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- W2893838959 abstract "Basic leucine zipper (bZIP) proteins reside at the end of cell-signaling cascades and function to modulate transcription of specific gene targets. bZIPs are recognized as important regulators of cellular processes such as cell growth, apoptosis, and cell differentiation. One such validated transcriptional regulator, activator protein-1, is typically comprised of heterodimers of Jun and Fos family members and is key in the progression and development of a number of different diseases. The best described component, cJun, is upregulated in a variety of diseases such as cancer, osteoporosis, and psoriasis. Toward our goal of inhibiting bZIP proteins implicated in disease pathways, we here describe the first use of a novel in silico peptide library screening platform that facilitates the derivation of sequences exhibiting a high affinity for cJun while disfavoring homodimer formation or formation of heterodimers with other closely related Fos sequences. In particular, using Fos as a template, we have computati..." @default.
- W2893838959 created "2018-10-05" @default.
- W2893838959 creator A5004541105 @default.
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- W2893838959 date "2018-09-26" @default.
- W2893838959 modified "2023-10-13" @default.
- W2893838959 title "Computational Competitive and Negative Design To Derive a Specific cJun Antagonist" @default.
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- W2893838959 doi "https://doi.org/10.1021/acs.biochem.8b00782" @default.
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