Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Aromatic residue mutations reveal direct correlation between HIV-1 nucleocapsid protein's nucleic acid chaperone activity and retroviral replication.

Virus research - 1 Feb 2013

Wu Hao, Mitra Mithun, McCauley Micah J, Thomas James A, Rouzina Ioulia, Musier-Forsyth Karin, Williams Mark C, Gorelick Robert J

Abstract excerpt

The human immunodeficiency virus type 1 (HIV-1) nucleocapsid (NC) protein plays an essential role in several stages of HIV-1 replication. One important function of HIV-1 NC is to act as a nucleic acid chaperone, in which the protein facilitates nucleic acid rearrangements important for reverse transcription and recombination. NC contains only 55 amino acids, with 15 basic residues and two zinc fingers, each...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to DNA, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to gag Gene Products, Human Immunodeficiency Virus

Share to HIV Infections

Share to Molecular Chaperones

Share to Nucleic Acid Conformation

Share to Reverse Transcription

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 22814429
DOI: 10.1016/j.virusres.2012.07.008
PMCID: PMC3745225

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Aromatic residue mutations reveal direct correlation between HIV-1 nucleocapsid protein's nucleic acid chaperone activity and retroviral replication.PMID 22814429Read ↗

Differential contribution of basic residues to HIV-1 nucleocapsid protein's nucleic acid chaperone function and retroviral replication.Semantic proximity Read ↗

Rapid kinetics of protein-nucleic acid interaction is a major component of HIV-1 nucleocapsid protein's nucleic acid chaperone function.Semantic proximity Read ↗

Single aromatic residue location alters nucleic acid binding and chaperone function of FIV nucleocapsid protein.Semantic proximity Read ↗

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

Complex interactions of HIV-1 nucleocapsid protein with oligonucleotides.Semantic proximity Read ↗

Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein.Semantic proximity Read ↗

HIV-1 nucleocapsid protein bends double-stranded nucleic acids.Semantic proximity Read ↗

Human cellular nucleic acid-binding protein Zn2+ fingers support replication of human immunodeficiency virus type 1 when they are substituted in the nucleocapsid protein.Semantic proximity Read ↗

Probing dynamics of HIV-1 nucleocapsid protein/target hexanucleotide complexes by 2-aminopurine.Semantic proximity Read ↗

Cationic Residues of the HIV-1 Nucleocapsid Protein Enable DNA Condensation to Maintain Viral Core Particle Stability during Reverse Transcription.Semantic proximity Read ↗

Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcriptionSemantic proximity Read ↗

Molecular determinants of HIV-1 NCp7 chaperone activity in maturation of the HIV-1 dimerization initiation site.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.