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

Integrated analysis of residue coevolution and protein structures capture key protein sectors in HIV-1 proteins.

PloS one - 1 Jan 2015

Zhao Yuqi, Wang Yanjie, Gao Yuedong, Li Gonghua, Huang Jingfei

Abstract excerpt

HIV type 1 (HIV-1) is characterized by its rapid genetic evolution, leading to challenges in anti-HIV therapy. However, the sequence variations in HIV-1 proteins are not randomly distributed due to a combination of functional constraints and genetic drift. In this study, we examined patterns of sequence variability for evidence of linked sequence changes (termed as coevolution or covariation) in 15 HIV-1...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Computational Biology
Share to Drug Resistance, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitopes

Share to Evolution, Molecular

Share to Human Immunodeficiency Virus Proteins

Share to Molecular Dynamics Simulation

Source

Open in PubMed Open full text

Identifiers

PMID: 25671429
DOI: 10.1371/journal.pone.0117506
PMCID: PMC4324911

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

Integrated analysis of residue coevolution and protein structures capture key protein sectors in HIV-1 proteins.PMID 25671429Read ↗

Dissecting the dynamics of HIV-1 protein sequence diversity.Semantic proximity Read ↗

Patterns of amino acid conservation in human and animal immunodeficiency virusesSemantic proximity Read ↗

Co-evolution networks of HIV/HCV are modular with direct association to structure and function.Semantic proximity Read ↗

Coevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.Semantic proximity Read ↗

Extracting the phylogenetic dimension of coevolution reveals hidden functional signalSemantic proximity Read ↗

A Study of the Coevolutionary Patterns Operating within the env Gene of the HIV-1 Group M SubtypesSemantic proximity Read ↗

Inferring protein-protein interactions in viral proteins by co-evolution of conserved side chains.Semantic proximity Read ↗

Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes.Semantic proximity Read ↗

Identification of coevolving residues and coevolution potentials emphasizing structure, bond formation and catalytic coordination in protein evolution.Semantic proximity Read ↗

Conservation and coevolution determine evolvability of different classes of disordered residues in human intrinsically disordered proteins.Semantic proximity Read ↗

Amino-acid co-variation in HIV-1 Gag subtype C: HLA-mediated selection pressure and compensatory dynamics.Semantic proximity Read ↗

Co-evolution networks of HIV/HCV are modular with direct association to structure and functionSemantic proximity Read ↗

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