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 stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.

PLoS computational biology - 1 Apr 2009

Bloom Jesse D, Glassman Matthew J

Abstract excerpt

One selection pressure shaping sequence evolution is the requirement that a protein fold with sufficient stability to perform its biological functions. We present a conceptual framework that explains how this requirement causes the probability that a particular amino acid mutation is fixed during evolution to depend on its effect on protein stability. We mathematically formalize this framework to develop a...

Read the complete abstract on PubMed

Topics

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

Share to Evolution, Molecular
Share to Amino Acid Sequence
Share to Biological Evolution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Mutational Analysis

Share to Genomic Instability

Share to Hemagglutinin Glycoproteins, Influenza Virus

Share to Phylogeny

Share to Sequence Analysis, Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 19381264
DOI: 10.1371/journal.pcbi.1000349
PMCID: PMC2664478

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

Inferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.PMID 19381264Read ↗

Stability of the Influenza Virus Hemagglutinin Protein Correlates with Evolutionary DynamicsSemantic proximity Read ↗

Mutational effects on stability are largely conserved during protein evolution.Semantic proximity Read ↗

Combining molecular dynamics with bayesian analysis to predict and evaluate ligand-binding mutations in influenza hemagglutinin.Semantic proximity Read ↗

Mutation trend of hemagglutinin of influenza A virus: a review from a computational mutation viewpoint.Semantic proximity Read ↗

Stability effects of mutations and protein evolvability.Semantic proximity Read ↗

Detection of positive selection eliminating effects of structural constraints in hemagglutinin of H3N2 human influenza A virus.Semantic proximity Read ↗

The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin.Semantic proximity Read ↗

The stability effects of protein mutations appear to be universally distributed.Semantic proximity Read ↗

Deep mutational scanning of hemagglutinin helps predict evolutionary fates of human H3N2 influenza variantsSemantic proximity Read ↗

Improved Prediction of Stabilizing Mutations in Proteins by Incorporation of Mutational Effects on Ligand Binding.Semantic proximity Read ↗

Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.Semantic proximity Read ↗

Deep mutational scanning of hemagglutinin helps predict evolutionary fates of human H3N2 influenza variants.Semantic proximity Read ↗

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