Výsledky vyhledávání - "Erlynda Munar"

Expression of the Casein Kinase 2 Subunits in Chinese Hamster Ovary and 3T3 L1 Cells Provides Information on the Role of the Enzyme in Cell Proliferation and the Cell Cycle

Autor: Erlynda Munar, Peter Drueckes, Lauri D. Aicher, Elizabeth L. Dunphy, Dongxia Li, Mingzi Chen, Grażyna Dobrowolska, Jocelyn H. Wright, Edwin G. Krebs

Publikováno v: Journal of Biological Chemistry. 274:32988-32996

In order to investigate the in vivo functions of protein kinase CK2 (CK2), the expression of Myc-tagged versions of the subunits, Myc-CK2alpha and Myc-CK2beta, was carried out in Chinese hamster ovary cells (CHO cells) and in 3T3 L1 fibroblasts. Cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::366632dbd2d59f5152bc541abdce7490
https://doi.org/10.1074/jbc.274.46.32988

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Mitogen-activated protein kinase kinase activity is required for the G 2 /M transition of the cell cycle in mammalian fibroblasts

Autor: Erlynda Munar, Rony Seger, Damon R. Jameson, Robert L. Margolis, Edwin G. Krebs, Paul R. Andreassen, Jocelyn H. Wright

Publikováno v: Proceedings of the National Academy of Sciences. 96:11335-11340

The mitogen-activated protein kinase (MAPK) cascade is required for mitogenesis in somatic mammalian cells and is activated by a wide variety of oncogenic stimuli. Specific roles for this signaling module in growth were dissected by inhibiting MAPK k

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a706cde3cfcfd3da018fc6d8db8f74cc
https://doi.org/10.1073/pnas.96.20.11335

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Overexpression of mitogen-activated protein kinase kinase (MAPKK) and its mutants in NIH 3T3 cells. Evidence that MAPKK involvement in cellular proliferation is regulated by phosphorylation of serine residues in its kinase subdomains VII and VIII

Autor: Grażyna Dobrowolska, Jean S. Campbell, Edmond H. Fischer, Rony Seger, E G Krebs, Dalia Seger, Hagit Eldar-Finkelman, Erlynda Munar, Amy M. Jensen, Alfred A. Reszka

Publikováno v: Journal of Biological Chemistry. 269:25699-25709

Mitogen-activated protein kinase kinase (MAPKK) is a dual specificity protein kinase that exhibits a high degree of specificity toward its downstream target, mitogen-activated protein kinase (MAPK). In this study, we used stable overexpression of MAP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c3fd53137ccb9d2b058dacff20011c27
https://doi.org/10.1016/s0021-9258(18)47305-x

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Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells

Autor: Natalie G. Ahn, Melanie H. Cobb, Jonathan A. Cooper, James Posada, Amy M. Jensen, Erlynda Munar, Rony Seger, Edwin G. Krebs

Publikováno v: Journal of Biological Chemistry. 267:14373-14381

Two peaks of mitogen-activated protein (MAP) kinase activator activity are resolved upon ion exchange chromatography of cytosolic extracts from epidermal growth factor-stimulated A431 cells. Two forms of the activator (1 and 2) have been purified fro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a6c4355f87d7f5c91fa8d0ec4cc10eee
https://doi.org/10.1016/s0021-9258(19)49722-6

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Inhibition of cellular differentiation by phospholipase C

Autor: Erlynda Munar, Mark Nameroff

Publikováno v: Developmental Biology. 49:288-293

Myogenic cells cultured in concentrations of phospholipase C which inhibit fusion still recognize each other. Recognition is accompanied by withdrawal from the cell cycle. We conclude that recognition and fusion are two distinct and separable process

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a252b98522654638822fa7327a0d6146
https://doi.org/10.1016/0012-1606(76)90275-x

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INHIBITION OF CELLULAR DIFFERENTIATION BY PHOSPHOLIPASE C

Autor: John M. Keller, Erlynda Munar, John A. Trotter, Mark Nameroff

Publikováno v: Journal of Cell Biology. 58:107-118

In cell culture, a partially purified commercial preparation of phospholipase C (PLC) from Clostridium welchii inhibited fusion of myoblasts at concentrations of 12–50 µg per ml. At lower concentrations, PLC-treated cultures were indistinguishable

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7efd4d1cc6b82633637517500b9a9f59
https://doi.org/10.1083/jcb.58.1.107

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