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

Inferring protein-protein interactions in viral proteins by co-evolution of conserved side chains.

Genome informatics. International Conference on Genome Informatics - 1 Jan 2006

Wang Yaoyu E, DeLisi Charles

Abstract excerpt

We introduce a new and potentially valuable method for delineating the repertoire of protein complexes in highly mutable organisms and, in conjunction with other methods, for specifying the structural details of complexes. In the first instance the method provides a guide to selecting proteins for co-crystallization; in the second it augments the collection of structures determined by crystallography and other...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Conserved Sequence
Share to Evolution, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Reverse Transcriptase

Share to Protein Interaction Mapping

Share to Protein Subunits

Share to Viral Proteins

Source

Identifiers

PMID: 17503353

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inferring protein-protein interactions in viral proteins by co-evolution of conserved side chains.PMID 17503353Read ↗

Exposing the co-adaptive potential of protein-protein interfaces through computational sequence design.Semantic proximity Read ↗

Emerging methods in protein co-evolution.Semantic proximity Read ↗

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

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

Protein 3D structure computed from evolutionary sequence variation.Semantic proximity Read ↗

Correlated mutations and residue contacts in proteins.Semantic proximity Read ↗

Detection and reduction of evolutionary noise in correlated mutation analysis.Semantic proximity Read ↗

The human protein coevolution network.Semantic proximity Read ↗

Co-evolutionary analysis of domains in interacting proteins reveals insights into domain-domain interactions mediating protein-protein interactions.Semantic proximity Read ↗

Improving protein-protein interaction prediction using evolutionary information from low-quality MSAs.Semantic proximity Read ↗

Evolution of protein structures and interactions from the perspective of residue contact networks.Semantic proximity Read ↗

Individual human genomes frequently contain variants that have evolutionary couplingsSemantic proximity Read ↗

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