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• W2041639550 abstract "The biochemical analysis of cellular trans-activators involved in promoter recognition provides an important step toward understanding the mechanisms of gene expression in animal cells. The promoter selective transcription factor, Sp1, has been purified from human cells to more than 95 percent homogeneity by sequence-specific DNA affinity chromatography. Isolation and renaturation of proteins purified from sodium dodecyl sulfate polyacrylamide gels allowed the identification of two polypeptides (105 and 95 kilodaltons) as those responsible for recognizing and interacting specifically with the GC-box promoter elements characteristic of Sp1 binding sites." @default.
• W2041639550 created "2016-06-24" @default.
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• W2041639550 date "1986-10-03" @default.
• W2041639550 modified "2023-10-17" @default.
• W2041639550 title "Purification and Biochemical Characterization of the Promoter-Specific Transcription Factor, Sp1" @default.
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• W2041639550 doi "https://doi.org/10.1126/science.3529394" @default.
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