Correction to: Laboratory Investigation. https://doi.org/10.1038/labinvest.2017.126; published online 4 December 2017
Since the publication of the paper the authors have noted some errors in the text.
The corrected text for page 5, paragraph 1 can be found below:
By contrast in an early study of phosphorylated human erythrocytic NDPK by Walinder [77], phospholysine (pLys) and both isomers of pHis were found in the base hydrolysate after chromatographic separation of the phosphoamino acids. However, 31P NMR [66], X-ray crystallography (only the π imidazole nitrogen is available for phosphorylation) [68, 69], and base hydrolysate data [9] have shown that NDPK is autophosphorylated by ATP on a specific His residue to form the π-pHis residue exclusively. Similarly, ACLY has been found to be phosphorylated by NDPK or ATP to form τ-pHis only, both by 31P NMR and in the base hydrolysate [9,78]. So why the discrepancy with the results from Walinder?
Other compound labeling and numbering errors:
Scheme 4: The labelling of the chemical structures has been transposed. The structure on the left should be π-pHis and the structure on the right should be τ-pHis, not the other way round as indicated.
The phrase “triazole residue 16” should be replaced by “triazole residue in peptide 17”, in three locations:
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Page 8, third paragraph, line 14
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Page 9, third paragraph, line 3
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Page 9, third paragraph, line 12
These errors have now been corrected in both the HTML and PDF versions of the paper.
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Makwana, M.V., Muimo, R. & Jackson, R.F. Correction: Advances in development of new tools for the study of phosphohistidine. Lab Invest 99, 438 (2019). https://doi.org/10.1038/s41374-018-0097-5
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DOI: https://doi.org/10.1038/s41374-018-0097-5