Tyrosine kinome proiling: Oncogenic mutations and therapeutic targeting in cancer

Paramita Ghosh, Yun Qiu, Ling Yu Wang, Hsing Jien Kung

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Introduction Protein phosphorylation was first discovered by Fischer and Krebs in the mid-1950s (1), and it has been generally accepted that reversible protein phosphorylation regulates virtually every physiological event in mammalian cells. There are approximately 518 protein kinases in human cells. Among them, 89 are tyrosine kinases (2). Phosphorylation by protein tyrosine kinases is crucial to the control of development and growth of multi-cellular organisms. Deregulation or mutation of tyrosine kinases in human cancers has been repeatedly reported in the literature (3). About a quarter of tyrosine kinases were originally discovered as oncogenes, and represent the largest family of oncogenes. Tyrosine kinases are classified as receptor and non-receptor tyrosine kinases. Both classes of tyrosine kinases catalyze the addition of a phosphoryl group on a tyrosine residue but at different locations within the cell – whereas receptor tyrosine kinases (RTKs) are transmembrane proteins, non-receptor tyrosine kinases (NRTKs) are intra-cellular. At present, there are 57 known RTKs in mammalian cells classified into about 20 families, whereas 32 are NRTK, classified into approximately 10 families (Table 8.1).

Original languageEnglish
Title of host publicationMolecular Oncology
Subtitle of host publicationCauses of Cancer and Targets for Treatment
PublisherCambridge University Press
Pages58-75
Number of pages18
ISBN (Electronic)9781139046947
ISBN (Print)9780521876629
DOIs
Publication statusPublished - Jan 1 2015
Externally publishedYes

Fingerprint

Protein-Tyrosine Kinases
Tyrosine
Mutation
Receptor Protein-Tyrosine Kinases
Neoplasms
Phosphorylation
Oncogenes
Therapeutics
TYK2 Kinase
Growth and Development
Protein Kinases
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Ghosh, P., Qiu, Y., Wang, L. Y., & Kung, H. J. (2015). Tyrosine kinome proiling: Oncogenic mutations and therapeutic targeting in cancer. In Molecular Oncology: Causes of Cancer and Targets for Treatment (pp. 58-75). Cambridge University Press. https://doi.org/10.1017/CBO9781139046947.009

Tyrosine kinome proiling : Oncogenic mutations and therapeutic targeting in cancer. / Ghosh, Paramita; Qiu, Yun; Wang, Ling Yu; Kung, Hsing Jien.

Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press, 2015. p. 58-75.

Research output: Chapter in Book/Report/Conference proceedingChapter

Ghosh, P, Qiu, Y, Wang, LY & Kung, HJ 2015, Tyrosine kinome proiling: Oncogenic mutations and therapeutic targeting in cancer. in Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press, pp. 58-75. https://doi.org/10.1017/CBO9781139046947.009
Ghosh P, Qiu Y, Wang LY, Kung HJ. Tyrosine kinome proiling: Oncogenic mutations and therapeutic targeting in cancer. In Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press. 2015. p. 58-75 https://doi.org/10.1017/CBO9781139046947.009
Ghosh, Paramita ; Qiu, Yun ; Wang, Ling Yu ; Kung, Hsing Jien. / Tyrosine kinome proiling : Oncogenic mutations and therapeutic targeting in cancer. Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press, 2015. pp. 58-75
@inbook{49b95ecd9b2b43e9ab4ed79b7f4ac580,
title = "Tyrosine kinome proiling: Oncogenic mutations and therapeutic targeting in cancer",
abstract = "Introduction Protein phosphorylation was first discovered by Fischer and Krebs in the mid-1950s (1), and it has been generally accepted that reversible protein phosphorylation regulates virtually every physiological event in mammalian cells. There are approximately 518 protein kinases in human cells. Among them, 89 are tyrosine kinases (2). Phosphorylation by protein tyrosine kinases is crucial to the control of development and growth of multi-cellular organisms. Deregulation or mutation of tyrosine kinases in human cancers has been repeatedly reported in the literature (3). About a quarter of tyrosine kinases were originally discovered as oncogenes, and represent the largest family of oncogenes. Tyrosine kinases are classified as receptor and non-receptor tyrosine kinases. Both classes of tyrosine kinases catalyze the addition of a phosphoryl group on a tyrosine residue but at different locations within the cell – whereas receptor tyrosine kinases (RTKs) are transmembrane proteins, non-receptor tyrosine kinases (NRTKs) are intra-cellular. At present, there are 57 known RTKs in mammalian cells classified into about 20 families, whereas 32 are NRTK, classified into approximately 10 families (Table 8.1).",
author = "Paramita Ghosh and Yun Qiu and Wang, {Ling Yu} and Kung, {Hsing Jien}",
year = "2015",
month = "1",
day = "1",
doi = "10.1017/CBO9781139046947.009",
language = "English",
isbn = "9780521876629",
pages = "58--75",
booktitle = "Molecular Oncology",
publisher = "Cambridge University Press",

}

TY - CHAP

T1 - Tyrosine kinome proiling

T2 - Oncogenic mutations and therapeutic targeting in cancer

AU - Ghosh, Paramita

AU - Qiu, Yun

AU - Wang, Ling Yu

AU - Kung, Hsing Jien

PY - 2015/1/1

Y1 - 2015/1/1

N2 - Introduction Protein phosphorylation was first discovered by Fischer and Krebs in the mid-1950s (1), and it has been generally accepted that reversible protein phosphorylation regulates virtually every physiological event in mammalian cells. There are approximately 518 protein kinases in human cells. Among them, 89 are tyrosine kinases (2). Phosphorylation by protein tyrosine kinases is crucial to the control of development and growth of multi-cellular organisms. Deregulation or mutation of tyrosine kinases in human cancers has been repeatedly reported in the literature (3). About a quarter of tyrosine kinases were originally discovered as oncogenes, and represent the largest family of oncogenes. Tyrosine kinases are classified as receptor and non-receptor tyrosine kinases. Both classes of tyrosine kinases catalyze the addition of a phosphoryl group on a tyrosine residue but at different locations within the cell – whereas receptor tyrosine kinases (RTKs) are transmembrane proteins, non-receptor tyrosine kinases (NRTKs) are intra-cellular. At present, there are 57 known RTKs in mammalian cells classified into about 20 families, whereas 32 are NRTK, classified into approximately 10 families (Table 8.1).

AB - Introduction Protein phosphorylation was first discovered by Fischer and Krebs in the mid-1950s (1), and it has been generally accepted that reversible protein phosphorylation regulates virtually every physiological event in mammalian cells. There are approximately 518 protein kinases in human cells. Among them, 89 are tyrosine kinases (2). Phosphorylation by protein tyrosine kinases is crucial to the control of development and growth of multi-cellular organisms. Deregulation or mutation of tyrosine kinases in human cancers has been repeatedly reported in the literature (3). About a quarter of tyrosine kinases were originally discovered as oncogenes, and represent the largest family of oncogenes. Tyrosine kinases are classified as receptor and non-receptor tyrosine kinases. Both classes of tyrosine kinases catalyze the addition of a phosphoryl group on a tyrosine residue but at different locations within the cell – whereas receptor tyrosine kinases (RTKs) are transmembrane proteins, non-receptor tyrosine kinases (NRTKs) are intra-cellular. At present, there are 57 known RTKs in mammalian cells classified into about 20 families, whereas 32 are NRTK, classified into approximately 10 families (Table 8.1).

UR - http://www.scopus.com/inward/record.url?scp=84954153477&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84954153477&partnerID=8YFLogxK

U2 - 10.1017/CBO9781139046947.009

DO - 10.1017/CBO9781139046947.009

M3 - Chapter

AN - SCOPUS:84954153477

SN - 9780521876629

SP - 58

EP - 75

BT - Molecular Oncology

PB - Cambridge University Press

ER -