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Matches in Nanopublications for { ?s ?p "Because MYC proteins function primarily as transcription factors, the consequences of these alterations result in the deregulation of MYC target genes and subsequent effects on cell behavior and in the inability to down-regulate MYC expression to levels sufficiently low for a cell to exit the cell cycle and enter a quiescent state or to differentiate in response to appropriate signals. MYC is a member of the MYC/MAX/MAD network of the basic region/helix-loop-helix/leucine zipper (bHLHZ) domain transcriptional regulators (for a summary of the domain structure see Fig. 1). MYC proteins form obligatory heterodimers with MAX, and these complexes bind to specific E-box DNA sequences with the consensus 5beta-CACGTG (7). The transactivation domain (TAD) is localized at theNterminus, containing two highly conserved elements, Myc box (MB) I and II, that are particularly relevant for MYC regulation and cofactor recruitment, respectively (Fig. 1). Within the MYC/MAX/MAD network, MYC proteins are antagonized by several bHLHZ proteins collectively referred to as MAD proteins (for an overview of the network see Fig. S2A) (8)." ?g. }

• _7 value "Because MYC proteins function primarily as transcription factors, the consequences of these alterations result in the deregulation of MYC target genes and subsequent effects on cell behavior and in the inability to down-regulate MYC expression to levels sufficiently low for a cell to exit the cell cycle and enter a quiescent state or to differentiate in response to appropriate signals. MYC is a member of the MYC/MAX/MAD network of the basic region/helix-loop-helix/leucine zipper (bHLHZ) domain transcriptional regulators (for a summary of the domain structure see Fig. 1). MYC proteins form obligatory heterodimers with MAX, and these complexes bind to specific E-box DNA sequences with the consensus 5beta-CACGTG (7). The transactivation domain (TAD) is localized at theNterminus, containing two highly conserved elements, Myc box (MB) I and II, that are particularly relevant for MYC regulation and cofactor recruitment, respectively (Fig. 1). Within the MYC/MAX/MAD network, MYC proteins are antagonized by several bHLHZ proteins collectively referred to as MAD proteins (for an overview of the network see Fig. S2A) (8)." provenance.
• _7 value "Because MYC proteins function primarily as transcription factors, the consequences of these alterations result in the deregulation of MYC target genes and subsequent effects on cell behavior and in the inability to down-regulate MYC expression to levels sufficiently low for a cell to exit the cell cycle and enter a quiescent state or to differentiate in response to appropriate signals. MYC is a member of the MYC/MAX/MAD network of the basic region/helix-loop-helix/leucine zipper (bHLHZ) domain transcriptional regulators (for a summary of the domain structure see Fig. 1). MYC proteins form obligatory heterodimers with MAX, and these complexes bind to specific E-box DNA sequences with the consensus 5beta-CACGTG (7). The transactivation domain (TAD) is localized at theNterminus, containing two highly conserved elements, Myc box (MB) I and II, that are particularly relevant for MYC regulation and cofactor recruitment, respectively (Fig. 1). Within the MYC/MAX/MAD network, MYC proteins are antagonized by several bHLHZ proteins collectively referred to as MAD proteins (for an overview of the network see Fig. S2A) (8)." provenance.
• _7 value "Because MYC proteins function primarily as transcription factors, the consequences of these alterations result in the deregulation of MYC target genes and subsequent effects on cell behavior and in the inability to down-regulate MYC expression to levels sufficiently low for a cell to exit the cell cycle and enter a quiescent state or to differentiate in response to appropriate signals. MYC is a member of the MYC/MAX/MAD network of the basic region/helix-loop-helix/leucine zipper (bHLHZ) domain transcriptional regulators (for a summary of the domain structure see Fig. 1). MYC proteins form obligatory heterodimers with MAX, and these complexes bind to specific E-box DNA sequences with the consensus 5beta-CACGTG (7). The transactivation domain (TAD) is localized at theNterminus, containing two highly conserved elements, Myc box (MB) I and II, that are particularly relevant for MYC regulation and cofactor recruitment, respectively (Fig. 1). Within the MYC/MAX/MAD network, MYC proteins are antagonized by several bHLHZ proteins collectively referred to as MAD proteins (for an overview of the network see Fig. S2A) (8)." provenance.
• _7 value "Because MYC proteins function primarily as transcription factors, the consequences of these alterations result in the deregulation of MYC target genes and subsequent effects on cell behavior and in the inability to down-regulate MYC expression to levels sufficiently low for a cell to exit the cell cycle and enter a quiescent state or to differentiate in response to appropriate signals. MYC is a member of the MYC/MAX/MAD network of the basic region/helix-loop-helix/leucine zipper (bHLHZ) domain transcriptional regulators (for a summary of the domain structure see Fig. 1). MYC proteins form obligatory heterodimers with MAX, and these complexes bind to specific E-box DNA sequences with the consensus 5beta-CACGTG (7). The transactivation domain (TAD) is localized at theNterminus, containing two highly conserved elements, Myc box (MB) I and II, that are particularly relevant for MYC regulation and cofactor recruitment, respectively (Fig. 1). Within the MYC/MAX/MAD network, MYC proteins are antagonized by several bHLHZ proteins collectively referred to as MAD proteins (for an overview of the network see Fig. S2A) (8)." provenance.