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Robert H. Costa

Researcher at University of Illinois at Chicago

Publications -  121
Citations -  13096

Robert H. Costa is an academic researcher from University of Illinois at Chicago. The author has contributed to research in topics: Transcription factor & Hepatocyte nuclear factors. The author has an hindex of 67, co-authored 121 publications receiving 12502 citations. Previous affiliations of Robert H. Costa include Baylor College of Medicine & Rockefeller University.

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Forkhead Box M1 Regulates the Transcriptional Network of Genes Essential for Mitotic Progression and Genes Encoding the SCF (Skp2-Cks1) Ubiquitin Ligase

TL;DR: FoxM1 regulates transcription of cell cycle genes critical for progression into S-phase and mitosis, and is essential for transcription of the mitotic regulatory genes Cdc25B, Aurora B kinase, survivin, centromere protein A, and CENPB.
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Multiple hepatocyte-enriched nuclear factors function in the regulation of transthyretin and alpha 1-antitrypsin genes.

TL;DR: A detailed analysis of the proximal regulatory region of the TTR gene is reported, which has uncovered two new DNA-binding factors that are present mainly (or only) in hepatocytes and binds to two sites that are crucial in TTR expression as well as to two additional sites in the alpha 1-AT proximal enhancer region.
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Transcription factors in liver development, differentiation, and regeneration.

TL;DR: The HNF1 , HNF4 , Foxa2, and Foxa3 tran-scription factors regulate expression of genes critical forhepatocyte differentiation during embryonic and postna-talliver development.
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Foxm1b transcription factor is essential for development of hepatocellular carcinomas and is negatively regulated by the p19ARF tumor suppressor

TL;DR: It is demonstrated that conditional overexpression of Foxm1b protein in osteosarcoma U2OS cells greatly enhances anchorage-independent growth of cell colonies on soft agar and suggests that this (D-Arg)(9)-p19(ARF) 26-44 peptide is a potential therapeutic inhibitor of Fox m1b function during cellular transformation.
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The DNA-binding specificity of the hepatocyte nuclear factor 3/forkhead domain is influenced by amino-acid residues adjacent to the recognition helix.

TL;DR: It is shown that these HNF-3/fkh proteins bind to distinct DNA sites and that the specificity of protein recognition is dependent on subtle nucleotide alterations in the site, and a model is proposed in which this 20-amino-acid flanking region influences the DNA-binding properties of the recognition helix.