Detection and analysis of protein histidine phosphorylation

Besant, Paul G.; Attwood, Paul V.

doi:10.1007/s11010-009-0117-2

Cited by 50 publications

(54 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…[4] These phosphoHis proteins can in turn transphosphorylate Asp residues in transcription factor proteins. [5] In addition, phosphorylation of Arg and Lys are emerging as potentially biologically impactful but are in general poorly understood.…”

Section: Introductionmentioning

confidence: 99%

Synthetic approaches to protein phosphorylation

Chen

Cole

2015

Current Opinion in Chemical Biology

100

View full text Add to dashboard Cite

Reversible protein phosphorylation is critically important in biology and medicine. Hundreds of thousands of sites of protein phosphorylation have been discovered but our understanding of the functions of the vast majority of these post-translational modifications is lacking. This review describes several chemical and biochemical methods that are under development and in current use to install phospho-amino acids and their mimics site-specifically into proteins. The relative merits of total chemical synthesis, semisynthesis, and nonsense suppression strategies for studying protein phosphorylation are discussed in terms of technical simplicity, scope, and versatility.

show abstract

Section: Introductionmentioning

confidence: 99%

Synthetic approaches to protein phosphorylation

Chen

Cole

2015

Current Opinion in Chemical Biology

100

View full text Add to dashboard Cite

show abstract

“…The N-methylamide and acetamide functional groups in 5/6 and 7/8, respectively, mimic the peptide bonds of native phosphohistidine residues, with the free amino and carboxyl groups ready for bioconjugation to a carrier protein through amide linkages with aspartate/glutamate and lysine residues, respectively. In addition, the robust azide-alkyne dipolar cycloaddition (Meldal and Tornoe 2008;Rostovtsev et al 2002;Wu and Fokin 2007) offered the potential to rapidly access enantiopure analogues of both the N1-and N3-regioisomers of phosphohistidine, both of which are biologically relevant (Attwood et al 2007;Besant and Attwood 2009). …”

Section: Introductionmentioning

confidence: 99%

Stable triazolylphosphonate analogues of phosphohistidine

et al. 2011

Self Cite

View full text Add to dashboard Cite

Histidine-phosphorylated proteins and the corresponding kinases are important components of bacterial and eukaryotic cell-signalling pathways, and are therefore potential drug targets. The study of these biomolecules has been hampered by the lability of the phosphoramidate functional group in the phosphohistidines and the lack of generic antibodies. Herein, the design and concise synthesis of stable triazolylphosphonate analogues of N1- and N3-phosphohistidine, and derivatives suitable for bioconjugation, are described.

show abstract

“…71,74,81 However, in the context of this review, some of the most important methods need to be discussed briefly. Detection of pHis residues using antibodies will be discussed in a later section.…”

Section: Detection Of Phosphohistidinementioning

confidence: 99%

Advances in development of new tools for the study of phosphohistidine

Makwana

Muimo

Jackson

2018

Laboratory Investigation

View full text Add to dashboard Cite

Protein phosphorylation is an important post-translational modification that is an integral part of cellular function. The O-phosphorylated amino-acid residues, such as phosphoserine (pSer), phosphothreonine (pThr) and phosphotyrosine (pTyr), have dominated the literature while the acid labile N-linked phosphorylated amino acids, such as phosphohistidine (pHis), have largely been historically overlooked because of the acidic conditions routinely used in amino-acid detection and analysis. This review highlights some misinterpretations that have arisen in the existing literature, pinpoints outstanding questions and potential future directions to clarify the role of pHis in mammalian signalling systems. Particular emphasis is placed on pHis isomerization and the hybrid functionality for both pHis and pTyr of the proposed τ-pHis analogue bearing the triazole residue.

show abstract

Detection and analysis of protein histidine phosphorylation

Cited by 50 publications

References 51 publications

Synthetic approaches to protein phosphorylation

Synthetic approaches to protein phosphorylation

Stable triazolylphosphonate analogues of phosphohistidine

Advances in development of new tools for the study of phosphohistidine

Contact Info

Product

Resources

About