Transcription activation by Myc and Max: flanking sequences target activation to a subset of CACGTG motifs in vivo.

No abstract is available for this paper.

• Publication year

  1993

• Venue

  EMBO Journal

• Publication date

  1993-12-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1002/j.1460-2075.1993.tb06201.xPMID 8262050PMCID PMC413768
• 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.

• Sequence-specific transcriptional activation by Myc and repression by Max

  1993cited by this paper
• Opposite regulation of gene transcription and cell proliferation by c-Myc and Max.

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• Oncogenic activity of the c-Myc protein requires dimerization with Max.

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  1993cited by this paper
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• Single amino acid substitutions alter helix‐loop‐helix protein specificity for bases flanking the core CANNTG motif.

  1992cited by this paper
• Myc family oncoproteins function through a common pathway to transform normal cells in culture: cross-interference by Max and trans-acting dominant mutants.

  1992cited by this paper
• Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers.

  1992cited by this paper
• Mutational analysis of Max: role of basic, helix-loop-helix/leucine zipper domains in DNA binding, dimerization and regulation of Myc-mediated transcriptional activation.

  1992cited by this paper
• Max: functional domains and interaction with c-Myc.

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• Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis.

  1992cited by this paper
• Myc and Max associate in vivo.

  1992cited by this paper
• Max and c-Myc/Max DNA-binding activities in cell extracts.

  1992cited by this paper
• Biphasic effect of Max on Myc cotransformation activity and dependence on amino- and carboxy-terminal Max functions.

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• Myc and Max proteins possess distinct transcriptional activities

  1992cited by this paper
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  1992cited by this paper
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• Immunocytochemical localization of casein kinase II during interphase and mitosis

  1991cited by this paper
• Casein kinase II induces c‐fos expression via the serum response element pathway and p67SRF phosphorylation in living fibroblasts.

  1991cited by this paper
• Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc.

  1991cited by this paper
• Determination of the c-MYC DNA-binding site.

  1991cited by this paper
• TFEB has DNA-binding and oligomerization properties of a unique helix-loop-helix/leucine-zipper family.

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• Methylation-sensitive sequence-specific DNA binding by the c-Myc basic region.

  1991cited by this paper
• Sequence-specific DNA binding by Myc proteins.

  1991cited by this paper
• C-myc and the yeast transcription factor PHO4 share a common CACGTG-binding motif.

  1991cited by this paper
• Association of Myn, the murine homolog of max, with c-Myc stimulates methylation-sensitive DNA binding and ras cotransformation.

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• Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy.

  1990cited by this paper
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