Reconstitution of the Raf-1—MEK—ERK Signal Transduction Pathway In Vitro

No abstract is available for this paper.

• Publication year

  1993

• Venue

  Molecular and Cellular Biology

• Publication date

  1993-11-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1128/MCB.13.11.6615PMID 8413257PMCID PMC364724
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf

  1993cited by this paper
• Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro

  1993cited by this paper
• Protein kinase Cα activates RAF-1 by direct phosphorylation

  1993cited by this paper
• Characterization of full‐length neurofibromin: tubulin inhibits Ras GAP activity.

  1993cited by this paper
• Protein kinase C alpha activates RAF-1 by direct phosphorylation.

  1993cited by this paper
• A protein kinase similar to MAP kinase activator acts downstream of the raf kinase in Drosophila.

  1993cited by this paper
• Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

  1993cited by this paper
• Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase.

  1993cited by this paper
• Raf-1 and p21v-ras cooperate in the activation of mitogen-activated protein kinase.

  1993cited by this paper
• Activation of the c-Raf protein kinase by protein kinase C phosphorylation.

  1992cited by this paper
• The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product.

  1992cited by this paper
• Evidence that extracellular signal-regulated kinases are the insulin-activated Raf-1 kinase kinases.

  1992cited by this paper
• Raf functions downstream of Rasl in the Sevenless signal transduction pathway

  1992cited by this paper
• Raf-1 activates MAP kinase-kinase

  1992influential reference
• Activation of extracellular signal‐regulated kinase, ERK2, by p21ras oncoprotein.

  1992cited by this paper
• Activation of the MAP kinase pathway by the protein kinase raf.

  1992influential reference
• ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK.

  1992cited by this paper
• Ras is essential for nerve growth factor- and phorbol ester-induced tyrosine phosphorylation of MAP kinases.

  1992cited by this paper
• Both p21ras and pp60v-src are required, but neither alone is sufficient, to activate the Raf-1 kinase.

  1992cited by this paper
• Raf-1 protein kinase is an integral component of the oncogenic signal cascade shared by epidermal growth factor and platelet-derived growth factor

  1992cited by this paper
• Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro.

  1992influential reference
• Erythropoietin induces Raf-1 activation and Raf-1 is required for erythropoietin-mediated proliferation.

  1991cited by this paper
• Epidermal growth factor stimulates phosphorylation of RAF-1 independently of receptor autophosphorylation and internalization.

  1991cited by this paper
• Epidermal growth factor (EGF) stimulates association and kinase activity of Raf-1 with the EGF receptor.

  1991cited by this paper
• Raf-1 is a potential substrate for mitogen-activated protein kinase in vivo.

  1991cited by this paper
• Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine.

  1991cited by this paper
• Insulin and platelet-derived growth factor stimulate phosphorylation of the c-raf product at serine and threonine residues in intact cells.

  1991cited by this paper
• Differential regulation of the p72-74 RAF-1 kinase in 3T3 fibroblasts expressing ras or src oncogenes.

  1991cited by this paper
• Raf-1 protein kinase is required for growth of induced NIH/3T3 cells

  1991cited by this paper
• Insulin activates the kinase activity of the Raf-1 proto-oncogene by increasing its serine phosphorylation.

  1990cited by this paper
• Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor.

  1989cited by this paper
• Requirement of the Drosophila raf homologue for torso function

  1989cited by this paper
• Signal transduction from membrane to cytoplasm: growth factors and membrane-bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity.

  1988cited by this paper

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