Selection of fully processed HIV-1 nucleocapsid protein is required for optimal nucleic acid chaperone activity in reverse transcription (Q34614167)

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English	Selection of fully processed HIV-1 nucleocapsid protein is required for optimal nucleic acid chaperone activity in reverse transcription	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

Selection of fully processed HIV-1 nucleocapsid protein is required for optimal nucleic acid chaperone activity in reverse transcription (English)

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

molecular chaperones

0 references

viral nucleocapsid

1 reference

based on heuristic

inferred from title

Robert J Gorelick

2

object named as

Robert J Gorelick

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

author name string

Tiyun Wu

1

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

Judith G Levin

3

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Europe PubMed Central

PubMed publication ID

3 August 2017

publication date

20 June 2014

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Europe PubMed Central

PubMed publication ID

3 August 2017

number of pages

13

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based on heuristic

inferred from page(s)

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Europe PubMed Central

PubMed publication ID

3 August 2017

193

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Europe PubMed Central

PubMed publication ID

3 August 2017

52-64

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC4252486/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Flexible Nature and Specific Functions of the HIV-1 Nucleocapsid Protein

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Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription

1 reference

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Features, processing states, and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function

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1 reference

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1 reference

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

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

1 reference

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APOBEC3G inhibits elongation of HIV-1 reverse transcripts

1 reference

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The structural biology of HIV assembly

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Nucleocapsid protein function in early infection processes

1 reference

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Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G.

1 reference

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HIV-1 protease and reverse transcriptase control the architecture of their nucleocapsid partner

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Human immunodeficiency virus type 1 assembly, release, and maturation.

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

1 reference

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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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1 reference

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Ordered aggregation of ribonucleic acids by the human immunodeficiency virus type 1 nucleocapsid protein.

1 reference

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1 reference

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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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Formation of immature and mature genomic RNA dimers in wild-type and protease-inactive HIV-1: Differential roles of the Gag polyprotein, nucleocapsid proteins NCp15, NCp9, NCp7, and the dimerization initiation site

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIRUSRES.2014.06.004

7 January 2021

Involvement of HIV-I nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIRUSRES.2014.06.004

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Transmission electron microscopy reveals an optimal HIV-1 nucleocapsid aggregation with single-stranded nucleic acids and the mature HIV-1 nucleocapsid protein

1 reference

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7 January 2021

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1 reference

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7 January 2021

Identifiers

10.1016/J.VIRUSRES.2014.06.004

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 August 2017

ResearchGate publication ID

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