Papers
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26. Chia, W.N., Tan, C.W., Tan, A.W.K., Young, B., Starr, T.N., Lopez, E., Fibriansah, G., Barr, J., Cheng, S., Yeoh, A.Y., Yap, W.C., Lim, B.L., Ng, T.S., Sia, W.R., Zhu, F., Chen, S., Zhang, J., Kwek, M.S.S., Greaney, A.J., Chen, M., Au, G.G., Paradkar, P.N., Peiris, M., Chung, A.W., Bloom, J.D., Lye, D., Lok, S., Wang, L.F. (2023). Potent pan huACE2-dependent sarbecovirus neutralizing monoclonal antibodies isolated from a BNT162b2-vaccinated SARS survivor. Sci Adv. 9(30):eade3470.
PubMed ID: 37494438 |
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25. Shu, B., Ooi, J.S.G., Tan, A.W.K., Ng, T.S., Dejnirattisai, W., Mongkolsapaya, J., Fibriansah, G., Shi, J., Kostyuchenko, V.A., Screaton, G.R., Lok, S.M. (2022). CryoEM structures of the multimeric secreted NS1, a major factor for dengue hemorrhagic fever. Nat Commun. 13(1):6756.
PubMed ID: 36347841 |
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24. Fibriansah, G., Lim, X.N., Lok, S.M. (2021). Morphological diversity and dynamics of dengue virus affecting antigenicity. Viruses 13(8):1446.
PubMed ID: 34452312 |
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23. Fibriansah, G., Lim, E.X.Y., Marzinek, J.K., Ng, T.S., Tan, J.L., Huber, R.G., Lim, X.N., Chew, V.S.Y., Kostyuchenko, V.A., Shi, J., Anand, G.S., Bond, P.J., Crowe, J.E. Jr., Lok, S.M. (2021). Antibody affinity versus dengue morphology influences neutralization. PLoS Pathog. 17(2):e1009331.
PubMed ID: 33621239 |
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22. Zhou, Q.F., Fox, J.M., Earnest, J.T., Ng, T.S., Kim, A.S., Fibriansah, G., Kostyuchenko, V.A., Shi, J., Shu, B., Diamond, M.S., Lok, S.M. (2020). Structural basis of Chikungunya virus inhibition by monoclonal antibodies. Proc Natl Acad Sci U S A. 117(44):27637-27645.
PubMed ID: 33087569 |
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21. Tan, T. Y., Fibriansah, G., Lok, S. M. (2020). Capsid protein is central to the birth of flavivirus particles. PLoS pathogens, 16(5), e1008542.
PubMed ID: 32463839 |
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20. Tan, T. Y., Fibriansah, G., Kostyuchenko, V. A., Ng, T. S., Lim, X. X., Zhang, S., Lim, X. N., Wang, J., Shi, J., Morais, M. C., Corti, D., Lok, S. M. (2020). Capsid protein structure in Zika virus reveals the flavivirus assembly process. Nat Commun. 11(1):895.
PubMed ID: 32060358 |
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19. Lim, X.N., Shan, C., Marzinek, J.K., Dong, H., Ng, T.S., Ooi, J.S.G., Fibriansah, G., Wang, J., Verma, C.S., Bond, P.J., Shi, P.Y., Lok, S.M. (2019). Molecular basis of dengue virus serotype 2 morphological switch from 29°C to 37°C. PLoS Pathog. 19;15(9):e1007996.
PubMed ID: 31536610 |
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18. Wirawan, M., Fibriansah, G., Marzinek, J.K., Lim, X.X., Ng, T.S., Sim, A.Y.L., Zhang, Q., Kostyuchenko, V.A., Shi, J., Smith, S.A., Verma, C.S., Anand, G., Crowe, J.E. Jr, Bond, P.J., Lok, S.M. (2019). Mechanism of Enhanced Immature Dengue Virus Attachment to Endosomal Membrane Induced by prM Antibody. Structure 27(2):253-267.e8.
PubMed ID: 30471923 |
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17. Wang, J., Bardelli, M., Espinosa, D.A., Pedotti, M., Ng, T.-S., Bianchi, S., Simonelli, L., Lim, E.X.Y., Foglierini, M., Zatta, F., Jaconi, S., Beltramello, M., Cameroni, E., Fibriansah, G., Shi, J., Barca, T., Pagani, I., Rubio, A., Broccoli, V., Vicenzi, E., Graham, V., Pullan, S., Dowall, S., Hewson, R., Jurt, S., Zerbe, O., Stettler, K., Lanzavecchia, A., Sallusto, F., Cavalli, A., Harris, E., Lok, S.-M., Varani, L., Corti, D. (2017). A Human Bi-specific Antibody against Zika Virus with High Therapeutic Potential. Cell 171(1):229-241.
Pubmed ID: 28938115 |
16. Kostyuchenko, V.A., Lim, E.X., Zhang, S., Fibriansah, G., Ng, T.S., Ooi, J.S., Shi, J., Lok, S.M. (2016). Structure of the thermally stable Zika virus. Nature 533(7603):425-8.
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15. Fibriansah, G., Lok, S.M. (2016). The development of therapeutic antibodies against dengue virus. Antiviral Res. 128:7-19.
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14. Fibriansah, G., Ibarra, K.D., Ng, T.S., Smith, S.A., Tan, J.L., Lim, X.N., Ooi, J.S., Kostyuchenko, V.A., Wang, J., de Silva, A.M., Harris, E., Crowe, J.E. Jr, Lok, S.M. (2015). Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers. Science 349(6243):88-91.
Pubmed ID : 26138979 |
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13. Fibriansah, G., Tan, J.L., Smith, S.A., de Alwis, R., Ng, T.S., Kostyuchenko, V.A., Jadi, R.S., Kukkaro, P., de Silva, A.M., Crowe, J.E., Lok, S.M. (2015). A highly potent human antibody neutralizes dengue virus serotype 3 by binding across three surface proteins. Nature Commun. 6:6341.
Pubmed ID: 25698059 |
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12. Natalia, D., Vidilaseris, K., Ismaya, W.T., Puspasari, F., Prawira, I., Hasan, K., Fibriansah, G., Permentier, H.P., Nurachman, Z., Subroto, T., Dijkstra, B.W.,
Soemitro, S. (2015). Effect of introducing a disulphide bond between the A and C domains on the activity and stability of Saccharomycopsis fibuligera R64 α- amylase. J Biotechnol. 195:8-14.
Pubmed ID: 25533400 |
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11. Fibriansah, G., Tan, J.L., Smith, S.A., de Alwis, A.R., Ng, T.S., Kostyuchenko, V.A., Ibarra, K.D., Wang, J., Harris, E., de Silva, A., Crowe, J.E. Jr, Lok, S.M. (2014). A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface. EMBO Mol Med 6(3):358-371.
(Featured on the cover page)
Pubmed ID: 24421336 |
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10. Fibriansah, G., Ng, T.S., Kostyuchenko, V.A., Lee, J., Lee S, Wang J, Lok, S.M. (2013). Structural changes in dengue virus when exposed to a temperature of 37°C. J Virol., 87(13):7585-7592.
(Featured on the cover page)
Pubmed ID: 23637405 |
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9. Zhang, Q., Hunke, C., Yau, Y.H., Seow, V., Lee, S., Tanner, L.B., Guan, X.L., Wenk, M.R., Fibriansah, G., Chew, P.L., Kukkaro, P., Biukovic, G., Shi, P.Y., Shochat, S.G., Grüber, G., Lok, S.-M. (2012). The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation. J Biol Chem., 287(48):40525-40534
Pubmed ID: 23035113 |
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8. Fibriansah, G., Kovács, Á.T., Pool, T.J., Boonstra, M., Kuipers, O.P., Thunnissen, A.-M. (2012). Crystal structures of two transcriptional regulators from Bacillus cereus define the conserved structural features of a PadR subfamily. PLoS One, 7(11):e48015.
Pubmed ID: 23189126 |
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7. Fibriansah, G., Gliubich, F.I., Thunnissen, A.-M. (2012). On the mechanism of peptidoglycan binding and cleavage by the endo-specific lytic transglycosylase MltE from Escherichia coli. Biochemistry, 51(45):9164-9177.
Pubmed ID: 23075328 |
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6. Puthan Veetil, V., Fibriansah, G., Raj, H., Thunnissen, A.-M., Poelarends, G.J. (2012). Aspartase/fumarase superfamily: a common catalytic strategy involving general base-catalyzed formation of a highly stabilized aci - carboxylate intermediate. Biochemistry, 51(21):4237-4243.
Pubmed ID: 22551392 |
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5. Fibriansah, G., Veetil, V.P., Poelarends, G.J., Thunnissen, A.-M. (2011). Structural basis for the catalytic mechanism of aspartate ammonia lyase. Biochemistry, 50(27):6053-6062
Pubmed ID: 21661762 |
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4. Natalia, D., Vidilaseris, K., Satrimafitrah, P., Ismaya, W.T., Purkan, Permentier, H., Fibriansah, G., Puspasari, F., Nurachman, Z., Dijkstra, B.W., and Soemitro, S. (2011). Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64. Biologia, 66:27-32.
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3. Koizumi, N., Isoda, Y., Maeda, K., Masuda, S., Fibriansah, G., Kumasaka, T., Yatsunami, R., Fukui, T., Nakamura, S. (2007). Characterization of Nocardiopsis β-1,3-glucanase with additional carbohydrate-binding domains. Nucleic Acids Symp Ser (Oxf), 51:459-460.
Pubmed ID: 18029785 |
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2. Fibriansah, G., Masuda, S., Koizumi, N., Nakamura, S., and Kumasaka,T. (2007).The 1.3 Å crystal structure of a novel endo-β-1,3-glucanase of glycoside hydrolase family 16 from alkaliphilic Nocardiopsis sp. strain F96. Proteins, 69(3):683-690.
Pubmed ID: 17879342 |
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1. Fibriansah, G., Masuda, S., Hirose, R., Hamada, K., Tanaka, N., Nakamura, S. and Kumasaka, T. (2006). Crystallization and preliminary crystallographic analysis of endo-1,3-β-glucanase from alkaliphilic Nocardiopsis sp. strain F96. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun., 62(1):20- 22.
Pubmed ID: 16511252 |