Label-free relative quantification of co-eluting isobaric phosphopeptides of insulin receptor substrate-1 by HPLC-ESI-MS/MS.

Label-free relative quantification of co-eluting isobaric phosphopeptides of insulin receptor substrate-1 by HPLC-ESI-MS/MS.

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http://www.wikidata.org/entity/Q34369237
Adenine nucleotide translocase is acetylated in vivo in human muscle: Modeling predicts a decreased ADP affinity and altered control of oxidative phosphorylation.Separation of peptide isomers with variant modified sites by high-resolution differential ion mobility spectrometry.The identification of raptor as a substrate for p44/42 MAPKIncreased abundance of the adaptor protein containing pleckstrin homology domain, phosphotyrosine binding domain and leucine zipper motif (APPL1) in patients with obesity and type 2 diabetes: evidence for altered adiponectin signalling.Ultrasensitive identification of localization variants of modified peptides using ion mobility spectrometry.Ion mobility separation of isomeric phosphopeptides from a protein with variant modification of adjacent residues.Label-free quantitative phosphorylation analysis of human transgelin2 in Jurkat T cells reveals distinct phosphorylation patterns under PKA and PKC activation conditionsIon mobility separation of variant histone tails extending to the "middle-down" rangeSite-specific phosphorylation of protein phosphatase 1 regulatory subunit 12A stimulated or suppressed by insulinInsulin-stimulated phosphorylation of protein phosphatase 1 regulatory subunit 12B revealed by HPLC-ESI-MS/MSGlobal IRS-1 phosphorylation analysis in insulin resistance.An insight into iTRAQ: where do we stand now?Localization of Post-Translational Modifications in Peptide Mixtures via High-Resolution Differential Ion Mobility Separations Followed by Electron Transfer Dissociation.Identification of mechanically regulated phosphorylation sites on tuberin (TSC2) that control mechanistic target of rapamycin (mTOR) signaling.Metallothionein prevents diabetes-induced cardiac pathological changes, likely via the inhibition of succinyl-CoA:3-ketoacid coenzyme A transferase-1 nitration at Trp(374).A targeted proteomics approach to the quantitative analysis of ERK/Bcl-2-mediated anti-apoptosis and multi-drug resistance in breast cancer.
P2860

Label-free relative quantification of co-eluting isobaric phosphopeptides of insulin receptor substrate-1 by HPLC-ESI-MS/MS.

Item
http://www.wikidata.org/entity/Q34369237
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@ast
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@en
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@nl
type
label
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@ast
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@en
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@nl
prefLabel
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@ast
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@en
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@nl
P1433
P1476
P2093
P2860
P2888
P304
P31
P356
P433
P478
P577
P5875
P6179
P698
P921
P932
P356
P1433
P1476
Label-free relative quantifica ...... substrate-1 by HPLC-ESI-MS/MS.
@en
P2093
P2860
P2888
P304
P31
P356
10.1016/J.JASMS.2010.05.009
P433
P478
P577
P5875
P6179
P698
P921
P932