Young In Chi

Summary

Affiliation: University of Kentucky
Country: USA

Publications

  1. pmc Homeodomain revisited: a lesson from disease-causing mutations
    Young In Chi
    Department of Molecular and Cellular Biochemistry, Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA
    Hum Genet 116:433-44. 2005
  2. pmc Capturing hammerhead ribozyme structures in action by modulating general base catalysis
    Young In Chi
    Department of Molecular and Cellular Biochemistry, Center for Structural Biology, University of Kentucky, Lexington, Kentucky, United States of America
    PLoS Biol 6:e234. 2008
  3. pmc Structural basis of natural promoter recognition by a unique nuclear receptor, HNF4alpha. Diabetes gene product
    Peng Lu
    Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536, USA
    J Biol Chem 283:33685-97. 2008
  4. pmc Multiple binding modes between HNF4alpha and the LXXLL motifs of PGC-1alpha lead to full activation
    Geun Bae Rha
    Department of Molecular and Cellular Biochemistry, Center for Structural Biology, University of Kentucky, Lexington, Kentucky 40536, USA
    J Biol Chem 284:35165-76. 2009
  5. ncbi request reprint Structure of the globular tail of nuclear lamin
    Sirano Dhe-Paganon
    Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215, USA
    J Biol Chem 277:17381-4. 2002
  6. ncbi request reprint Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand
    Sirano Dhe-Paganon
    Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215, USA
    J Biol Chem 277:37973-6. 2002
  7. ncbi request reprint Diabetes mutations delineate an atypical POU domain in HNF-1alpha
    Young In Chi
    Joslin Diabetes Center, Department of Medicine, Harvard Medical School, Boston, MA 02215, USA
    Mol Cell 10:1129-37. 2002
  8. ncbi request reprint Structural basis for HNF-4alpha activation by ligand and coactivator binding
    Karen Duda
    Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, Massachussets 02215, USA
    J Biol Chem 279:23311-6. 2004

Collaborators

Detail Information

Publications8

  1. pmc Homeodomain revisited: a lesson from disease-causing mutations
    Young In Chi
    Department of Molecular and Cellular Biochemistry, Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA
    Hum Genet 116:433-44. 2005
    ..These findings should be useful in understanding the essential components of the homeodomain and in attempts to design agonist or antagonists to modulate their activity and to reverse the effects caused by the mutations...
  2. pmc Capturing hammerhead ribozyme structures in action by modulating general base catalysis
    Young In Chi
    Department of Molecular and Cellular Biochemistry, Center for Structural Biology, University of Kentucky, Lexington, Kentucky, United States of America
    PLoS Biol 6:e234. 2008
    ..The predissociation enzyme-product complex structure reveals RNA and metal ion interactions potentially relevant to transition-state stabilization that are absent in precatalytic structures...
  3. pmc Structural basis of natural promoter recognition by a unique nuclear receptor, HNF4alpha. Diabetes gene product
    Peng Lu
    Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536, USA
    J Biol Chem 283:33685-97. 2008
    ....
  4. pmc Multiple binding modes between HNF4alpha and the LXXLL motifs of PGC-1alpha lead to full activation
    Geun Bae Rha
    Department of Molecular and Cellular Biochemistry, Center for Structural Biology, University of Kentucky, Lexington, Kentucky 40536, USA
    J Biol Chem 284:35165-76. 2009
    ....
  5. ncbi request reprint Structure of the globular tail of nuclear lamin
    Sirano Dhe-Paganon
    Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215, USA
    J Biol Chem 277:17381-4. 2002
    ..These findings distinguish myopathy- and lipodystrophy-associated mutations and provide a structural framework for further testing hypotheses concerning lamin function...
  6. ncbi request reprint Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand
    Sirano Dhe-Paganon
    Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215, USA
    J Biol Chem 277:37973-6. 2002
    ..These findings suggest that fatty acids are endogenous ligands for HNF4 alpha and establish a framework for understanding how HNF4 alpha activity is enhanced by ligand binding and diminished by MODY1 mutations...
  7. ncbi request reprint Diabetes mutations delineate an atypical POU domain in HNF-1alpha
    Young In Chi
    Joslin Diabetes Center, Department of Medicine, Harvard Medical School, Boston, MA 02215, USA
    Mol Cell 10:1129-37. 2002
    ..The numerous diabetes-causing mutations in HNF-1alpha thus identified a previously unrecognized POU domain which was used as a search model to identify additional POU domain proteins in sequence databases...
  8. ncbi request reprint Structural basis for HNF-4alpha activation by ligand and coactivator binding
    Karen Duda
    Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, Massachussets 02215, USA
    J Biol Chem 279:23311-6. 2004
    ..We conclude that for HNF-4alpha, coactivator rather than ligand binding locks the active conformation...