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Conformationally Induced Off-On Cell Membrane Chemosensor Targeting Receptor Protein-Tyrosine Kinases for in Vivo and in Vitro Fluorescence Imaging of Cancers.

Journal of the American Chemical Society, 2018
Molecules capable of monitoring receptor protein-tyrosine kinase expression could potentially serve as useful tools for cancer diagnosis due to the overexpression of tyrosine kinases during tumor growth and metastasis.
Yang Jiao   +5 more
semanticscholar   +1 more source

Inhibitors of protein tyrosine kinases

Current Opinion in Biotechnology, 1995
The description in the past year of several novel protein tyrosine kinase inhibitors, which exhibit dramatic improvements in potency and specificity over earlier agents, will be considered a major turning point in the field. These compounds appear to have the necessary pharmacological properties to finally allow clarification of whether suppression of ...
David W. Fry, Alexander James Bridges
openaire   +3 more sources

Protein Tyrosine Kinase Activity Assays [PDF]

open access: possibleCurrent Protocols in Pharmacology, 1999
AbstractProtein tyrosine kinases (PTKs) are ubiquitous enzymes that are integrally involved in the regulation of transformation mechanisms, normal and pathological growth, cell cycle regulation, immune responses, and a variety of intracellular signaling mechanisms.
Brian E. Hawes, Tim van Biesen
openaire   +2 more sources

GPI-anchored cell-surface molecules complexed to protein tyrosine kinases.

Science, 1991
Binding of ligand or antibody to certain cell-surface proteins that are anchored to the membrane by glycophosphatidylinositol (GPI) can cause activation of leukocytes.
I. Štefanov́a   +4 more
semanticscholar   +1 more source

Platelet Protein Tyrosine Kinases [PDF]

open access: possible, 1997
The first protein tyrosine kinase (PTK) to be identified, detected by Hunter and Sefton in 1979, was the transforming protein of the Rous sarcoma virus (Hunter and Sefton 1980). This 60-kDa phosphoprotein is encoded by the viral src oncogene (v-src) and is denoted pp60 v-src .
E. A. Martinson, P. Presek
openaire   +1 more source

6 Protein Tyrosine Kinase Inhibitors

1996
Publisher Summary This chapter describes the classification and structure of protein tyrosine kinases (PTKs), their mode of action, their cellular targets, and the processes in which they are involved. A vast amount of research has been carried out to try to identify the role of PTKs in the general functioning and development of normal mammalian ...
Kevin R. H. Solomons   +3 more
openaire   +3 more sources

Cytokine signaling through nonreceptor protein tyrosine kinases.

Science, 1995
Cytokines are a family of soluble mediators of cell-to-cell communication that includes interleukins, interferons, and colony-stimulating factors. The characteristic features of cytokines lie in their functional redundancy and pleiotropy.
T. Taniguchi
semanticscholar   +1 more source

SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases.

Science, 1993
A mouse phosphotyrosine phosphatase containing two Src homology 2 (SH2) domains, Syp, was identified. Syp bound to autophosphorylated epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors through its SH2 domains and was ...
G. Feng, C. Hui, T. Pawson
semanticscholar   +1 more source

Nuclear protein tyrosine kinases

Trends in Biochemical Sciences, 1994
Protein tyrosine phosphorylation plays an important role in the transduction of extracellular signals. The prototypical protein tyrosine kinases are localized at the plasma membrane and are coupled to receptors that bind extracellular factors. Thus, protein tyrosine phosphorylation was previously thought to occur only in the cytoplasm. However, several
openaire   +3 more sources

Protein—Tyrosine Kinases and Their Substrates [PDF]

open access: possible, 1990
Protein phosphorylation, through its ability to increase or decrease the activity of proteins, plays a central role in cellular regulation. Most proteins known to be regulated by phosphorylation are substrates for both a protein kinase and a protein phosphatase.
David S. Middlemas   +5 more
openaire   +1 more source

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