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Diabetes|May 30, 1998
MODY1 mutation Q268X in hepatocyte nuclear factor 4alpha allows for dimerization in solution but causes abnormal subcellular localizationF M Sladek, Q Dallas-Yang, L NepomucenoJournal of Molecular Biology|September 20, 2000
Analysis of protein dimerization and ligand binding of orphan receptor HNF4alphaA A Bogan, Q Dallas-Yang, M D Ruse, et al.Archives of Biochemistry and Biophysics|April 1, 1997
Serine/threonine phosphorylation of orphan receptor hepatocyte nuclear factor 4G Jiang, L Nepomuceno, Q Yang, et al.Molecular and Cellular Biology|September 1, 1995
Exclusive homodimerization of the orphan receptor hepatocyte nuclear factor 4 defines a new subclass of nuclear receptorsG Jiang, L Nepomuceno, K Hopkins, et al.Molecular and Cellular Biology|September 22, 1999
Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor hepatocyte nuclear factor 4alpha1F M Sladek, M D Ruse, L Nepomuceno, et al.The Journal of Biological Chemistry|January 10, 1997
The DNA binding domain of hepatocyte nuclear factor 4 mediates cooperative, specific binding to DNA and heterodimerization with the retinoid X receptor alphaG Jiang, F M SladekCurrent Opinion in Genetics & Development|April 1, 1992
Mechanisms of liver-specific gene expressionF M Sladek, J E DarnellMolecular and Cellular Biology|October 29, 1997
Proposed mechanism for the stabilization of nuclear receptor DNA binding via protein dimerizationG Jiang, U Lee, F M SladekProceedings of the National Academy of Sciences of the United States of America|June 1, 1989
Incision by UvrABC excinuclease is a step in the path to mutagenesis by psoralen crosslinks in Escherichia coliF M Sladek, A Melian, P Howard-FlandersPageof 8