GENERIC 17721543

Download in:

Switch to

Custom View

Named Graph Language Inference

Statements in which the resource exists as a subject.
Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0086168, umls-concept:C0936012, umls-concept:C1623086
pubmed:issue	9
pubmed:dateCreated	2007-8-31
pubmed:abstractText	Peptide sequencing is the basis of mass spectrometry-driven proteomics. Here we show that in the linear ion trap-orbitrap mass spectrometer (LTQ Orbitrap) peptide ions can be efficiently fragmented by high-accuracy and full-mass-range tandem mass spectrometry (MS/MS) via higher-energy C-trap dissociation (HCD). Immonium ions generated via HCD pinpoint modifications such as phosphotyrosine with very high confidence. Additionally we show that an added octopole collision cell facilitates de novo sequencing.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101215604
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
pubmed:status	MEDLINE
pubmed:month	Sep
pubmed:issn	1548-7091
pubmed:author	pubmed-author:HorningStevanS, pubmed-author:LangeOliverO, pubmed-author:MacekBorisB, pubmed-author:MakarovAlexanderA, pubmed-author:MannMatthiasM, pubmed-author:OlsenJesper VJV
pubmed:issnType	Print
pubmed:volume	4
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	709-12
pubmed:meshHeading	pubmed-meshheading:17721543-Mass Spectrometry, pubmed-meshheading:17721543-Peptide Fragments, pubmed-meshheading:17721543-Protein Conformation, pubmed-meshheading:17721543-Proteomics, pubmed-meshheading:17721543-Tandem Mass Spectrometry
pubmed:year	2007
pubmed:articleTitle	Higher-energy C-trap dissociation for peptide modification analysis.
pubmed:affiliation	Department for Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Am Klopferspitz 18, D-82131 Martinsried, Germany.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't