scholarly article | Q13442814 |
P356 | DOI | 10.1002/PMIC.201500453 |
P698 | PubMed publication ID | 27219855 |
P50 | author | Albert J.R. Heck | Q2865808 |
Maarten Altelaar | Q42757801 | ||
Erik L de Graaf | Q56515712 | ||
Thierry Schmidlin | Q67226701 | ||
Harm Post | Q114290773 | ||
Luc B Garrigues | Q114290790 | ||
P2093 | author name string | Simone Lemeer | |
Catherine S Lane | |||
Sander van Doorn | |||
T Celine Mulder | |||
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Phosphorylation of Raptor by p38beta participates in arsenite-induced mammalian target of rapamycin complex 1 (mTORC1) activation | Q35213239 | ||
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Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks | Q35749545 | ||
Protein significance analysis in selected reaction monitoring (SRM) measurements | Q35878777 | ||
Targeted proteomic quantification on quadrupole-orbitrap mass spectrometer. | Q36455720 | ||
Quantitative phosphoproteomic analysis of signaling network dynamics. | Q36936477 | ||
Site-specific mTOR phosphorylation promotes mTORC1-mediated signaling and cell growth. | Q37275196 | ||
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Signal Transduction Reaction Monitoring Deciphers Site-Specific PI3K-mTOR/MAPK Pathway Dynamics in Oncogene-Induced Senescence. | Q38870887 | ||
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Single-step enrichment by Ti4+-IMAC and label-free quantitation enables in-depth monitoring of phosphorylation dynamics with high reproducibility and temporal resolution. | Q42229898 | ||
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OpenSWATH enables automated, targeted analysis of data-independent acquisition MS data | Q48317444 | ||
Disruption of the 14-3-3 binding site within the B-Raf kinase domain uncouples catalytic activity from PC12 cell differentiation | Q48899475 | ||
Quantitation of 47 human tear proteins using high resolution multiple reaction monitoring (HR-MRM) based-mass spectrometry. | Q51067809 | ||
Multiple Reaction Monitoring to Identify Sites of Protein Phosphorylation with High Sensitivity | Q57011006 | ||
Use of Fast HPLC Multiple Reaction Monitoring Cubed for Endogenous Retinoic Acid Quantification in Complex Matrices | Q57704484 | ||
P433 | issue | 15-16 | |
P921 | main subject | phosphorylation | Q242736 |
P304 | page(s) | 2193-2205 | |
P577 | publication date | 2016-06-27 | |
P1433 | published in | Proteomics | Q15614164 |
P1476 | title | Assessment of SRM, MRM(3) , and DIA for the targeted analysis of phosphorylation dynamics in non-small cell lung cancer | |
P478 | volume | 16 |
Q49922966 | Application of targeted mass spectrometry in bottom-up proteomics for systems biology research. |
Q91960893 | Breast Cancer Classification Based on Proteotypes Obtained by SWATH Mass Spectrometry |
Q36354836 | Clinical applications of quantitative proteomics using targeted and untargeted data-independent acquisition techniques |
Q51267763 | Comparison of targeted proteomics approaches for detecting and quantifying proteins derived from human cancer tissues. |
Q58787412 | Data-independent acquisition-based SWATH-MS for quantitative proteomics: a tutorial |
Q90108769 | High-Throughput Assessment of Kinome-wide Activation States |
Q57842120 | Joining forces: studying multiple post-translational modifications to understand dynamic disease mechanisms |
Q63407254 | Phosphopeptide Fragmentation and Site Localization by Mass Spectrometry: An Update |
Q41540355 | Quantitative Phosphoproteomic Analysis Reveals Key Mechanisms of Cellular Proliferation in Liver Cancer Cells |
Q33796358 | Quantitative proteomics in lung cancer |
Q36262132 | SWATH-MS as a tool for biomarker discovery - from basic research to clinical applications |
Q64066950 | The whole transcriptome and proteome changes in the early stage of myocardial infarction |
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