ArticleChembiochem : a European journal of chemical biology2014
Evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Phosphonopeptides containing free phosphonic groups: recent advances.RSC advances · 2020Review
- Synthesis and In Vitro Cytotoxicity and Antibacterial Activity of Novel 1,2,3-Triazol-5-yl-phosphonates.Molecules (Basel, Switzerland) · 2020Article
- Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation.The EMBO journal · 2019Article
- Advances in development of new tools for the study of phosphohistidine.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- pHisphorylation: the emergence of histidine phosphorylation as a reversible regulatory modification.Current opinion in cell biology · 2017Review
- Advances in Fmoc solid-phase peptide synthesis.Journal of peptide science : an official publication of the European Peptide Society · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
We have investigated the interaction of peptides containing phosphohistidine analogues and their homologues with the prototypical phosphotyrosine binding SH2 domain from the eukaryotic cell signalling protein Grb2 by using a combination of isothermal titration calorimetry and a fluorescence anisotropy competition assay. These investigations demonstrated that the triazole class of phosphohistidine analogues are capable of binding too, suggesting that phosphohistidine could potentially be detected by this class of proteins in vivo.
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Registered trials
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