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

Proteomic analysis and prediction of amino acid variations that influence protein posttranslational modifications.

Briefings in bioinformatics - 27 Sept 2019

Shi Shaoping, Wang Lina, Cao Man, Chen Guodong, Yu Jialin

Abstract excerpt

Accumulative studies have indicated that amino acid variations through changing the type of residues of the target sites or key flanking residues could directly or indirectly influence protein posttranslational modifications (PTMs) and bring about a detrimental effect on protein function. Computational mutation analysis can greatly narrow down the efforts on experimental work. To increase the utilization of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Amino Acids
Share to Computational Biology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Processing, Post-Translational

Share to Proteins

Share to Proteomics

Source

Identifiers

PMID: 29788276
DOI: 10.1093/bib/bby036

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

Proteomic analysis and prediction of amino acid variations that influence protein posttranslational modifications.PMID 29788276Read ↗

Loss of post-translational modification sites in disease.Semantic proximity Read ↗

Nonsynonymous Single-Nucleotide Variations on Some Posttranslational Modifications of Human Proteins and the Association with Diseases.Semantic proximity Read ↗

Computational approaches for identifying disease-causing mutations in proteins.Semantic proximity Read ↗

Impact of Nonsynonymous Single-Nucleotide Variations on Post-Translational Modification Sites in Human Proteins.Semantic proximity Read ↗

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

Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations.Semantic proximity Read ↗

AWESOME: a database of SNPs that affect protein post-translational modifications.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 ↗

Progress on the development of prediction tools for detecting disease causing mutations in proteins.Semantic proximity Read ↗

Analyzing effects of naturally occurring missense mutations.Semantic proximity Read ↗

Large differences in proportions of harmful and benign amino acid substitutions between proteins and diseases.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 ↗

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