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2001 1
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Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding.
Nollau P, Mayer BJ. Nollau P, et al. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13531-6. doi: 10.1073/pnas.241215998. Epub 2001 Nov 6. Proc Natl Acad Sci U S A. 2001. PMID: 11698653 Free PMC article.
We have developed a simple, rapid, and flexible competitive binding assay based on the far-Western blot technique, in which a battery of Src homology 2 domain probes is used to detect patterns of specific tyrosine-phosphorylated si …
We have developed a simple, rapid, and flexible competitive binding assay based on the far-Western blot technique, in which a battery …
Src homology 2 domain-based high throughput assays for profiling downstream molecules in receptor tyrosine kinase pathways.
Yaoi T, Chamnongpol S, Jiang X, Li X. Yaoi T, et al. Mol Cell Proteomics. 2006 May;5(5):959-68. doi: 10.1074/mcp.T600002-MCP200. Epub 2006 Feb 13. Mol Cell Proteomics. 2006. PMID: 16477079 Free article.
Src homology 2 (SH2) domains are evolutionary conserved small protein modules that bind specifically to tyrosine-phosphorylated peptides. ...Here we developed an SH2 domain profiling method based on a multiplexed fluo
Src homology 2 (SH2) domains are evolutionary conserved small protein modules that bind specifically to
Profiling the tyrosine phosphorylation state using SH2 domains.
Dierck K, Machida K, Mayer BJ, Nollau P. Dierck K, et al. Methods Mol Biol. 2009;527:131-55, ix. doi: 10.1007/978-1-60327-834-8_11. Methods Mol Biol. 2009. PMID: 19241011 Review.
Tyrosine phosphorylation of intracellular signaling proteins followed by the recognition and binding of Src homology 2 (SH2) domains are key mechanisms in the downstream transmission of many important biological signals. SH2 dom
Tyrosine phosphorylation of intracellular signaling proteins followed by the recognition and binding of Src h
SH2-PLA: a sensitive in-solution approach for quantification of modular domain binding by proximity ligation and real-time PCR.
Thompson CM, Bloom LR, Ogiue-Ikeda M, Machida K. Thompson CM, et al. BMC Biotechnol. 2015 Jun 26;15:60. doi: 10.1186/s12896-015-0169-1. BMC Biotechnol. 2015. PMID: 26112401 Free PMC article.
BACKGROUND: There is a great interest in studying phosphotyrosine dependent protein-protein interactions in tyrosine kinase pathways that play a critical role in many aspects of cellular function. We previously established SH2 profiling, a phosphoprote …
BACKGROUND: There is a great interest in studying phosphotyrosine dependent protein-protein interactions in tyrosine ki …
High-throughput phosphotyrosine profiling using SH2 domains.
Machida K, Thompson CM, Dierck K, Jablonowski K, Kärkkäinen S, Liu B, Zhang H, Nash PD, Newman DK, Nollau P, Pawson T, Renkema GH, Saksela K, Schiller MR, Shin DG, Mayer BJ. Machida K, et al. Mol Cell. 2007 Jun 22;26(6):899-915. doi: 10.1016/j.molcel.2007.05.031. Mol Cell. 2007. PMID: 17588523 Free article.
Protein tyrosine phosphorylation controls many aspects of signaling in multicellular organisms. One of the major consequences of tyrosine phosphorylation is the creation of binding sites for proteins containing Src homology
Protein tyrosine phosphorylation controls many aspects of signaling in multicellular organisms. One of the major conseq
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