Zobrazeno 1 - 10
of 23
pro vyhledávání: '"D. E. Cool"'
Autor:
D. E. Cool, J. J. Blum
Publikováno v:
Molecular and Cellular Biochemistry. :143-149
Autor:
B Bossenmaier, Joseph Schlessinger, Axel Ullrich, Richard L. Lammers, E H Fischer, Nicholas K. Tonks, D E Cool
Publikováno v:
Journal of Biological Chemistry. 268:22456-22462
We have employed transient co-overexpression of protein tyrosine phosphatases (PTPs) with a panel of receptor tyrosine kinases (RTKs) to investigate molecular parameters that regulate dephosphorylation activity and specificity in intact cells. Our re
Autor:
D. E. Cool, Jeanne B. Lawrence, Arthur M. Bruskin, Nancy R. Green, David E. Hill, Moira B. Glaccum, Edmond H. Fischer, Carol V. Johnson
Publikováno v:
Genomics. 16:619-629
This work reports the isolation, partial characterization, and chromosomal mapping of several human T-cell protein tyrosine phosphatase (PTPase) sequences and provides a direct comparison of the specificity of cDNA versus genomic probes in discrimina
Publikováno v:
Analytical Biochemistry. 211:50-54
The determination of protein tyrosine phosphatase (PTP) activity using different protein substrates such as modified lysozyme or myelin basic protein is greatly affected by the type of enzyme involved, the condition of the assay, and the presence of
Publikováno v:
Ciba Foundation Symposium 164-Interactions Among Cell Signalling Systems
Protein tyrosine phosphatases represent a new family of intracellular and receptor-linked enzymes. They are totally specific toward tyrosyl residues in proteins, and, with specific activities 10-1000-fold greater than those of the protein tyrosine ki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2181a5cace769dd8597558fcc8e5732c
https://doi.org/10.1002/9780470514207.ch9
https://doi.org/10.1002/9780470514207.ch9
Publikováno v:
Molecular and cellular biochemistry.
L. Donovani promastigotes were grown to late-log and 3-day stationary phase to determine the level of protein tyrosine phosphatase activity in crude extracts and in fractions following gel filtration column chromatography. Over 90% of the activity wa
Publikováno v:
The Journal of biological chemistry. 268(30)
We have employed transient co-overexpression of protein tyrosine phosphatases (PTPs) with a panel of receptor tyrosine kinases (RTKs) to investigate molecular parameters that regulate dephosphorylation activity and specificity in intact cells. Our re
Publikováno v:
Oncogene. 8(5)
Rat 2 cells stably transformed by murine v-fms (pB5 cells) were infected with retroviruses containing a human cDNA encoding either a full-length human T-cell protein tyrosine phosphatase (TC.PTP) or a truncated form (delta C11.PTP) in which an 11-kDa
Autor:
D. E. Cool, J. J. Blum
Publikováno v:
Reversible Protein Phosphorylation in Cell Regulation ISBN: 9780792326373
L. Donovani promastigotes were grown to late-log and 3-day stationary phase to determine the level of protein tyro sine phosphatase activity in crude extracts and in fractions following gel filtration column chromatography. Over 90% of the activity w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b717c69f98ce65ad1dad8df416d1a8d
https://doi.org/10.1007/978-1-4615-2600-1_13
https://doi.org/10.1007/978-1-4615-2600-1_13
Publikováno v:
Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling ISBN: 9783642782497
Tyrosine phosphorylation, discovered a little over ten years ago, has represented one of the most exciting developments in the field of cellular regulation. It has been well established that receptor or membrane-bound tyrosine kinases afford primary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::178c212967402337364bda071f276b93
https://doi.org/10.1007/978-3-642-78247-3_1
https://doi.org/10.1007/978-3-642-78247-3_1