A fluorescence resonance energy transfer-based method for histone methyltransferases

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A fluorescence resonance energy transfer-based method for histone methyltransferases. / Devkota, Kanchan; Lohse, Brian; Nyby Jakobsen, Camilla; Berthelsen, Jens; Clausen, Rasmus Prætorius.

In: Analytical Biochemistry, Vol. 476, 19.02.2015, p. 78-80.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Devkota, K, Lohse, B, Nyby Jakobsen, C, Berthelsen, J & Clausen, RP 2015, 'A fluorescence resonance energy transfer-based method for histone methyltransferases', Analytical Biochemistry, vol. 476, pp. 78-80. https://doi.org/10.1016/j.ab.2015.02.012

APA

Devkota, K., Lohse, B., Nyby Jakobsen, C., Berthelsen, J., & Clausen, R. P. (2015). A fluorescence resonance energy transfer-based method for histone methyltransferases. Analytical Biochemistry, 476, 78-80. https://doi.org/10.1016/j.ab.2015.02.012

Vancouver

Devkota K, Lohse B, Nyby Jakobsen C, Berthelsen J, Clausen RP. A fluorescence resonance energy transfer-based method for histone methyltransferases. Analytical Biochemistry. 2015 Feb 19;476:78-80. https://doi.org/10.1016/j.ab.2015.02.012

Author

Devkota, Kanchan ; Lohse, Brian ; Nyby Jakobsen, Camilla ; Berthelsen, Jens ; Clausen, Rasmus Prætorius. / A fluorescence resonance energy transfer-based method for histone methyltransferases. In: Analytical Biochemistry. 2015 ; Vol. 476. pp. 78-80.

Bibtex

@article{638ae6471b984cd8863da9407b0bfc21,
title = "A fluorescence resonance energy transfer-based method for histone methyltransferases",
abstract = "A simple dye–quencher fluorescence resonance energy transfer (FRET)-based assay for methyltransferases was developed and used to determine kinetic parameters and inhibitory activity at EHMT1 and EHMT2. Peptides mimicking the truncated histone H3 tail were functionalized in each end with a dye and a quencher, respectively. When lysine-9 residues in the peptides were methylated, they were protected from cleavage by endoproteinase–EndoLysC, whereas unmethylated peptides were cleaved, resulting in an increase in fluorescent intensity.",
keywords = "The Faculty of Health and Medical Sciences",
author = "Kanchan Devkota and Brian Lohse and {Nyby Jakobsen}, Camilla and Jens Berthelsen and Clausen, {Rasmus Pr{\ae}torius}",
year = "2015",
month = "2",
day = "19",
doi = "10.1016/j.ab.2015.02.012",
language = "English",
volume = "476",
pages = "78--80",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - A fluorescence resonance energy transfer-based method for histone methyltransferases

AU - Devkota, Kanchan

AU - Lohse, Brian

AU - Nyby Jakobsen, Camilla

AU - Berthelsen, Jens

AU - Clausen, Rasmus Prætorius

PY - 2015/2/19

Y1 - 2015/2/19

N2 - A simple dye–quencher fluorescence resonance energy transfer (FRET)-based assay for methyltransferases was developed and used to determine kinetic parameters and inhibitory activity at EHMT1 and EHMT2. Peptides mimicking the truncated histone H3 tail were functionalized in each end with a dye and a quencher, respectively. When lysine-9 residues in the peptides were methylated, they were protected from cleavage by endoproteinase–EndoLysC, whereas unmethylated peptides were cleaved, resulting in an increase in fluorescent intensity.

AB - A simple dye–quencher fluorescence resonance energy transfer (FRET)-based assay for methyltransferases was developed and used to determine kinetic parameters and inhibitory activity at EHMT1 and EHMT2. Peptides mimicking the truncated histone H3 tail were functionalized in each end with a dye and a quencher, respectively. When lysine-9 residues in the peptides were methylated, they were protected from cleavage by endoproteinase–EndoLysC, whereas unmethylated peptides were cleaved, resulting in an increase in fluorescent intensity.

KW - The Faculty of Health and Medical Sciences

U2 - 10.1016/j.ab.2015.02.012

DO - 10.1016/j.ab.2015.02.012

M3 - Journal article

VL - 476

SP - 78

EP - 80

JO - Analytical Biochemistry

JF - Analytical Biochemistry

SN - 0003-2697

ER -

ID: 135502040