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Cited by 225

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression.

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Seth, A., Alvarez, E., Gupta, S., Davis, R.J.·1991·Journal of Biological Chemistry

Abstract

The c-myc gene encodes a sequence-specific DNA-binding protein (c-Myc) that forms leucine zipper complexes and can act as a transcription factor. Growth factor stimulation of cells causes the phosphorylation of the c-Myc transcriptional activation domain at Ser62 within a proline-rich region that is highly conserved among members of the Myc family (Alvarez, E., Northwood, I.C., Gonzalez, F. A., Latour, D. A., Seth, A., Abate, C., Curran, T., and Davis, R. J. (1991) J. Biol. Chem. 266, 15277-15285). This phosphorylation site is a substrate for growth factor-regulated MAP kinases and for the cell cycle-dependent protein kinase p34cdc2. We report that serum treatment of cells results in a marked increase in the transactivation of gene expression mediated by the c-Myc transcriptional activation domain. A point mutation at the site of growth factor-stimulated phosphorylation (Ser62) decreases the serum induction of transactivation. These data indicate that the c-Myc transcriptional activation domain may be a direct target of signal transduction pathways.

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Metadata

Authors
Seth, A., Alvarez, E., Gupta, S., & Davis, R. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1991-12
Volume
266
Issue
35
Pages
23521-23524
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2140566131
Cited by
225
References
1
FWCI
9.89
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression. https://app.cochat.ai/papers/10.1016/s0021-9258(18)54312-x
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Seth, A., Alvarez, E., Gupta, S., & Davis, R. J. (1991). A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)54312-x

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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