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From the same journal

Efficient N-terminal labeling of proteins by use of sortase

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Efficient N-terminal labeling of proteins by use of sortase. / Williamson, D.J.; Fascione, M.A.; Webb, M.E.; Turnbull, W.B.

In: Angewandte Chemie International Edition, Vol. 51, No. 37, 10.09.2012, p. 9377-9380.

Research output: Contribution to journalArticlepeer-review

Harvard

Williamson, DJ, Fascione, MA, Webb, ME & Turnbull, WB 2012, 'Efficient N-terminal labeling of proteins by use of sortase', Angewandte Chemie International Edition, vol. 51, no. 37, pp. 9377-9380. https://doi.org/10.1002/anie.201204538

APA

Williamson, D. J., Fascione, M. A., Webb, M. E., & Turnbull, W. B. (2012). Efficient N-terminal labeling of proteins by use of sortase. Angewandte Chemie International Edition, 51(37), 9377-9380. https://doi.org/10.1002/anie.201204538

Vancouver

Williamson DJ, Fascione MA, Webb ME, Turnbull WB. Efficient N-terminal labeling of proteins by use of sortase. Angewandte Chemie International Edition. 2012 Sep 10;51(37):9377-9380. https://doi.org/10.1002/anie.201204538

Author

Williamson, D.J. ; Fascione, M.A. ; Webb, M.E. ; Turnbull, W.B. / Efficient N-terminal labeling of proteins by use of sortase. In: Angewandte Chemie International Edition. 2012 ; Vol. 51, No. 37. pp. 9377-9380.

Bibtex - Download

@article{f21d126d51904921a64113900791550d,
title = "Efficient N-terminal labeling of proteins by use of sortase",
abstract = "{"}Sorting out{"} N-terminal labeling: The reversibility of transpeptidase reactions makes protein N-terminal labeling challenging. Depsipeptide substrates for sortase A release alcohol by-products, which are poor nucleophiles for the reverse reaction, during ligation. Proteins with an unhindered N-terminal glycine residue can be labeled efficiently with only a minimal excess of the labeling reagent (see scheme).",
author = "D.J. Williamson and M.A. Fascione and M.E. Webb and W.B. Turnbull",
year = "2012",
month = sep,
day = "10",
doi = "10.1002/anie.201204538",
language = "English",
volume = "51",
pages = "9377--9380",
journal = "Angewandte Chemie International Edition",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",
number = "37",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Efficient N-terminal labeling of proteins by use of sortase

AU - Williamson, D.J.

AU - Fascione, M.A.

AU - Webb, M.E.

AU - Turnbull, W.B.

PY - 2012/9/10

Y1 - 2012/9/10

N2 - "Sorting out" N-terminal labeling: The reversibility of transpeptidase reactions makes protein N-terminal labeling challenging. Depsipeptide substrates for sortase A release alcohol by-products, which are poor nucleophiles for the reverse reaction, during ligation. Proteins with an unhindered N-terminal glycine residue can be labeled efficiently with only a minimal excess of the labeling reagent (see scheme).

AB - "Sorting out" N-terminal labeling: The reversibility of transpeptidase reactions makes protein N-terminal labeling challenging. Depsipeptide substrates for sortase A release alcohol by-products, which are poor nucleophiles for the reverse reaction, during ligation. Proteins with an unhindered N-terminal glycine residue can be labeled efficiently with only a minimal excess of the labeling reagent (see scheme).

UR - http://www.scopus.com/inward/record.url?scp=84865850342&partnerID=8YFLogxK

U2 - 10.1002/anie.201204538

DO - 10.1002/anie.201204538

M3 - Article

AN - SCOPUS:84865850342

VL - 51

SP - 9377

EP - 9380

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

SN - 1433-7851

IS - 37

ER -