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

BeAtMuSiC: Prediction of changes in protein-protein binding affinity on mutations.

Nucleic acids research - 1 Jul 2013

Dehouck Yves, Kwasigroch Jean Marc, Rooman Marianne, Gilis Dimitri

Abstract excerpt

The ability of proteins to establish highly selective interactions with a variety of (macro)molecular partners is a crucial prerequisite to the realization of their biological functions. The availability of computational tools to evaluate the impact of mutations on protein-protein binding can the...

Read the complete abstract on PubMed

Topics

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

Share to Internet
Share to Models, Molecular
Share to Multiprotein Complexes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Protein Folding

Share to Software

Source

Open in PubMed Open full text

Identifiers

PMID: 23723246
DOI: 10.1093/nar/gkt450
PMCID: PMC3692068

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23723246-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

BeAtMuSiC: Prediction of changes in protein-protein binding affinity on mutations.PMID 23723246Read ↗

ProAffiMuSeq: sequence-based method to predict the binding free energy change of protein-protein complexes upon mutation using functional classification.Semantic proximity Read ↗

SKEMPI 2.0: an updated benchmark of changes in protein-protein binding energy, kinetics and thermodynamics upon mutation.Semantic proximity Read ↗

UEP: an open-source and fast classifier for predicting the impact of mutations in protein-protein complexes.Semantic proximity Read ↗

SKEMPI 2.0: An updated benchmark of changes in protein-protein binding energy, kinetics and thermodynamics upon mutationSemantic proximity Read ↗

MechPPI: Binding Mechanism-based Machine-Learning tool for Predicting Protein-Protein Binding Affinity Changes Upon MutationsSemantic proximity Read ↗

SAAMBE-MEM: a sequence-based method for predicting binding free energy change upon mutation in membrane protein-protein complexes.Semantic proximity Read ↗

SAAMBE-3D: Predicting Effect of Mutations on Protein-Protein Interactions.Semantic proximity Read ↗

Applying physics-based scoring to calculate free energies of binding for single amino acid mutations in protein-protein complexes.Semantic proximity Read ↗

PremPLI: Predicting the Effects of Missense Mutations on Protein-Ligand InteractionsSemantic proximity Read ↗

Exploring the interplay between experimental methods and the performance of predictors of binding affinity change upon mutations in protein complexes.Semantic proximity Read ↗

DeepPPAPredMut: deep ensemble method for predicting the binding affinity change in protein-protein complexes upon mutation.Semantic proximity Read ↗

SSIPe: accurately estimating protein-protein binding affinity change upon mutations using evolutionary profiles in combination with an optimized physical energy function.Semantic proximity Read ↗

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