Article

Constructing Functional Networks of Phosphorylation Sites Using Co-Phosphorylation

2021-08-16

Abstract excerpt

Protein phosphorylation is a ubiquitous regulatory mechanism that plays a central role in cellular signaling. According to recent estimates, up to 70% of human proteins can be phosphorylated. Therefore, characterization of phosphorylation dynamics is critical for understanding a broad range of biological and biochemical processes. Technologies based on mass spectrometry are rapidly advancing to meet the needs for...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 1b18c3e4-98ab-514a-b3ab-fe659a7694d3
DOI: 10.1101/2021.08.16.456448

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Constructing Functional Networks of Phosphorylation Sites Using Co-PhosphorylationDOI 10.1101/2021.08.16.456448Read

The functional landscape of the human phosphoproteomeSemantic proximity Read

CoPhosK: A Method for Comprehensive Kinase Substrate Annotation Using Co-phosphorylation AnalysisSemantic proximity Read

EPSD 2.0: An Updated Database of Protein Phosphorylation Sites across Eukaryotic SpeciesSemantic proximity Read

Computational analysis of phosphoproteomics: progresses and perspectives.Semantic proximity Read

A panoramic perspective on human phosphositesSemantic proximity Read

Spatially interacting phosphorylation sites and mutations in cancer.Semantic proximity Read

Spatially Interacting Phosphorylation Sites and Mutations in CancerSemantic proximity Read

Kinase Interaction Network Expands Functional and Disease Roles of Human KinasesSemantic proximity Read

PhosphoBlast, a computational tool for comparing phosphoprotein signatures among large datasets.Semantic proximity Read

Omic-Sig: Utilizing Omics Data to Explore and Visualize Kinase-Substrate InteractionsSemantic proximity Read

Scop3P in 2026: an expanded proteomics-informed resource contextualizing phosphorylation sites through sequence, structure, mutation, and experimental provenanceSemantic proximity Read

A global atlas of substrate specificities for the human serine/threonine kinomeSemantic proximity Read