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

Investigation of N-terminal domain charged residues on the assembly and stability of HIV-1 CA.

Biochemistry - 17 Aug 2004

Douglas Chanel C, Thomas Dennis, Lanman Jason, Prevelige Peter E

Abstract excerpt

The human immunodeficiency virus type 1 (HIV-1) capsid protein (CA) plays a crucial role in both assembly and maturation of the virion as well as viral infectivity. Previous in vivo experiments generated two N-terminal domain charge change mutants (E45A and E128A/R132A) that showed an increase in stability of the viral core. This increase in core stability resulted in decreased infectivity, suggesting the need...

Read the complete abstract on PubMed

Topics

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

Share to Capsid Proteins
Share to Dimerization
Share to HIV-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Protein Structure, Tertiary

Share to Protein Subunits

Share to Static Electricity

Share to Virus Assembly

Source

Identifiers

PMID: 15301542
DOI: 10.1021/bi049359g

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

Investigation of N-terminal domain charged residues on the assembly and stability of HIV-1 CA.PMID 15301542Read ↗

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.Semantic proximity Read ↗

Formation of a Human Immunodeficiency Virus Type 1 Core of Optimal Stability Is Crucial for Viral ReplicationSemantic proximity Read ↗

A retroviral chimeric capsid protein reveals the role of the N-terminal β-hairpin in mature core assembly.Semantic proximity Read ↗

Determinants of the HIV-1 core assembly pathway.Semantic proximity Read ↗

Assembly properties of the human immunodeficiency virus type 1 CA protein.Semantic proximity Read ↗

Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptase.Semantic proximity Read ↗

Virological characterization of HIV-1 CA-NTD mutants constructed in a virus-lineage reflected manner.Semantic proximity Read ↗

Functional domains of the capsid protein of human immunodeficiency virus type 1Semantic proximity Read ↗

Electrostatic repulsion between HIV-1 capsid proteins modulates hexamer plasticity and in vitro assembly.Semantic proximity Read ↗

Flexibility in HIV-1 assembly subunits: solution structure of the monomeric C-terminal domain of the capsid protein.Semantic proximity Read ↗

Critical Role of the Human T-Cell Leukemia Virus Type 1 Capsid N-Terminal Domain for Gag-Gag Interactions and Virus Particle Assembly.Semantic proximity Read ↗

Mutation of dileucine-like motifs in the human immunodeficiency virus type 1 capsid disrupts virus assembly, gag-gag interactions, gag-membrane binding, and virion maturation.Semantic proximity Read ↗

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