High-Throughput Characterization of Histidine Phosphorylation Sites Using UPAX and Tandem Mass Spectrometry.
Enrichment
Mass spectrometry
Phosphohistidine
Phosphoproteomics
Strong anion exchange
pHis
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2020
2020
Historique:
entrez:
11
11
2019
pubmed:
11
11
2019
medline:
30
12
2020
Statut:
ppublish
Résumé
Liquid chromatography (LC)-tandem mass spectrometry (MS/MS) is key for the characterization of phosphorylation sites in a high-throughput manner, and its application has proven essential to elucidate the phosphoproteome of many biological systems. Following proteolytic digestion of proteins extracted from tissues or cells, phosphopeptides are typically enriched by affinity chromatography using TiO
Identifiants
pubmed: 31707662
doi: 10.1007/978-1-4939-9884-5_15
doi:
Substances chimiques
Phosphopeptides
0
Histidine
4QD397987E
phosphohistidine
UKY8AGM174
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
225-235Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M012557/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R000182/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/H007113/1
Pays : United Kingdom