Physiological functions of protein kinase inhibitors.

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Protein kinases are key regulatory enzymes involved in a multitude of biochemical pathways. This chapter will describe the current research on targeting specific protein kinases with inhibitors in attempts to disrupt flux through specific pathways. Targeting specific kinases presents a distinct challenge as there are hundreds of individual kinase enzymes that use ATP as a substrate to phosphorylate specific target molecules. The challenge clearly lies in obtaining specificity for a given kinase, thus allowing inhibition or activation of a specific pathway. This chapter will focus on two areas of kinase inhibitors, those that target the MAP kinase pathway and those directed against the phosphatidylinositol-3 kinase (PI-3K) related kinase family. The cellular and physiological effects of inhibition of the various pathways controlled by these kinases will be reviewed.

Original languageEnglish (US)
Pages (from-to)109-121
Number of pages13
JournalEXS
Volume89
StatePublished - 2000
Externally publishedYes

Fingerprint

Protein Kinase Inhibitors
Phosphotransferases
Phosphatidylinositol 3-Kinase
Enzymes
Protein Kinases
Adenosine Triphosphate
Research

Cite this

Physiological functions of protein kinase inhibitors. / Turchi, John; Ho, M.

In: EXS, Vol. 89, 2000, p. 109-121.

Research output: Contribution to journalArticle

Turchi, John ; Ho, M. / Physiological functions of protein kinase inhibitors. In: EXS. 2000 ; Vol. 89. pp. 109-121.
@article{9016fa0929f7417aa88dde3ac4325ce5,
title = "Physiological functions of protein kinase inhibitors.",
abstract = "Protein kinases are key regulatory enzymes involved in a multitude of biochemical pathways. This chapter will describe the current research on targeting specific protein kinases with inhibitors in attempts to disrupt flux through specific pathways. Targeting specific kinases presents a distinct challenge as there are hundreds of individual kinase enzymes that use ATP as a substrate to phosphorylate specific target molecules. The challenge clearly lies in obtaining specificity for a given kinase, thus allowing inhibition or activation of a specific pathway. This chapter will focus on two areas of kinase inhibitors, those that target the MAP kinase pathway and those directed against the phosphatidylinositol-3 kinase (PI-3K) related kinase family. The cellular and physiological effects of inhibition of the various pathways controlled by these kinases will be reviewed.",
author = "John Turchi and M. Ho",
year = "2000",
language = "English (US)",
volume = "89",
pages = "109--121",
journal = "Experientia. Supplementum",
issn = "1023-294X",
publisher = "Birkhauser Verlag Basel",

}

TY - JOUR

T1 - Physiological functions of protein kinase inhibitors.

AU - Turchi, John

AU - Ho, M.

PY - 2000

Y1 - 2000

N2 - Protein kinases are key regulatory enzymes involved in a multitude of biochemical pathways. This chapter will describe the current research on targeting specific protein kinases with inhibitors in attempts to disrupt flux through specific pathways. Targeting specific kinases presents a distinct challenge as there are hundreds of individual kinase enzymes that use ATP as a substrate to phosphorylate specific target molecules. The challenge clearly lies in obtaining specificity for a given kinase, thus allowing inhibition or activation of a specific pathway. This chapter will focus on two areas of kinase inhibitors, those that target the MAP kinase pathway and those directed against the phosphatidylinositol-3 kinase (PI-3K) related kinase family. The cellular and physiological effects of inhibition of the various pathways controlled by these kinases will be reviewed.

AB - Protein kinases are key regulatory enzymes involved in a multitude of biochemical pathways. This chapter will describe the current research on targeting specific protein kinases with inhibitors in attempts to disrupt flux through specific pathways. Targeting specific kinases presents a distinct challenge as there are hundreds of individual kinase enzymes that use ATP as a substrate to phosphorylate specific target molecules. The challenge clearly lies in obtaining specificity for a given kinase, thus allowing inhibition or activation of a specific pathway. This chapter will focus on two areas of kinase inhibitors, those that target the MAP kinase pathway and those directed against the phosphatidylinositol-3 kinase (PI-3K) related kinase family. The cellular and physiological effects of inhibition of the various pathways controlled by these kinases will be reviewed.

UR - http://www.scopus.com/inward/record.url?scp=0033641520&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033641520&partnerID=8YFLogxK

M3 - Article

VL - 89

SP - 109

EP - 121

JO - Experientia. Supplementum

JF - Experientia. Supplementum

SN - 1023-294X

ER -