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| <div class="title">References</div> | | <div class="title">References</div> |
| <div class="text"> | | <div class="text"> |
− | <b>Introduction</b> | + | <ul> |
− | <ol>
| + | <li><b>Introduction</b></li> |
− | <li>Taiwan National Infectious Disease Statistics System - Taiwan Centers of Disease Control (TCDC), https://reurl.cc/EzLvE1</li>
| + | <ol> |
− | <li>Dengue and severe dengue - World Health Organization, https://reurl.cc/q84qQp</li>
| + | <li>Taiwan National Infectious Disease Statistics System - Taiwan Centers of Disease Control (TCDC), https://reurl.cc/EzLvE1</li> |
− | <li>Dengue Fever – Taiwan Centers of Disease Control (TCDC), https://reurl.cc/q84qQR</li>
| + | <li>Dengue and severe dengue - World Health Organization, https://reurl.cc/q84qQp</li> |
− | </ol>
| + | <li>Dengue Fever – Taiwan Centers of Disease Control (TCDC), https://reurl.cc/q84qQR</li> |
− | <br>
| + | </ol> |
− | <b>Inspiration</b>
| + | <br> |
− | <ol>
| + | <li><b>Inspiration</b></li> |
− | <li>Szu-Ting Chen, Fei-Ju Li, Tzy-yun Hsu, Shu-Mei Liang, Yi-Chen Yeh, Wen-Yu Liao, Teh-Ying Chou, Nien-Jun Chen, Michael Hsiao, Wen-Bin Yang, and Shie-Liang Hsieh. CLEC5A is a critical receptor in innate immunity against Listeria infection. Nature Communications. 2017; 8(1): 299. doi:10.1038/s41467-017-00356-3.</li>
| + | <ol> |
− | <li>Aleksandra A Watson, Andrey A Lebedev, Benjamin A Hall, Angharad E Fenton-May, Alexei A Vagin, Wanwisa Dejnirattisai, James Felce, Juthathip Mongkolsapaya, Angelina S Palma, Yan Liu, Ten Feizi, Gavin R Screaton, Garib N Murshudov, and Christopher A O'Callaghan. Structural flexibility of the macrophage dengue virus receptor CLEC5A: implications for ligand binding and signaling. Journal of Biological Chemistry. 2011; 286(27): 24208-24218. doi: 10.1074/jbc.M111.226142.</li>
| + | <li>Szu-Ting Chen, Fei-Ju Li, Tzy-yun Hsu, Shu-Mei Liang, Yi-Chen Yeh, Wen-Yu Liao, Teh-Ying Chou, Nien-Jun Chen, Michael Hsiao, Wen-Bin Yang, and Shie-Liang Hsieh. CLEC5A is a critical receptor in innate immunity against Listeria infection. Nature Communications. 2017; 8(1): 299. doi:10.1038/s41467-017-00356-3.</li> |
− | </ol>
| + | <li>Aleksandra A Watson, Andrey A Lebedev, Benjamin A Hall, Angharad E Fenton-May, Alexei A Vagin, Wanwisa Dejnirattisai, James Felce, Juthathip Mongkolsapaya, Angelina S Palma, Yan Liu, Ten Feizi, Gavin R Screaton, Garib N Murshudov, and Christopher A O'Callaghan. Structural flexibility of the macrophage dengue virus receptor CLEC5A: implications for ligand binding and signaling. Journal of Biological Chemistry. 2011; 286(27): 24208-24218. doi: 10.1074/jbc.M111.226142.</li> |
− | <br>
| + | </ol> |
− | <b>LAE</b>
| + | <br> |
− | <br>
| + | <li><b>LAE</b></li> |
− | <ol>
| + | <br> |
− | <li>Peng-Yeh Lai, Chia-Tse Hsu, Shao-Hung Wang, Jin-Ching Lee, Min-Jen Tseng, Jaulang Hwang, Wen-Tsai Ji, and Hau-Ren Chen. Production of a neutralizing antibody against envelope protein of dengue virus type 2 using the linear array epitope technique. Journal of General Virology. 2014; 95(10): 2155-2165. doi: 10.1099/vir.0.062562-0.</li>
| + | <ol> |
− | </ol>
| + | <li>Peng-Yeh Lai, Chia-Tse Hsu, Shao-Hung Wang, Jin-Ching Lee, Min-Jen Tseng, Jaulang Hwang, Wen-Tsai Ji, and Hau-Ren Chen. Production of a neutralizing antibody against envelope protein of dengue virus type 2 using the linear array epitope technique. Journal of General Virology. 2014; 95(10): 2155-2165. doi: 10.1099/vir.0.062562-0.</li> |
− | <br><br>
| + | </ol> |
− | <b>Modeling: Interaction between the Tandem-repeated Sequence Peptide and E Protein</b>
| + | <br><br> |
− | <ol>
| + | <li><b>Modeling: Interaction between the Tandem-repeated Sequence Peptide and E Protein</b></li> |
− | <li>Maciej Ciemny, Mateusz Kurcinski, Karol Kamel, Andrzej Kolinski, Nawsad Alam, Ora Schueler-Furman, and Sebastian Kmiecik. Protein–peptide docking: opportunities and challenges. Drug Discovery Today. 2018; 23(8): 1530-1537. doi: 10.1016/j.drudis.2018.05.006.</li>
| + | <ol> |
− | <li>Steven A Combs, Samuel L Deluca, Stephanie H Deluca, Gordon H Lemmon, David P Nannemann, Elizabeth D Nguyen, Jordan R Willis, Jonathan H Sheehan, and Jens Meiler. Small-molecule ligand docking into comparative models with Rosetta. Nature Protocols. 2013; 8(7): 1277-1298. doi: 10.1038/nprot.2013.074.</li>
| + | <li>Maciej Ciemny, Mateusz Kurcinski, Karol Kamel, Andrzej Kolinski, Nawsad Alam, Ora Schueler-Furman, and Sebastian Kmiecik. Protein–peptide docking: opportunities and challenges. Drug Discovery Today. 2018; 23(8): 1530-1537. doi: 10.1016/j.drudis.2018.05.006.</li> |
− | </ol>
| + | <li>Steven A Combs, Samuel L Deluca, Stephanie H Deluca, Gordon H Lemmon, David P Nannemann, Elizabeth D Nguyen, Jordan R Willis, Jonathan H Sheehan, and Jens Meiler. Small-molecule ligand docking into comparative models with Rosetta. Nature Protocols. 2013; 8(7): 1277-1298. doi: 10.1038/nprot.2013.074.</li> |
− | <br>
| + | </ol> |
− | <b>Modeling: Interaction between Gold Nanoparticles</b>
| + | <br> |
− | <ol>
| + | <li><b>Modeling: Interaction between Gold Nanoparticles</b></li> |
− | <li>Elena Pokidysheva, Ying Zhang, Anthony J Battisti, Carol M Bator-Kelly, Paul R Chipman, Chuan Xiao, G Glenn Gregorio, Wayne A Hendrickson, Richard J Kuhn, and Michael G Rossmann. Cryo-EM Reconstruction of Dengue Virus in Complex with the Carbohydrate Recognition Domain of DC-SIGN. Cell. 2006; 124(3): 485-93. doi: 10.1016/j.cell.2005.11.042.</li>
| + | <ol> |
− | <li>Jörg Polte. Fundamental growth principles of colloidal metal nanoparticles – a new perspective. CrystEngComm. 2015, 17(36): 6809-6830. doi:10.1039/C5CE01014D.</li>
| + | <li>Elena Pokidysheva, Ying Zhang, Anthony J Battisti, Carol M Bator-Kelly, Paul R Chipman, Chuan Xiao, G Glenn Gregorio, Wayne A Hendrickson, Richard J Kuhn, and Michael G Rossmann. Cryo-EM Reconstruction of Dengue Virus in Complex with the Carbohydrate Recognition Domain of DC-SIGN. Cell. 2006; 124(3): 485-93. doi: 10.1016/j.cell.2005.11.042.</li> |
− | <li>Phillip E Mason, Adrien Lerbret, Marie-Louise Saboungi, George W Neilson, Christopher E Dempsey, and John W Brady. Glucose Interactions with a Model Peptide. Proteins. 2011; 79(7): 2224-2232. doi: 10.1002/prot.23047.</li>
| + | <li>Jörg Polte. Fundamental growth principles of colloidal metal nanoparticles – a new perspective. CrystEngComm. 2015, 17(36): 6809-6830. doi:10.1039/C5CE01014D.</li> |
− | <li>Taehoon Kim, Kangtaek Lee, Myoung-seon Gong, and Sang-Woo Joo. Control of Gold Nanoparticle Aggregates by Manipulation of Interparticle Interaction. Langmuir . 2005; 21(21): 9524-9528. doi: 10.1021/la0504560.</li>
| + | <li>Phillip E Mason, Adrien Lerbret, Marie-Louise Saboungi, George W Neilson, Christopher E Dempsey, and John W Brady. Glucose Interactions with a Model Peptide. Proteins. 2011; 79(7): 2224-2232. doi: 10.1002/prot.23047.</li> |
− | </ol>
| + | <li>Taehoon Kim, Kangtaek Lee, Myoung-seon Gong, and Sang-Woo Joo. Control of Gold Nanoparticle Aggregates by Manipulation of Interparticle Interaction. Langmuir . 2005; 21(21): 9524-9528. doi: 10.1021/la0504560.</li> |
| + | </ol> |
| + | </ul> |
| </div> | | </div> |
| </div> | | </div> |