ArticleNature methods2012
FLEXIQinase, a mass spectrometry-based assay, to unveil multikinase mechanisms.
Article in Nature methods, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
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- Identification of the phosphorylation targets of symbiotic receptor-like kinases using a high-throughput multiplexed assay for kinase specificity.The Plant journal : for cell and molecular biology · 2017Article
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- JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships.Microbiology and molecular biology reviews : MMBR · 2016Review
- Sortilin mediates vascular calcification via its recruitment into extracellular vesicles.The Journal of clinical investigation · 2016Article
- Oligomer formation of tau protein hyperphosphorylated in cells.The Journal of biological chemistry · 2014Article
- Co-regulation proteomics reveals substrates and mechanisms of APC/C-dependent degradation.The EMBO journal · 2014Article
- NANOG is multiply phosphorylated and directly modified by ERK2 and CDK1 in vitro.Stem cell reports · 2014Article
- Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.Nature protocols · 2013Article
- Quantitative dynamics of phosphoproteome: the devil is in the details.Analytical chemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
We introduce a mass spectrometry-based method that provides residue-resolved quantitative information about protein phosphorylation. In this assay we combined our full-length expressed stable isotope-labeled protein for quantification strategy (FLEXIQuant) with a traditional kinase assay to determine the mechanisms of multikinase substrate phosphorylation such as priming-dependent kinase activities. The assay monitors the decrease in signal intensity of the substrate peptides and the concomitant increase in the (n × 80 Da)-shifted phosphorylated peptide. We analyzed the c-Jun N-terminal kinase (JNK)-dependent glycogen synthase kinase 3β (GSK3β) activity on doublecortin (DCX) revealing mechanistic details about the role of phosphorylation cross-talk in GSK3β activity and permitting an advanced model for GSK3β-mediated signaling.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.