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ProteomicsIdentification of ABL Kinase Substrates by Kinase Assay Linked Phosphoproteomics and Multiple Drug Treatments
The kinase assay linked phosphoproteomics (KALIP) strategy was used to identify direct substrates of the Abelson tyrosine kinase (ABL). First, kinase assays using peptides and proteins from chronic myelogenous leukemia cells and recombinant ABL were done to identify kinase substrates in vitro. The A...
ORGANISM(S): Homo Sapiens (human) 
2019-03-20 | PXD005431 | JPOST Repository
ProteomicsHigh-throughput identification of FLT3 wild-type and mutant kinase substrate preferences and application to design of sensitive in vitro kinase assay substrates
Abnormalities in the FLT3 signaling pathway play an integral role in AML disease relapse and drug resistance. Developing new and specific FLT3 tyrosine kinase inhibitors for use in combination to induction therapy is an important step to reduce disease relapse and achieve clinical remission. To deve...
ORGANISM(S): Homo sapiens (Human) 
2019-01-07 | PXD011478 | Pride
Kinase assay linked with phosphoproteomics Flt3 Acute myeloid leukemia Mass spectrometry Phosphoproteomics 
ProteomicsIdentification of ERK1 direct substrates using stable isotope labeled kinase assay linked phosphoproteomics
Following the kinase assay linked phosphoproteomics strategy (KALIP) (Xue, L et al., 2012), we used extracellular signal-regulated kinases 1 (ERK1) to phosphorylate the HEK293 cell lysate under the in vitro kinase assay condition. The phosphorylated proteins were then isolated and identified by mass...
ORGANISM(S): Homo sapiens (Human) 
2014-07-17 | PXD000357 | Pride
Erk1 Phosphoproteomics Kinase substrates 
UnknownIdentification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomics.
Not available
S-EPMC3790304 | biostudies-literature
UnknownIdentification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics.
Not available
S-EPMC4223502 | biostudies-literature
ProteomicsMolecular Basis of the mechanisms controlling MASTL - Proteomics analysis of MASTL substrate proteome and phosphorylation state
As part of our study on human MASTL (microtubule-associated serine/threonine kinase-like), we used mass spectrometry (MS)-based proteomics in the aim to unravel novel aspects about MASTL activation, regulation and potential substrates. Specifically, we performed a phosphoproteomics-based kinase assa...
ORGANISM(S): Homo sapiens (Human) 
2020-01-09 | PXD007991 | Pride
Human Lc-msms Mastl 
ProteomicsMaximizing Confidence and Sensitivity in quantitative Phosphoproteomics - Targets of Mec1 kinase
Proteome-wide analysis of phosphorylation events is a challenging, yet essential, task for the comprehensive and unbiased investigation of kinase action. Here we developed a phosphoproteomic approach in which quantitation consistency among reversed isotopically labeled samples is used as a central f...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2020-01-30 | MSV000084875 | MassIVE
ProteomicsMaximizing Confidence and Sensitivity in quantitative Phosphoproteomics - Targets of Tel1 kinase
Proteome-wide analysis of phosphorylation events is a challenging, yet essential, task for the comprehensive and unbiased investigation of kinase action. Here we developed a phosphoproteomic approach in which quantitation consistency among reversed isotopically labeled samples is used as a central f...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2020-01-30 | MSV000084871 | MassIVE
ProteomicsPhosphoproteomics analysis identifies novel candidate substrates of the non-receptor tyrosine kinase, SRMS
SRMS (Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites) or PTK 70 (Protein tyrosine kinase 70) is a non-receptor tyrosine kinase that belongs to the BRK family kinases (BFKs). The gene encoding SRMS was first discovered in 1994. Yet to date less is known ...
ORGANISM(S): Homo sapiens (Human) 
2018-03-08 | PXD006809 | Pride
Frk Srms Substrates Brk Mass spectrometry Ptk6 Src Phosphoproteomics Ptk 70 
UnknownHigh-throughput Identification of FLT3 Wild-type and Mutant Kinase Substrate Preferences and Application to Design of Sensitive In Vitro Kinase Assay Substrates.
Not available
S-EPMC6398213 | biostudies-literature
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