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Oscience. Trends Neurosci. 1999;22(4):167-173. PubMed Silverman ES, Collins T. Pathways of Egr-1-mediated gene transcription in vascular biology. Am J Pathol. 1999;154(3):665-70. doi:10.1016/S00029440(10)65312-6. PubMed PMID: 10079243; PMCID: PMC1866415. Thiel G, Cibelli G. Regulation of life and death by the zinc finger transcription factor Egr-1. J Cell Physiol. 2002;193(3):287-292. doi:10.1002/
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Ns [102, 106]. In contrast, IDPs are charged proteins, thus they can control their interfacial absorption onto solid surfaces [106]. Experiments, in silico, suggest that intrinsically disordered peptides absorbed to a surface with a complementary pattern form a well-defined structure (-helix) indicating that a specific surface can stabilize the structure of an IDP peptide. The effect of a compleme
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Riments performed in duplicate and normalized to the amplification of ACTB mRNA. Bars represent mean ?SEM of the fold change with respect to untreated. *p < 0.05 (significantly different from control treated cells using student's t-test). (PDF 491 kb) Additional file 3: Figure S3 The effect of ERK1/2 inhibition on EGR2 expression in human and mouse mammary epithelial cells deficient in SFRP1 expre
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Riments performed in duplicate and normalized to the amplification of ACTB mRNA. Bars represent mean ?SEM of the fold change with respect to untreated. *p < 0.05 (significantly different from control treated cells using student's t-test). (PDF 491 kb) Additional file 3: Figure S3 The effect of ERK1/2 inhibition on EGR2 expression in human and mouse mammary epithelial cells deficient in SFRP1 expre
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Poprotein; SFRP1: Secreted frizzled-related protein-1; TAM: Tumor Associated Macrophage; TGF-: Transforming growth factor- Acknowledgements Not applicable.5.6.7. Funding The design of this study, collection, analysis, interpretation, and writing of the manuscript were made possible because of the funding support by the Rays of Hope Foundation. Availability of data and materials The raw files are n
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F the IDP domain containing an asparagine and proline (Asn- and Pro)-rich region, with glycine (Gly)- and glutamine (Gln)-rich repeats mid-sequence is implicated in self- assembly. Based on analytical ultracentrifugation, the glycine-rich region oligomerizes to form large protein assemblies. The proline-rich region also shows a self-Author Manuscript Author Manuscript Author Manuscript Author Manu
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