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

Platinum: a database of experimentally measured effects of mutations on structurally defined protein-ligand complexes.

Nucleic acids research - 1 Jan 2015

Pires Douglas E V, Blundell Tom L, Ascher David B

Abstract excerpt

Drug resistance is a major challenge for the treatment of many diseases and a significant concern throughout the drug development process. The ability to understand and predict the effects of mutations on protein-ligand affinities and their roles in the emergence of resistance would significantly...

Read the complete abstract on PubMed

Topics

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

Share to Databases, Protein
Share to Drug Design
Share to HIV/AIDS drug development and treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Internet

Share to Ligands

Share to Mutation

Share to Protein Binding

Share to Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 25324307
DOI: 10.1093/nar/gku966
PMCID: PMC4384026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25324307-2026-09-04.2. 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

Platinum: a database of experimentally measured effects of mutations on structurally defined protein-ligand complexes.PMID 25324307Read ↗

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

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

MdrDB: Mutation-induced drug resistance DataBaseSemantic proximity Read ↗

Systematic evaluation of computational tools to predict the effects of mutations on protein-ligand binding affinity in the absence of experimental structures.Semantic proximity Read ↗

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

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

PANDA: Predicting the change in proteins binding affinity upon mutations by finding a signal in primary structures.Semantic proximity Read ↗

Combating mutations in genetic disease and drug resistance: understanding molecular mechanisms to guide drug design.Semantic proximity Read ↗

Leveraging AI to Explore Structural Contexts of Post-Translational Modifications in Drug BindingSemantic proximity Read ↗

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

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

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