Guntur Fibriansah
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Research articles

Papers


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
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
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
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
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
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
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.
Pubmed ID: 27093288

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15.         Fibriansah, G., Lok, S.M. (2016). The development of therapeutic antibodies against dengue virus. Antiviral Res. 128:7-19.
Pubmed ID: 26794397

​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
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

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
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
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

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

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
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  • Home
  • About me
  • Publications
    • Research Papers
    • Structures
    • Science Art
    • Posters
    • Doctoral Thesis
  • Protocols
    • Cryo-EM
    • X-ray Crystallography
  • Links
    • Proteomic works
    • Genomic works
    • Cryo-EM
    • X-Ray Crystallography
    • Structure Analysis
    • Programming
    • Data Analysis
    • Lectures
  • Contact me
  • Photography
  • VIPER Blog