Results 201 to 210 of about 3,793,046 (254)

CD14 Plays a Critical Role in Pain and Inflammation Across Multiple Models of Post‐traumatic Osteoarthritis

Arthritis &Rheumatology, EarlyView.
Objective We employed global genetic deletion of CD14 and intra‐articular CD14 blockade across multiple murine osteoarthritis (OA) models that vary in severity of pathology and rate of progression to test the hypothesis that CD14 inhibition attenuates synovial inflammation and associated pain during disease progression.
Kevin G. Burt, Sanique M. South, Natalie S. Adamczyk, Vu Nguyen, Shingo Ishihara, Cheng Zhou, Kate L. Sharp, Sung Y. Kim, Anna E. Rapp, Baofeng Hu, Lance A. Murphy, Li‐Yin Hung, De'Broski Herbert, Joshua F. Baker, Robert L. Mauck, Timothy M. Griffin, Anne‐Marie Malfait, Rachel E. Miller, Carla R. Scanzello   +18 more
wiley   +1 more source

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Protein tyrosine kinases in the initiation of antigen receptor signaling

Current Opinion in Immunology, 1995
Intracellular responses to antigen receptor engagement involve the activation of protein tyrosine kinases and the tyrosine phosphorylation of cellular proteins, including components of the antigen receptor. Phosphorylation of two tyrosine residues within an 18 amino acid segment of the cytoplasmic domain of antigen receptor subunits, and the subsequent
Joseph B Bolen, J B Bolen, J Bolen
exaly   +3 more sources

Regulation of antigen receptor signal transduction by protein tyrosine kinases

Current Opinion in Immunology, 1996
The past two years have seen further clarification of the early events occurring in antigen receptor signal transduction that are mediated by the immunoreceptor tyrosine-based activation motif (ITAM). The ITAM was shown to be a specific binding site for the ZAP-70/Syk protein tyrosine kinases and the structure of this complex was solved.
Andrey Shaw, Andrew Chan
exaly   +3 more sources

Signalling pathways initiated by receptor protein tyrosine kinases in Drosophila

Current Opinion in Cell Biology, 1994
The isolation and characterization of Drosophila mutations in receptor protein tyrosine kinases (RPTKs) have allowed a detailed analysis of the cellular processes regulated by these proteins. Recent investigations have identified a number of putative ligands involved in the activation of the receptors, and have demonstrated that these RPTKs trigger an ...
Norbert Perrimon
exaly   +3 more sources

Receptor Protein-Tyrosine Kinases and Their Signal Transduction Pathways

Annual Review of Cell Biology, 1994
Tony Hunter, Peter Van Der Geer, Richard A Lindberg   +2 more
exaly   +3 more sources

Membrane receptors with protein-tyrosine kinase activity

Biochimie, 1987
Protein-tyrosine kinase activities have appeared so far to be intrinsic for two classes of proteins: the transforming proteins of certain retroviral oncogenes and the membrane receptors for certain cellular growth factors. In this latter family, the protein-tyrosine kinase is activated upon binding of the growth factor to its receptor and ...
J J, Feige, E M, Chambaz
openaire   +2 more sources

src-related protein tyrosine kinases and their surface receptors

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer, 1993
The CD4-p56lck and CD8-p56lck complexes have served as a paradym for an expanding number of interactions between src-family members (p56lck, p59fyn, p56lyn, p55blk) and surface receptors. These interactions implicate src-related kinases in the regulation of a variety of intracellular events, from lymphokine production and cytotoxicity to the expression
Telfer, Janice T., Rudd, C.E., Janssen, O., Prasad, K.V.S., Raab, M., Dasilva, A., Yamamoto, H.   +6 more
openaire   +2 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

B61 is a ligand for the ECK receptor protein-tyrosine kinase

Nature, 1994
A protein ligand for the ECK receptor protein-tyrosine kinase has been isolated by using the extracellular domain (ECK-X) of the receptor as an affinity reagent. Initially, concentrated cell culture supernatants were screened for receptor binding activity using immobilized ECK-X in a surface plasmon resonance detection system.
Timothy D. Bartley, Robert W. Hunt, Andrew A. Welcher, William J. Boyle, Vann P. Parker, Richard A. Lindberg, Hsieng S. Lu, Anne M. Colombero, Robin L. Elliott, Brenda A. Guthrie, Paige L. Holst, James D. Skrine, Robert J. Toso, Ming Zhang, Elsa Fernandez, Geraldine Trail, Brian Varnum, Yosef Yarden, Tony Hunter, Gary M. Fox   +19 more
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Comparative characterization of receptor and non-receptor associated protein tyrosine kinases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
By using poly(Glu: Tyr, 4:1) as an exogenous substrate, the characteristics of insulin receptor associated protein tyrosine kinase (PTK) from rabbit skeletal muscle has been compared with a growth factor-independent non-receptor PTK partially purified from rat lung particulate fraction.
A K, Srivastava, J L, Chiasson
openaire   +2 more sources