Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Curtis D. Diltz"'
Autor:
Edmond H. Fischer, Diana I. Lurie, Flavio F. Solca, Santosh Kumar, Curtis D. Diltz, Richard S. Johnson, Edwin W. Rubel
Publikováno v:
Journal of Biological Chemistry. 269:27559-27565
The identification, purification, and biochemical characterization of specific markers for neuroglial cells in the central nervous system is an essential step toward a better understanding of the function of glial cells. This manuscript reports the i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::647ea61f4ea7dd1243e0f784cc6a4c40
https://doi.org/10.1016/s0021-9258(18)47021-4
https://doi.org/10.1016/s0021-9258(18)47021-4
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::218001f4c549e815590cdc2534be9192
https://doi.org/10.1006/abio.1993.1231
https://doi.org/10.1006/abio.1993.1231
Publikováno v:
Journal of Biological Chemistry. 268:2816-2820
A protein tyrosine phosphatase (PTP) containing two SH2 domains (PTP1C) was purified to near homogeneity from an adenovirus expression system by a two-step chromatographic procedure with a yield of 67%. The purified enzyme behaves as a monomer of 68
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24a73042500b703faa139bd749a3e428
https://doi.org/10.1016/s0021-9258(18)53846-1
https://doi.org/10.1016/s0021-9258(18)53846-1
Autor:
Curtis D. Diltz, E G Krebs, Nicholas K. Tonks, Natalie G. Ahn, Rony Seger, Rebecca L. Bratlien
Publikováno v:
Journal of Biological Chemistry. 266:4220-4227
Epidermal growth factor stimulates the activity of several cytosolic serine/threonine protein kinases in quiescent Swiss 3T3 cells. Two of these, which use myelin basic protein (MBP) as substrate, act as kinase kinases in that they are able to activa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6112e86f210e5c44abe06bb9b8b7dc1
https://doi.org/10.1016/s0021-9258(20)64310-1
https://doi.org/10.1016/s0021-9258(20)64310-1
Publikováno v:
Journal of Biological Chemistry. 265:10674-10680
Although CD45 resembles the low Mr protein tyrosine phosphatases (PTPases) from human placenta in its specificity for phosphotyrosyl residues and absolute dependence on sulfhydryl compounds for activity, it also exhibits a number of distinguishing fe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c45e4df354a8d9a1cb498c2231540e7d
https://doi.org/10.1016/s0021-9258(18)86999-x
https://doi.org/10.1016/s0021-9258(18)86999-x
Publikováno v:
Molecular and Cellular Biology. 10:458-463
Homogeneous preparations of a protein phosphatase that is specific for phosphotyrosyl residues (protein tyrosine phosphatase [PTPase] 1B) were isolated from human placenta and microinjected into Xenopus oocytes. This resulted in an increase in activi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07edba9ac174185b806fc035f0af1461
https://doi.org/10.1128/mcb.10.2.458-463.1990
https://doi.org/10.1128/mcb.10.2.458-463.1990
The mitogen-activated protein kinases (MAPKs) are integral to the mechanisms by which cells respond to physiological stimuli, such as growth factors, hormones, and cytokines, and to a wide variety of environmental stresses. The MAPKs, which are stimu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf06dba2138030616681912c4ed2045e
https://europepmc.org/articles/PMC61089/
https://europepmc.org/articles/PMC61089/
Publikováno v:
The Journal of biological chemistry. 271(36)
Rapid tyrosine phosphorylation of key cellular proteins is a crucial event in signal transduction. The regulatory role of protein-tyrosine phosphatases (PTPs) in this process was explored by studying the effects of a powerful PTP inhibitor, pervanada
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80ad2b6643850f5ec25fbfb4d5e5bd3d
https://pubmed.ncbi.nlm.nih.gov/8703041
https://pubmed.ncbi.nlm.nih.gov/8703041
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 92(19)
Using indirect immunofluorescence microscopy and biochemical techniques, we have determined that approximately one-third of the total mitogen-activated protein kinase (MAPK) is associated with the microtubule cytoskeleton in NIH 3T3 mouse fibroblasts
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9793d9f95d067ff0aa4892f63a5bc5a9
https://pubmed.ncbi.nlm.nih.gov/7568036
https://pubmed.ncbi.nlm.nih.gov/7568036
Autor:
Zhongjia Tan, Jocelyn H. Wright, Edmond H. Fischer, Shi-Hsiang Shen, Edwin G. Krebs, Zhizhuang Zhao, Curtis D. Diltz
Publikováno v:
The Journal of biological chemistry. 270(20)
PTP2C, an SH2 domain-containing protein-tyrosine phosphatase, is recruited to the growth factor receptors upon stimulation of cells. To investigate its role in growth factor signaling, we have overexpressed by approximately 6-fold the native PTP2C an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::238023cca6c35f4ca5df2ac3cb66591e
https://pubmed.ncbi.nlm.nih.gov/7744825
https://pubmed.ncbi.nlm.nih.gov/7744825