Novel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags

scientific article

Novel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1021/AC203248S
P932PMC publication ID3311540
P698PubMed publication ID22304650
P5875ResearchGate publication ID221805266

P50authorJulie A. LearyQ6307994
P2093author name stringArmann Andaya
Weitao Jia
P2860cites workQuantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosisQ24294864
Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometryQ24298332
Global, in vivo, and site-specific phosphorylation dynamics in signaling networksQ27864128
Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomicsQ28131742
Quantitative analysis of complex protein mixtures using isotope-coded affinity tagsQ28145324
mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation eventsQ28281590
Phosphorylation-Dephosphorylation of EnzymesQ28306047
Universal sample preparation method for proteome analysisQ29615662
Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signalingQ29617453
An oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3Q30438861
Dissection of proteolytic 18O labeling: endoprotease-catalyzed 16O-to-18O exchange of truncated peptide substrates.Q30919892
Quantitative Analysis of Protein Complex Constituents and Their Phosphorylation States on a LTQ-Orbitrap InstrumentQ30987532
Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometryQ31159025
N-Terminal peptide labeling strategy for incorporation of isotopic tags: a method for the determination of site-specific absolute phosphorylation stoichiometryQ33185434
Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometryQ33185788
iTRAQ reagent-based quantitative proteomic analysis on a linear ion trap mass spectrometerQ33300715
An efficient method for dephosphorylation of phosphopeptides by cerium oxideQ33310044
Stable isotope-free relative and absolute quantitation of protein phosphorylation stoichiometry by MSQ33926837
Tandem Mass Tags: A Novel Quantification Strategy for Comparative Analysis of Complex Protein Mixtures by MS/MSQ34192662
Distinct regions of human eIF3 are sufficient for binding to the HCV IRES and the 40S ribosomal subunitQ34284595
Systematic identification of mitotic phosphoproteinsQ34422813
eIF3j is located in the decoding center of the human 40S ribosomal subunitQ34641203
Relative quantification of proteins in human cerebrospinal fluids by MS/MS using 6-plex isobaric tagsQ34756963
Label-free quantitative proteomics reveals differentially regulated proteins influencing urolithiasisQ35144109
Different phosphorylation states of the anaphase promoting complex in response to antimitotic drugs: a quantitative proteomic analysis.Q36579320
Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometerQ36914493
Mapping protein post-translational modifications with mass spectrometryQ36954374
Global and site-specific quantitative phosphoproteomics: principles and applicationsQ37286195
Measurement of protein phosphorylation stoichiometry by selected reaction monitoring mass spectrometryQ38469062
A large-scale method to measure absolute protein phosphorylation stoichiometriesQ42847626
An improved purification procedure of alkaline phosphatase from calf intestine by applying partition in aqueous two-phase systems and dye-ligand chromatographyQ43516217
The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modificationsQ45275572
Multiple reaction monitoring of mTRAQ-labeled peptides enables absolute quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissuesQ46481136
Preparation of high purity alkaline phosphatase from calf intestine using dye-ligand chromatography.Q50762661
Quantitative profiling of serum samples using TMT protein labelling, fractionation and LC-MS/MS.Q53937060
High Precision Quantitative Proteomics Using iTRAQ on an LTQ Orbitrap: A New Mass Spectrometric Method Combining the Benefits of AllQ57184382
Functional and quantitative proteomics using SILACQ57369727
Quantitative in vitro kinase reaction as a guide for phosphoprotein analysis by mass spectrometryQ73504617
High-performance liquid chromatography/electrospray ionization ion-trap mass spectrometry for analysis of oligosaccharides derivatized by reductive amination and N,N-dimethylationQ80391118
P433issue5
P407language of work or nameEnglishQ1860
P921main subjectceriumQ1385
nanoparticleQ61231
phosphorylationQ242736
P304page(s)2466-2473
P577publication date2012-02-09
P1433published inAnalytical ChemistryQ485223
P1476titleNovel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags
P478volume84

Reverse relations

cites work (P2860)
Q88562596Heterogeneity and specialized functions of translation machinery: from genes to organisms
Q38881491Integrated Strategies to Gain a Systems-Level View of Dynamic Signaling Networks
Q46924675Kinetic control in the CID-induced elimination of H3PO4 from phosphorylated serine probed using IRMPD spectroscopy
Q34313411Lanthanum silicate coated magnetic microspheres as a promising affinity material for phosphopeptide enrichment and identification.
Q58631294Nanoparticles for Mass Spectrometry Applications
Q34072222Phosphorylation stoichiometries of human eukaryotic initiation factors
Q38245231Toward a systems-level view of dynamic phosphorylation networks
Q41886466Unblocking the sink: improved CID-based analysis of phosphorylated peptides by enzymatic removal of the basic C-terminal residue.

Search more.