Articles with "ptyr" as a keyword



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High-throughput Phosphotyrosine Protein Complexes Screening by Photoaffinity-engineered Protein Scaffold-based Forward-phase Protein Array.

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Published in 2019 at "Analytical chemistry"

DOI: 10.1021/acs.analchem.9b01845

Abstract: Low abundance phosphotyrosine (pTyr)-mediated signaling protein complexes play critical roles in cancer signaling. The precise and comprehensive profiling of these pTyr-mediated protein complexes remains challenging due to their dynamic nature and weak binding affinity. Taking… read more here.

Keywords: protein; scaffold based; ptyr; based forward ... See more keywords
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High-Density, Targeted Monitoring of Tyrosine Phosphorylation Reveals Activated Signaling Networks in Human Tumors

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Published in 2021 at "Cancer Research"

DOI: 10.1158/0008-5472.can-20-3804

Abstract: SureQuant pTyr is a mass spectrometry–based targeted method that enables sensitive and selective targeted quantitation of several hundred low-abundance tyrosine phosphorylated peptides commonly dysregulated in cancer, including oncogenic signaling networks. Tyrosine phosphorylation (pTyr) plays a… read more here.

Keywords: tyrosine phosphorylation; ptyr; signaling networks; mass spectrometry ... See more keywords
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The relative binding position of Nck and Grb2 adaptors impacts actin-based motility of Vaccinia virus

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Published in 2022 at "eLife"

DOI: 10.7554/elife.74655

Abstract: Phosphotyrosine (pTyr) motifs in unstructured polypeptides orchestrate important cellular processes by engaging SH2-containing adaptors to assemble complex signalling networks. The concept of phase separation has recently changed our appreciation of multivalent networks, however, the role… read more here.

Keywords: nck grb2; based motility; ptyr; ptyr motifs ... See more keywords