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ProteomicsA sensitive and cost-effective approach for tyrosine phosphoproteome analysis based on SH2 superbinder
Albeit much less abundant than Ser/Thr phosphorylation (pSer/pThr), Tyr phosphorylation (pTyr) is considered a hallmark in cellular signal transduction. However, its analysis remains a challenge. The conventional immunopurification (IP) approach using antibodies pan-specific to pTyr sites is known t...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2017-08-29 | PXD005838 | Pride
Lc ms/ms Sh2 superbinder Ptyr phosphoproteome 
UnknownBlockade of phosphotyrosine pathways suggesting SH2 superbinder as a novel therapy for pulmonary fibrosis.
Not available
S-EPMC9254236 | biostudies-literature
Unknown(Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling.
Not available
S-EPMC6034221 | biostudies-literature
UnknownAptamer-SH2 superbinder-based targeted therapy for pancreatic ductal adenocarcinoma.
Not available
S-EPMC7908048 | biostudies-literature
ProteomicsScalable Phosphotyrosine Enrichment with SH2 Superbinder Enables Deep Profiling of EGF Responses
Phosphotyrosine signaling plays a critical role in many biological processes, from cell proliferation to immune response. Despite its importance, proteomic studies of tyrosine phosphorylation have been limited in scale and throughput by costly reagents and labor-intensive protocols. To address this,...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae Saccharomyces cerevisiae (Baker's yeast) 
2026-07-03 | PXD062515 | Pride
Phosphotyrosine Automated Hela Enrichment High-throughput Egf Lc-ms/ms 
ProteomicsPatient-derived KEAP1 superbinder mutants stabilize KEAP1 structure and sequester NRF2 in p62-dependent clusters
Cancer-derived loss-of-function mutations in the KEAP1 tumor suppressor gene stabilize the NRF2 transcription factor, resulting in a pro-survival gene expression program that alters cellular metabolism and neutralizes oxidative stress. In a previous study of KEAP1 mutations observed in lung cancer, ...
ORGANISM(S): Homo sapiens (Human) 
2018-11-07 | PXD008411 | Pride
Nrf2 Keap1 Superbinders P62 Clusters Mutations Lung cancer 
UnknownSuperbinder based phosphoproteomic landscape revealed PRKCD_pY313 mediates the activation of Src and p38 MAPK to promote TNBC progression.
Not available
S-EPMC10860301 | biostudies-literature
ProteomicsEngineering human SH2 domains for targeted phospho-proteomics
A comprehensive analysis of the phosphoproteome is essential for understanding molecular mechanisms of human diseases. However, current tools to enrich phosphotyrosine are limited in their applicability and scope. Here, we engineered new superbinder SH2 domains that enrich diverse sets of phosphotyr...
ORGANISM(S): Homo sapiens (Human) 
2023-01-13 | PXD030038 | Pride
Phosphoproteomics Synthetic biology K562 Src homology 2 domains Sh2 superbinders Mass spectrometry Human Structural biology Protein engineering Phosphotyrosine 
ProteomicsUltra-deep tyrosine phosphoproteome analysis enabled by an SH2 domain-derived phosphotyrosine superbinder
We present a new strategy for systematic identification of phosphotyrosine (pTyr) by AP-MS using an SH2 domain-derived pTyr-superbinder as the affinity reagent. The superbinder allows for markedly deeper and broader coverage of the Tyr phosphoproteome than conventional anti-phosphotyrosine antibodie...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-02-03 | MSV000079489 | MassIVE
ProteomicsOne-step SH2 superbinder based approach for sensitive analysis of tyrosine phosphoproteome
Tyrosine phosphorylation plays a major role in regulating cell signaling pathways governing diverse biological functions such as proliferation and differentiation. Systemically mapping phosphotyrosine (pTyr) sites is the key to understand molecular mechanisms underlining pTyr-dependent signaling. Al...
ORGANISM(S): Homo Sapiens (human) 
2020-03-07 | PXD012268 | JPOST Repository
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