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

PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins

31 Oct 2014

Abstract excerpt

The post-translational regulation of proteins is mainly driven by two molecular events, their modification by several types of moieties and their interaction with other proteins. These two processes are interdependent and together are responsible for the function of the protein in a particular cell state. Several databases focus on the prediction and compilation of protein-protein interactions (PPIs) and no less...

Read the complete abstract on PubMed

Topics

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

Share to Bioinformatics and Genomic Networks
Share to Microbial Natural Products and Biosynthesis
Share to Viral Infectious Diseases and Gene Expression in Insects

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25361965
DOI: 10.1093/nar/gku1081

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PTMcode v2: a resource for functional associations of post-translational modifications within and between proteinsPMID 25361965Read ↗

Pyntheon: A Functional Analysis Framework for Protein Modifications and Mutations of 83 Model OrganismsSemantic proximity Read ↗

Prediction and discovery of protein-protein direct interactions and stable complexes based on gene co-expression and co-evolutionSemantic proximity Read ↗

Proteomic analysis and prediction of amino acid variations that influence protein posttranslational modifications.Semantic proximity Read ↗

Human proteins with target sites of multiple post-translational modification types are more prone to be involved in disease.Semantic proximity Read ↗

CPLM 4.0: an updated database with rich annotations for protein lysine modifications.Semantic proximity Read ↗

dbPTM: an information repository of protein post-translational modification.Semantic proximity Read ↗

Mechismo: predicting the mechanistic impact of mutations and modifications on molecular interactions.Semantic proximity Read ↗

dbPTM in 2019: exploring disease association and cross-talk of post-translational modificationsSemantic proximity Read ↗

Evolutionary, structural and functional features of cellular signalling networksSemantic proximity Read ↗

dbPTM 2025 update: comprehensive integration of PTMs and proteomic data for advanced insights into cancer researchSemantic proximity Read ↗

A global map of associations between types of protein posttranslational modifications and human genetic diseasesSemantic proximity Read ↗

Identification of Protein-Protein Interactions by Detecting Correlated Mutation at the Interface.Semantic proximity Read ↗

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