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Csnk2a1 phosphorylates MAX. 6 / 6
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"Similar to ARNT and Alt ARNT (1-358), ARNT and Alt ARNT (1-102) are differentially phosphorylated, predominantly at Ser77.The data of Figs. 3 A and B show that Ser77 is a phosphorylation site in the a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"DNA Binding of the Mad-Max Heterodimer Is Not Affected by CKII Phosphorylation Max is phosphorylated by CKII in vivo and in vitro, and recent work has shown that this phosphorylation blocks Max homadi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"However, the CM-1 binding activity of the GST, Mad, and Max complex was not affected by CKII phosphorylation of Max."
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"Previous work has demonstrated that Max is phosphorylated in vivo and in vitro by CKII (Blackwood et al., 1992a; Berberich and Cole, 1992)."
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"In contrast, phosphorylation of Max and/or Myc by CKII had no inhibitory or stimulatory effect on the DNA binding activity of Myc and Max heterodimers."
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"For instance, CK II phosphorylates c-Myb, c-Jun and Max proteins, among others, and inhibits their sequence specific DNA binding [7,8]."
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