A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination

Research output: Contribution to journal › Journal article › Research › peer-review

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A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination. / Rudolf, Amalie Frederikke; Skovgaard, Tine; Knapp, Stefan; Jensen, Lars Juhl; Berthelsen, Jens.

In: PloS one, Vol. 9, No. 6, e98800, 2014, p. 1-5.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rudolf, AF, Skovgaard, T, Knapp, S, Jensen, LJ & Berthelsen, J 2014, 'A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination', PloS one, vol. 9, no. 6, e98800, pp. 1-5. https://doi.org/10.1371/journal.pone.0098800

APA

Rudolf, A. F., Skovgaard, T., Knapp, S., Jensen, L. J., & Berthelsen, J. (2014). A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination. PloS one, 9(6), 1-5. [e98800]. https://doi.org/10.1371/journal.pone.0098800

Vancouver

Rudolf AF, Skovgaard T, Knapp S, Jensen LJ, Berthelsen J. A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination. PloS one. 2014;9(6):1-5. e98800. https://doi.org/10.1371/journal.pone.0098800

Author

Rudolf, Amalie Frederikke ; Skovgaard, Tine ; Knapp, Stefan ; Jensen, Lars Juhl ; Berthelsen, Jens. / A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination. In: PloS one. 2014 ; Vol. 9, No. 6. pp. 1-5.

Bibtex

@article{c91d1c46b6f14eca8ea9a2915e12c016,
title = "A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination",
abstract = "Binding assays are increasingly used as a screening method for protein kinase inhibitors; however, as yet only a weak correlation with enzymatic activity-based assays has been demonstrated. We show that the correlation between the two types of assays can be improved using more precise screening conditions. Furthermore a marked improvement in the correlation was found by using kinase constructs containing the catalytic domain in presence of additional domains or subunits.",
author = "Rudolf, {Amalie Frederikke} and Tine Skovgaard and Stefan Knapp and Jensen, {Lars Juhl} and Jens Berthelsen",
year = "2014",
doi = "10.1371/journal.pone.0098800",
language = "English",
volume = "9",
pages = "1--5",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "6",

}

RIS

TY - JOUR

T1 - A comparison of protein kinases inhibitor screening methods using both enzymatic activity and binding affinity determination

AU - Rudolf, Amalie Frederikke

AU - Skovgaard, Tine

AU - Knapp, Stefan

AU - Jensen, Lars Juhl

AU - Berthelsen, Jens

PY - 2014

Y1 - 2014

N2 - Binding assays are increasingly used as a screening method for protein kinase inhibitors; however, as yet only a weak correlation with enzymatic activity-based assays has been demonstrated. We show that the correlation between the two types of assays can be improved using more precise screening conditions. Furthermore a marked improvement in the correlation was found by using kinase constructs containing the catalytic domain in presence of additional domains or subunits.

AB - Binding assays are increasingly used as a screening method for protein kinase inhibitors; however, as yet only a weak correlation with enzymatic activity-based assays has been demonstrated. We show that the correlation between the two types of assays can be improved using more precise screening conditions. Furthermore a marked improvement in the correlation was found by using kinase constructs containing the catalytic domain in presence of additional domains or subunits.

U2 - 10.1371/journal.pone.0098800

DO - 10.1371/journal.pone.0098800

M3 - Journal article

C2 - 24915177

VL - 9

SP - 1

EP - 5

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 6

M1 - e98800

ER -

ID: 117611949