapsid proteins

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28 July 2018

Mutant murine leukemia virus Gag proteins lacking proline at the N-terminus of the capsid domain block infectivity in virions containing wild-type Gag.

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28 July 2018

Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism

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A HIV-1 minimal gag protein is superior to nucleocapsid at in vitro annealing and exhibits multimerization-induced inhibition of reverse transcription

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The chaperoning and assistance roles of the HIV-1 nucleocapsid protein in proviral DNA synthesis and maintenance

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Coupling of human immunodeficiency virus type 1 fusion to virion maturation: a novel role of the gp41 cytoplasmic tail

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Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein

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28 July 2018

Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells

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28 July 2018

Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the initiation step of reverse transcription in human immunodeficiency virus type 1.

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28 July 2018

Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer

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A conformational switch controlling HIV-1 morphogenesis

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Coupled integration of human immunodeficiency virus type 1 cDNA ends by purified integrase in vitro: stimulation by the viral nucleocapsid protein

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The role of Pr55(gag) in the annealing of tRNA3Lys to human immunodeficiency virus type 1 genomic RNA

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The human immunodeficiency virus type 1 Gag polyprotein has nucleic acid chaperone activity: possible role in dimerization of genomic RNA and placement of tRNA on the primer binding site

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In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain.

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Intra-tRNA distance measurements for nucleocapsid proteindependent tRNA unwinding during priming of HIV reverse transcription

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Structural biology of HIV.

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Roles of the human immunodeficiency virus type 1 nucleocapsid protein in annealing and initiation versus elongation in reverse transcription of viral negative-strand strong-stop DNA

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Compensatory point mutations in the human immunodeficiency virus type 1 Gag region that are distal from deletion mutations in the dimerization initiation site can restore viral replication

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Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly

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Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA.

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Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability

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Primer tRNA3Lys on the viral genome exists in unextended and two-base extended forms within mature human immunodeficiency virus type 1.

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Human immunodeficiency virus type 1 nucleocapsid protein reduces reverse transcriptase pausing at a secondary structure near the murine leukemia virus polypurine tract

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HIV-1 nucleocapsid protein induces "maturation" of dimeric retroviral RNA in vitro

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A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum

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DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein

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Human immunodeficiency virus type 1 virions composed of unprocessed Gag and Gag-Pol precursors are capable of reverse transcribing viral genomic RNA.

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Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1.

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Defects in primer-template binding, processive DNA synthesis, and RNase H activity associated with chimeric reverse transcriptases having the murine leukemia virus polymerase domain joined to Escherichia coli RNase H.

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First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses

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A new technique for the assay of infectivity of human adenovirus 5 DNA

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Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone

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Complete nucleotide sequence of the AIDS virus, HTLV-III

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Small finger protein of avian and murine retroviruses has nucleic acid annealing activity and positions the replication primer tRNA onto genomic RNA.

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Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete amino acid sequences

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Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain

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C-terminal domain modulates the nucleic acid chaperone activity of human T-cell leukemia virus type 1 nucleocapsid protein via an electrostatic mechanism

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Properties, functions, and drug targeting of the multifunctional nucleocapsid protein of the human immunodeficiency virus.

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Rapid kinetics of protein-nucleic acid interaction is a major component of HIV-1 nucleocapsid protein's nucleic acid chaperone function

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Human immunodeficiency virus type 1 nucleocapsid zinc-finger mutations cause defects in reverse transcription and integration

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28 October 2018

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The tRNALys packaging complex in HIV-1

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HIV-1 nucleocapsid protein zinc finger structures induce tRNA(Lys,3) structural changes but are not critical for primer/template annealing

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Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein

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28 October 2018

Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1.

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28 October 2018

Heteronuclear NMR studies of the interaction of tRNA3Lys with HIV-1 nucleocapsid protein11Edited by M. F. Summers

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Structural determinants of HIV-1 nucleocapsid protein for cTAR DNA binding and destabilization, and correlation with inhibition of self-primed DNA synthesis

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7 January 2021

Alteration of nucleic acid structure and stability modulates the efficiency of minus-strand transfer mediated by the HIV-1 nucleocapsid protein

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7 January 2021

NCp7 activates HIV-1Lai RNA dimerization by converting a transient loop-loop complex into a stable dimer

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7 January 2021

Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication

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7 January 2021

Molecular recognition in the HIV-1 capsid/cyclophilin A complex

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7 January 2021

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10.1016/J.VIROL.2010.06.042

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20655566%20AND%20SRC:MED&resulttype=core&format=json

8 February 2020

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