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

Prediction and experimental characterization of nsSNPs altering human PDZ-binding motifs.

PloS one - 1 Jan 2014

Gfeller David, Ernst Andreas, Jarvik Nick, Sidhu Sachdev S, Bader Gary D

Abstract excerpt

Single nucleotide polymorphisms (SNPs) are a major contributor to genetic and phenotypic variation within populations. Non-synonymous SNPs (nsSNPs) modify the sequence of proteins and can affect their folding or binding properties. Experimental analysis of all nsSNPs is currently unfeasible and therefore computational predictions of the molecular effect of nsSNPs are helpful to guide experimental investigations....

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Databases, Genetic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genome, Human

Share to Models, Statistical

Share to PDZ Domains

Share to Protein Binding

Share to Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 24722214
DOI: 10.1371/journal.pone.0094507
PMCID: PMC3983204

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Prediction and experimental characterization of nsSNPs altering human PDZ-binding motifs.PMID 24722214Read ↗

Domain altering SNPs in the human proteome and their impact on signaling pathways.Semantic proximity Read ↗

Identification of Sequence Variants within Experimentally Validated Protein Interaction Sites Provides New Insights into Molecular Mechanisms of Disease Development.Semantic proximity Read ↗

In Silico Tools and Approaches for the Prediction of Functional and Structural Effects of Single-Nucleotide Polymorphisms on Proteins: An Expert Review.Semantic proximity Read ↗

Proteome-scale characterisation of motif-based interactome rewiring by disease mutationsSemantic proximity Read ↗

Proteome-scale characterisation of motif-based interactome rewiring by disease mutations.Semantic proximity Read ↗

The effects of non-synonymous single nucleotide polymorphisms (nsSNPs) on protein-protein interactions.Semantic proximity Read ↗

Distribution bias analysis of germline and somatic single-nucleotide variations that impact protein functional site and neighboring amino acids.Semantic proximity Read ↗

Approaches and resources for prediction of the effects of non-synonymous single nucleotide polymorphism on protein function and interactions.Semantic proximity Read ↗

High-throughput methods for identification of protein-protein interactions involving short linear motifsSemantic proximity Read ↗

Assessing variant effect predictors and disease mechanisms in intrinsically disordered proteinsSemantic proximity Read ↗

Pathogenic mutations of human phosphorylation sites affect protein-protein interactions.Semantic proximity Read ↗

Proteome-wide analysis of human disease mutations in short linear motifs: neglected players in cancer?Semantic proximity Read ↗

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