Kinase Inhibitors

Costerton Biofilm Center

Department of Immunology and Microbiology

Kinase Inhibitors

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Kinase Inhibitors. / Wu, Peng; Givskov, Michael; Nielsen, Thomas E.

Drug Selectivity: An Evolving Concept in Medicinal Chemistry. Wiley-Interscience, 2017. p. 33-53.

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Wu, P, Givskov, M & Nielsen, TE 2017, Kinase Inhibitors. in Drug Selectivity: An Evolving Concept in Medicinal Chemistry. Wiley-Interscience, pp. 33-53. https://doi.org/10.1002/9783527674381.ch2

APA

Wu, P., Givskov, M., & Nielsen, T. E. (2017). Kinase Inhibitors. In Drug Selectivity: An Evolving Concept in Medicinal Chemistry (pp. 33-53). Wiley-Interscience. https://doi.org/10.1002/9783527674381.ch2

Vancouver

Wu P, Givskov M, Nielsen TE. Kinase Inhibitors. In Drug Selectivity: An Evolving Concept in Medicinal Chemistry. Wiley-Interscience. 2017. p. 33-53 https://doi.org/10.1002/9783527674381.ch2

Author

Wu, Peng ; Givskov, Michael ; Nielsen, Thomas E. / Kinase Inhibitors. Drug Selectivity: An Evolving Concept in Medicinal Chemistry. Wiley-Interscience, 2017. pp. 33-53

Bibtex

@inbook{aa6b69047a3e4c59add637f1beb4f99c,

title = "Kinase Inhibitors",

abstract = "The strategy of applying kinase inhibitors as effective therapeutic agents has achieved unparalleled success in the past decade, while it is still a daunting challenge to develop kinase inhibitors with desirable selectivity among different kinase families. This chapter describes the basic conceptions in the field of kinase selectivity, available profiling technologies, and quantification of selectivity levels. The chapter highlights the different selectivity of approved kinase inhibitors, which include non-covalent type I and II ATP-competitive inhibitors, allosteric inhibitors, one lipid kinase inhibitor, and covalent inhibitors. Most approved kinase inhibitors are multitarget or unselective inhibitors that bind with the highly conserved ATP pocket, high selectivity is more likely to be achieved among kinases with only few closely related homologs or unique structural features in binding sites.",

keywords = "Allosteric inhibitor, Covalent inhibitor, Kinase profiling, Selective inhibitor",

author = "Peng Wu and Michael Givskov and Nielsen, {Thomas E.}",

year = "2017",

doi = "10.1002/9783527674381.ch2",

language = "English",

isbn = "9783527335381",

pages = "33--53",

booktitle = "Drug Selectivity",

publisher = "Wiley-Interscience",

}

RIS

TY - CHAP

T1 - Kinase Inhibitors

AU - Wu, Peng

AU - Givskov, Michael

AU - Nielsen, Thomas E.

PY - 2017

Y1 - 2017

N2 - The strategy of applying kinase inhibitors as effective therapeutic agents has achieved unparalleled success in the past decade, while it is still a daunting challenge to develop kinase inhibitors with desirable selectivity among different kinase families. This chapter describes the basic conceptions in the field of kinase selectivity, available profiling technologies, and quantification of selectivity levels. The chapter highlights the different selectivity of approved kinase inhibitors, which include non-covalent type I and II ATP-competitive inhibitors, allosteric inhibitors, one lipid kinase inhibitor, and covalent inhibitors. Most approved kinase inhibitors are multitarget or unselective inhibitors that bind with the highly conserved ATP pocket, high selectivity is more likely to be achieved among kinases with only few closely related homologs or unique structural features in binding sites.

AB - The strategy of applying kinase inhibitors as effective therapeutic agents has achieved unparalleled success in the past decade, while it is still a daunting challenge to develop kinase inhibitors with desirable selectivity among different kinase families. This chapter describes the basic conceptions in the field of kinase selectivity, available profiling technologies, and quantification of selectivity levels. The chapter highlights the different selectivity of approved kinase inhibitors, which include non-covalent type I and II ATP-competitive inhibitors, allosteric inhibitors, one lipid kinase inhibitor, and covalent inhibitors. Most approved kinase inhibitors are multitarget or unselective inhibitors that bind with the highly conserved ATP pocket, high selectivity is more likely to be achieved among kinases with only few closely related homologs or unique structural features in binding sites.

KW - Allosteric inhibitor

KW - Covalent inhibitor

KW - Kinase profiling

KW - Selective inhibitor

U2 - 10.1002/9783527674381.ch2

DO - 10.1002/9783527674381.ch2

M3 - Book chapter

AN - SCOPUS:85045371021

SN - 9783527335381

SP - 33

EP - 53

BT - Drug Selectivity

PB - Wiley-Interscience

ER -

ID: 340025606