Matches in SemOpenAlex for { <https://semopenalex.org/work/W2015131346> ?p ?o ?g. }
Showing items 1 to 84 of
84
with 100 items per page.
- W2015131346 endingPage "156" @default.
- W2015131346 startingPage "146" @default.
- W2015131346 abstract "Many biological functions are regulated by tyrosine phosphorylation: cell proliferation, migration, differentiation, and tumorgenesis among them. Hence, aspects of cellular behavior may be illustrated by monitoring the global dynamics of cellular tyrosine phosphorylation in response to stimuli. In this review, we describe an approach that combines phosphoprotein/peptide enrichment with stable isotope labeling which can quantify unambiguously those changes in phosphorylation status that occur specifically in response to stimulation by growth factor, autocrines, drug treatment or cellular physiology. Current technologies for enrichment of phosphoproteins and peptides including phosphotyrosine or phosphospecific antibodies, SH2 domains, metal oxide and IMAC chemistries coupled to magnetic particles are discussed. Phosphopeptides from cultures supplemented with either light or heavy lysine and arginine appear in mass spectra as sequence-matched isotopomers, but are chemically identical and co-migrate in any other separation. Hence, the quantification of stimulated phosphorylation (dephosphorylation) at specific sites of a protein may be accomplished with MScoupled chromatographic separation by comparing the relative peak area response of sequence matched phosphopeptides arising from two (or more) cell states. Furthermore, we illustrate a crossover methodology that may be used to disentangle true protein binding partners from nonspecific interactions, which is a common problem in affinity enrichment endeavors. Keywords: SILAC, tyrosine phosphorylation, quantitation, mass spectrometry, IMAC, SH2 domain, anti-phosphotyrosine antibody" @default.
- W2015131346 created "2016-06-24" @default.
- W2015131346 creator A5004585029 @default.
- W2015131346 creator A5020071768 @default.
- W2015131346 creator A5036616302 @default.
- W2015131346 creator A5037798237 @default.
- W2015131346 date "2008-10-01" @default.
- W2015131346 modified "2023-10-16" @default.
- W2015131346 title "Quantitative Proteomics in the Study of Phosphotyrosine-Mediated Signal Transduction Pathway" @default.
- W2015131346 doi "https://doi.org/10.2174/157016408785909631" @default.
- W2015131346 hasPublicationYear "2008" @default.
- W2015131346 type Work @default.
- W2015131346 sameAs 2015131346 @default.
- W2015131346 citedByCount "2" @default.
- W2015131346 countsByYear W20151313462013 @default.
- W2015131346 countsByYear W20151313462020 @default.
- W2015131346 crossrefType "journal-article" @default.
- W2015131346 hasAuthorship W2015131346A5004585029 @default.
- W2015131346 hasAuthorship W2015131346A5020071768 @default.
- W2015131346 hasAuthorship W2015131346A5036616302 @default.
- W2015131346 hasAuthorship W2015131346A5037798237 @default.
- W2015131346 hasConcept C104317684 @default.
- W2015131346 hasConcept C11960822 @default.
- W2015131346 hasConcept C178666793 @default.
- W2015131346 hasConcept C181912034 @default.
- W2015131346 hasConcept C185592680 @default.
- W2015131346 hasConcept C197153747 @default.
- W2015131346 hasConcept C2776165026 @default.
- W2015131346 hasConcept C2777061661 @default.
- W2015131346 hasConcept C2777553839 @default.
- W2015131346 hasConcept C2779281246 @default.
- W2015131346 hasConcept C2779933727 @default.
- W2015131346 hasConcept C34905852 @default.
- W2015131346 hasConcept C46111723 @default.
- W2015131346 hasConcept C55493867 @default.
- W2015131346 hasConcept C62478195 @default.
- W2015131346 hasConcept C6675166 @default.
- W2015131346 hasConcept C80311884 @default.
- W2015131346 hasConcept C86803240 @default.
- W2015131346 hasConcept C87325107 @default.
- W2015131346 hasConcept C95444343 @default.
- W2015131346 hasConcept C97029542 @default.
- W2015131346 hasConceptScore W2015131346C104317684 @default.
- W2015131346 hasConceptScore W2015131346C11960822 @default.
- W2015131346 hasConceptScore W2015131346C178666793 @default.
- W2015131346 hasConceptScore W2015131346C181912034 @default.
- W2015131346 hasConceptScore W2015131346C185592680 @default.
- W2015131346 hasConceptScore W2015131346C197153747 @default.
- W2015131346 hasConceptScore W2015131346C2776165026 @default.
- W2015131346 hasConceptScore W2015131346C2777061661 @default.
- W2015131346 hasConceptScore W2015131346C2777553839 @default.
- W2015131346 hasConceptScore W2015131346C2779281246 @default.
- W2015131346 hasConceptScore W2015131346C2779933727 @default.
- W2015131346 hasConceptScore W2015131346C34905852 @default.
- W2015131346 hasConceptScore W2015131346C46111723 @default.
- W2015131346 hasConceptScore W2015131346C55493867 @default.
- W2015131346 hasConceptScore W2015131346C62478195 @default.
- W2015131346 hasConceptScore W2015131346C6675166 @default.
- W2015131346 hasConceptScore W2015131346C80311884 @default.
- W2015131346 hasConceptScore W2015131346C86803240 @default.
- W2015131346 hasConceptScore W2015131346C87325107 @default.
- W2015131346 hasConceptScore W2015131346C95444343 @default.
- W2015131346 hasConceptScore W2015131346C97029542 @default.
- W2015131346 hasIssue "3" @default.
- W2015131346 hasLocation W20151313461 @default.
- W2015131346 hasOpenAccess W2015131346 @default.
- W2015131346 hasPrimaryLocation W20151313461 @default.
- W2015131346 hasRelatedWork W1530487503 @default.
- W2015131346 hasRelatedWork W1579484156 @default.
- W2015131346 hasRelatedWork W2015131346 @default.
- W2015131346 hasRelatedWork W2130222062 @default.
- W2015131346 hasRelatedWork W2611522287 @default.
- W2015131346 hasRelatedWork W2762736481 @default.
- W2015131346 hasRelatedWork W2911789102 @default.
- W2015131346 hasRelatedWork W4214881459 @default.
- W2015131346 hasRelatedWork W4308446957 @default.
- W2015131346 hasRelatedWork W91423431 @default.
- W2015131346 hasVolume "5" @default.
- W2015131346 isParatext "false" @default.
- W2015131346 isRetracted "false" @default.
- W2015131346 magId "2015131346" @default.
- W2015131346 workType "article" @default.