Linked Life Data

10344244

Source:http://linkedlifedata.com/resource/pubmed/id/10344244

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10344244rdf:typepubmed:Citationlld:pubmed
pubmed-article:10344244lifeskim:mentionsumls-concept:C0020792lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0025663lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0002520lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0024337lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0025723lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0037813lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0023089lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0936012lld:lifeskim
pubmed-article:10344244lifeskim:mentionsumls-concept:C0392762lld:lifeskim
pubmed-article:10344244pubmed:issue4-5lld:pubmed
pubmed-article:10344244pubmed:dateCreated1999-7-29lld:pubmed
pubmed-article:10344244pubmed:abstractTextProtein methylation is a post-translational modification that might have important functional roles in cell regulation. We present a new technique with sufficient sensitivity (sub-pmol level) for analysis of methylation of proteins in abundances typically found on proteome maps produced by two-dimensional (2-D) gel electrophoresis. The method involves the identification and quantitation of lysine (Lys) methylation using Fmoc (9-fluorenylmethyl chloroformate)-based amino acid analysis (AAA). Tri- and monomethyl-Lys were baseline-separated from other amino acids using a modified buffer system. Trimethyl-Lys was quantitatively recovered after acid hydrolysis and AAA of two known methylated proteins - yeast cytochome c and human calmodulin. The methylated peptides from tryptic digestion of those two proteins were identified by high sensitivity matrix-assisted laser desorption/ionization - time-of-flight (MALDI-TOF) mass spectrometry (MS). An automated mass-screening approach is proposed for the study of various post-translational modifications to understand the distribution of those protein isoforms separated by two-dimensional polyacrylamide gel electrophoresis. It is concluded that the combination of AAA and MALDI-TOF-MS provides a high sensitivity quantitative tool for the analysis of protein post-translational methylation in the context of proteome studies.lld:pubmed
pubmed-article:10344244pubmed:languageenglld:pubmed
pubmed-article:10344244pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10344244pubmed:citationSubsetIMlld:pubmed
pubmed-article:10344244pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10344244pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10344244pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10344244pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10344244pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10344244pubmed:statusMEDLINElld:pubmed
pubmed-article:10344244pubmed:issn0173-0835lld:pubmed
pubmed-article:10344244pubmed:authorpubmed-author:WilliamsK LKLlld:pubmed
pubmed-article:10344244pubmed:authorpubmed-author:AyeU TUTlld:pubmed
pubmed-article:10344244pubmed:authorpubmed-author:HochstrasserD...lld:pubmed
pubmed-article:10344244pubmed:authorpubmed-author:SanchezJ CJClld:pubmed
pubmed-article:10344244pubmed:authorpubmed-author:BenzL ALAlld:pubmed
pubmed-article:10344244pubmed:issnTypePrintlld:pubmed
pubmed-article:10344244pubmed:volume20lld:pubmed
pubmed-article:10344244pubmed:ownerNLMlld:pubmed
pubmed-article:10344244pubmed:authorsCompleteYlld:pubmed
pubmed-article:10344244pubmed:pagination749-54lld:pubmed
pubmed-article:10344244pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:meshHeadingpubmed-meshheading:10344244...lld:pubmed
pubmed-article:10344244pubmed:articleTitleMethod for identification and quantitative analysis of protein lysine methylation using matrix-assisted laser desorption/ionization--time-of-flight mass spectrometry and amino acid analysis.lld:pubmed
pubmed-article:10344244pubmed:affiliationAustralian Proteome Analysis Facility, Macquarie University, Sydney, NSW. jun.yan@harefield.nthames.nhs.uklld:pubmed
pubmed-article:10344244pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10344244pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed