Sensitive Approaches for the Assay of the Global Protein Tyrosine Phosphorylation in Complex Samples Using a Mutated SH2 Domain.
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Summary
This study developed sensitive and cost-effective methods for the assay of the global protein tyrosine phosphorylation in complex samples by using a novel engineered pTyr binding protein, Src SH2 domain triple-point mutant (Trm-SH2).
- Type
- article
- Published
- 2017-02-09
- Cited by
- 13
- References
- 32
- Access
- Open access
- OpenAlex
- https://openalex.org/W2581276725
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:39993630
Keywords
SH2 domain, Tyrosine phosphorylation, Phosphorylation, Tyrosine, Chemistry
References
- Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation
- Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins
- Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks
- Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors.
- Target profiling of small molecules by chemical proteomics.
- Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
- Novel Phosphorylation Assay Based on Multi-Functionalized Soluble Nanopolymer
- Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling.
- Characterizing Tyrosine Phosphorylation Signaling in Lung Cancer Using SH2 Profiling
- A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
- Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains
- Sensitive measurement of total protein phosphorylation level in complex protein samples
- An enriched look at tyrosine phosphorylation
- The SH2 Domain–Containing Proteins in 21 Species Establish the Provenance and Scope of Phosphotyrosine Signaling in Eukaryotes
- Signaling—2000 and Beyond
- Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal.
- Phosphotyrosine-binding domains in signal transduction
- Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding
- Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
- Superbinder SH2 Domains Act as Antagonists of Cell Signaling
Cited by
- Novel functionalized nanomaterials for the effective enrichment of proteins and peptides with post-translational modifications.
- High-throughput Phosphotyrosine Protein Complexes Screening by Photoaffinity-engineered Protein Scaffold-based Forward-phase Protein Array.
- A polymer monolith composed of a perovskite and cucurbit[6]uril hybrid for highly selective enrichment of phosphopeptides prior to mass spectrometric analysis
- Mass Spectrometry-Based Identification of Phospho-Tyr in Plant Proteomics.
- Functional Nanochannels for Sensing Tyrosine Phosphorylation.
- Molecularly Imprinted and Cladded Nanoparticles Provide Better Phosphorylation Recognition.
- Zinc-Air Battery-Assisted Self-Powered PEC Sensors for Sensitive Assay of PTP1B Activity Based on Perovskite Quantum Dots Encapsulated in Vinyl-Functionalized Covalent Organic Frameworks.
- Integrated and High-Throughput Approach for Sensitive Analysis of Tyrosine Phosphoproteome.
- Mass spectrometry analysis of phosphotyrosine-containing proteins.
- Pilot investigation of magnetic nanoparticle–based immobilized metal affinity chromatography for efficient enrichment of phosphoproteoforms for mass spectrometry–based top-down proteomics
- In situ digestion-assisted multi-template imprinted nanoparticles for efficient analysis of protein phosphorylation
- Facile fabrication of Ti4+-immobilized magnetic nanoparticles by phase-transitioned lysozyme nanofilms for enrichment of phosphopeptides
- R2HaPpY: Rapid-robust phosphotyrosine peptide enrichment using HaloTag-Src SH2 pY superbinder
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