Results 301 to 310 of about 817,279 (353)

Self-reporting fluorescent substrates of protein tyrosine kinases.

Journal of the American Chemical Society, 2006
A new mechanistic principle by which protein tyrosine kinase substrates fluorescently report the introduction of a phosphate moiety has been developed.
Qunzhao Wang, S. Cahill, M. Blumenstein, D. Lawrence   +3 more
semanticscholar   +1 more source

Oncogenic protein tyrosine kinases

Cellular and Molecular Life Sciences, 2004
Tyrosine kinases (TKs) and related molecules comprise over 100 different genes. Approximately two-thirds represent receptor TKs, the other third being non receptor TKs. TKs regulate important cellular signalling, from the transduction of extracellular signals to the regulation of key biological processes such as cell proliferation and apoptosis [1, 2].
openaire   +3 more sources

Protein tyrosine kinases in thymocyte development

Current Opinion in Immunology, 1997
Much has been learned over the past few years about how protein tyrosine kinases mediate pre-TCR and mature alphabetaTCR function. The highlights include understanding the roles and the distinct effects of the Src and Syk families of protein tyrosine kinases in thymocyte development and function.
Andrew C. Chan, Alec M. Cheng
openaire   +3 more sources

The c-Fes family of protein-tyrosine kinases.

Critical reviews in oncogenesis, 1998
The human c-fes protooncogene encodes a protein-tyrosine kinase (c-Fes) distinct from c-Src, c-Abl and other nonreceptor tyrosine kinases. Although originally identified as the cellular homolog of several transforming retroviral oncoproteins, Fes was ...
T. Smithgall, J. Rogers, K. Peters, J. Li, S. Briggs, J. Lionberger, H. Cheng, A. Shibata, B. Scholtz, S. Schreiner, N. Dunham   +10 more
semanticscholar   +1 more source

Protein Tyrosine Kinase Structure and Function

Annual Review of Biochemistry, 2000
▪ Abstract  Tyrosine phosphorylation is one of the key covalent modifications that occurs in multicellular organisms as a result of intercellular communication during embryogenesis and maintenance of adult tissues. The enzymes that carry out this modification are the protein tyrosine kinases (PTKs), which catalyze the transfer of the γ phosphate of ...
Jeffrey H. Till, Stevan R. Hubbard
openaire   +2 more sources

Protein tyrosine kinases in malignant melanoma

Melanoma Research, 2000
Protein tyrosyl phosphorylation is an essential component in intracellular signalling, with diverse and crucial functions including mediation of cell proliferation, survival, death, differentiation, migration and attachment. It is regulated by the balance between the activities of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases.
Dorothy C. Bennett, David J. Easty
openaire   +3 more sources

Non-receptor protein tyrosine kinases

Frontiers in Bioscience, 2003
The protein tyrosine kinases (PTKs) are enzymes catalyzing the transfer of the gamma-phosphate group of ATP to the hydroxyl groups of specific tyrosine residues in peptides. Although phosphotransfer reactions catalyzed by various PTKs are similar with regard to their basic mechanisms, their biological functions demonstrate a considerable degree of ...
openaire   +2 more sources

Protein tyrosine kinase–substrate interactions

Current Opinion in Structural Biology, 2006
Protein tyrosine kinases (PTKs) are enzymes that catalyze the phosphorylation of tyrosyl residues. They are important in physiological and pathophysiological processes. Protein substrates of PTKs are often difficult to discern, but recently reported methods have helped to identify targets and characterize their structural interactions with kinases.
Philip A. Cole, Kerry A. Pickin, Marc A. Holbert, Ron Bose   +3 more
openaire   +3 more sources

Tec protein‐tyrosine kinase is an effector molecule of Lyn proteni‐tyroenie kinase

The FASEB Journal, 1996
The Tec family is a recently emerging subfamily among nonreceptor type protein-tyrosine kinases (PTKs) consisting of Tec, Txk, Btk, Bmx, and Itk/Tsk/Emt. They have a long amino-terminal unique region containing a pleckstrin homology domain and a Tec-homology domain.
Yasusada Miura, Yoshihiro Yamashita, Akkra Miyazato, Keiya Ozawa, Hiroyuki Mano   +4 more
openaire   +3 more sources

Mechanisms of Transformation by Protein-Tyrosine Kinases

1988
In multicellular organisms there must be stringent control over the processes of cellular proliferation and differentiation. Thus sophisticated networks of regulatory molecules have evolved to sense and transmit signals within and between normal cells.
William H. Colledge, Michael J. Fry, John C. Bell, Michael G. Sargent, J. Gordon Foulkes, A. Raymond Frackelton, Louis Mahadevan   +6 more
openaire   +3 more sources