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<dc:title>Regulation of cancer progression by hepatitis B virus X protein (HBx) and HBxAP/RSF1</dc:title>
<dc:title>B형 간염 바이러스 단백질인 HBx와 HBxAP/RSF1에 의한 암화과정 조절</dc:title>
<dc:creator>조, 미영</dc:creator>
<dc:contributor>조, 혜성</dc:contributor>
<dc:contributor>대학원 의생명과학과</dc:contributor>
<dc:contributor>110686</dc:contributor>
<dc:contributor>조, 미영</dc:contributor>
<dc:subject>Hepatitis B virus X (HBx)</dc:subject>
<dc:subject>catalase</dc:subject>
<dc:subject>cysteine</dc:subject>
<dc:subject>liver cancer</dc:subject>
<dc:subject>HBxAP/RSF1</dc:subject>
<dc:description>I. Regulation of catalase on hepatitis B virus X protein (HBx) in HBV-related advanced hepatocellular carcinomas 1 &#xd;
&#xd;
 A. INTRODUCTION 2 &#xd;
&#xd;
 B. MATERIALS AND METHODS. 4 &#xd;
&#xd;
  1. Cell cultures and plasmids 4 &#xd;
&#xd;
  2. RNA extraction, reverse transcription-polymerase chain reaction 4 &#xd;
&#xd;
  3. Western blotting . 5 &#xd;
&#xd;
  4. Luciferase assay 5 &#xd;
&#xd;
  5. Clonogenic cell proliferation assays 5 &#xd;
&#xd;
  6. Patients characteristics 6 &#xd;
&#xd;
  7. Statistics 6 &#xd;
&#xd;
 C. RESULTS 7 &#xd;
&#xd;
  1. The protein levels of HBx are decreased by catalase and MnSOD 7 &#xd;
&#xd;
  2. Catalase downregulates HBx protein levels at the translational level 7 &#xd;
&#xd;
  3. Cysteine residues of HBx are essential to maintain protein stability . 9 &#xd;
&#xd;
  4. Cysteine null mutant of HBx is insufficient for transactivation activities 12 &#xd;
&#xd;
  5. Cysteine null mutant is not affected by catalase or N-acetyl cysteine 12 &#xd;
&#xd;
  6. Cysteine residues are important for HBx-mediated clonogenic cell proliferation 14 &#xd;
&#xd;
  7. Catalase expression level is lower in tumor tissues than in non-tumor tissues in HBV-related HCC. 17 &#xd;
&#xd;
  8. Catalase expression level is significantly lower in HBV-related advanced HCC 17 &#xd;
&#xd;
  9. HBx protein levels are negatively correlated with catalase expression in HBV-related advanced HCC. 20 &#xd;
&#xd;
  10. HBx protein levels have no correlation with MnSOD expression in HBV-related advanced HCC 23 &#xd;
&#xd;
  11. Prognostic significance of catalase expression in HBV-related advanced HCC 23 &#xd;
&#xd;
 D. DISCUSSION 30 &#xd;
&#xd;
II. HBxAP/RSF1 as a chromatin remodeller and HBx-associated protein 32 &#xd;
&#xd;
 A. INTRODUCTION 33 &#xd;
&#xd;
 B. MATERIALS AND METHODS . 36 &#xd;
&#xd;
  1. Cell cultures and antibody. 36 &#xd;
&#xd;
  2. Plasmid. 36 &#xd;
&#xd;
  3. Chromosome spreading and Giemsa staining. 36 &#xd;
&#xd;
  4. FRET (Fluorescence Resonance Energy Transfer) assay. 37 &#xd;
&#xd;
  5. Modified histone peptide array. 37 &#xd;
&#xd;
  6. Purification of RSF1. 37 &#xd;
&#xd;
  7. Protein microchip array. . 37 &#xd;
&#xd;
 C. RESULTS 39 &#xd;
&#xd;
  1. RSF1 is overexpressed in HBV-related advanced HCC. 39 &#xd;
&#xd;
  2. RSF1 depletion induces premature separation of sister chromatids. 39 &#xd;
&#xd;
  3. The centromeric expression level of H3K9me3 is downregulated at metaphase in RSF1 knock-down cells 43 &#xd;
&#xd;
  4. RSF1 depletion enhances the expression levels of H3K9me3 and H3K27me3 in mitosis 46 &#xd;
&#xd;
  5. RSF1 dissociates from histone peptides with phosphorylated H3S28 modification 46 &#xd;
&#xd;
  6. RSF1 directly interacts with diverse targets. 48 &#xd;
&#xd;
 D. DISCUSSION 51 &#xd;
&#xd;
III. CONCLUSION 53 &#xd;
&#xd;
IV. REFFERENCE 54 &#xd;
&#xd;
국문요약 59</dc:description>
<dc:description>Doctor</dc:description>
<dc:date>2016-11-25T09:58:15Z</dc:date>
<dc:date>2016-11-25T09:58:15Z</dc:date>
<dc:date>2016</dc:date>
<dc:date>2016</dc:date>
<dc:type>Thesis</dc:type>
<dc:type>Theses</dc:type>
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<dc:language>en</dc:language>
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