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Nur Alia Oktaviani
Nur Alia Oktaviani
RIKEN Center for Sustainable Resource Science (CSRS), Japan
Verified email at riken.jp
Title
Cited by
Cited by
Year
Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies
TT O’Malley, NA Oktaviani, D Zhang, A Lomakin, B O’Nuallain, S Linse, ...
Biochemical Journal 461 (3), 413-426, 2014
752014
Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
NA Oktaviani, A Matsugami, AD Malay, F Hayashi, DL Kaplan, K Numata
Nature communications 9 (1), 2121, 2018
592018
Selenomethionine incorporation in proteins expressed in Lactococcus lactis
RPA Berntsson, N Alia Oktaviani, F Fusetti, AMWH Thunnissen, ...
Protein Science 18 (5), 1121-1127, 2009
532009
1000 spider silkomes: Linking sequences to silk physical properties
K Arakawa, N Kono, AD Malay, A Tateishi, N Ifuku, H Masunaga, R Sato, ...
Science advances 8 (41), eabo6043, 2022
452022
Unambiguous determination of protein arginine ionization states in solution by NMR spectroscopy
Y Yoshimura, NA Oktaviani, K Yonezawa, H Kamikubo, FAA Mulder
Angewandte Chemie International Edition 56 (1), 239-242, 2017
312017
Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide
NA Oktaviani, MW Risør, YH Lee, RP Megens, DH de Jong, R Otten, ...
Journal of Biomolecular NMR 62, 129-142, 2015
272015
A marine photosynthetic microbial cell factory as a platform for spider silk production
CP Foong, M Higuchi-Takeuchi, AD Malay, NA Oktaviani, C Thagun, ...
Communications biology 3 (1), 357, 2020
242020
Complexity of spider dragline silk
AD Malay, HC Craig, J Chen, NA Oktaviani, K Numata
Biomacromolecules 23 (5), 1827-1840, 2022
222022
Ion effects on the conformation and dynamics of repetitive domains of a spider silk protein: Implications for solubility and β-sheet formation
NA Oktaviani, A Matsugami, F Hayashi, K Numata
Chemical communications 55 (66), 9761-9764, 2019
222019
Comprehensive determination of protein tyrosine pKa values for photoactive yellow protein using indirect 13C NMR spectroscopy
NA Oktaviani, TJ Pool, H Kamikubo, J Slager, RM Scheek, M Kataoka, ...
Biophysical journal 102 (3), 579-586, 2012
222012
100% complete assignment of non-labile 1H, 13C, and 15N signals for calcium-loaded calbindin D9k P43G
NA Oktaviani, R Otten, K Dijkstra, RM Scheek, E Thulin, M Akke, ...
Biomolecular NMR Assignments 5, 79-84, 2011
152011
Aspartate buffer and divalent metal ions affect oxytocin in aqueous solution and protect it from degradation
C Avanti, NA Oktaviani, WLJ Hinrichs, HW Frijlink, FAA Mulder
International journal of pharmaceutics 444 (1-2), 139-145, 2013
132013
1H, 13C, and 15N resonance assignment of photoactive yellow protein
TJ Pool, NA Oktaviani, H Kamikubo, M Kataoka, FAA Mulder
Biomolecular NMR Assignments 7, 97-100, 2013
102013
Nearly complete 1H, 13C and 15N chemical shift assignment of monomeric form of N-terminal domain of Nephila clavipes major ampullate spidroin 2
NA Oktaviani, AD Malay, A Matsugami, F Hayashi, K Numata
Biomolecular NMR Assignments 14, 335-338, 2020
62020
Active-site pKa determination for photoactive yellow protein rationalizes slow ground-state recovery
NA Oktaviani, TJ Pool, Y Yoshimura, H Kamikubo, RM Scheek, M Kataoka, ...
Biophysical Journal 112 (10), 2109-2116, 2017
62017
Unusual pKa Values Mediate the Self-Assembly of Spider Dragline Silk Proteins
NA Oktaviani, AD Malay, A Matsugami, F Hayashi, K Numata
Biomacromolecules 24 (4), 1604-1616, 2023
32023
NMR studies of folded and unfolded proteins: method developments and biological insight
N Oktaviani
22014
NMR assignment and dynamics of the dimeric form of soluble C-terminal domain major ampullate spidroin 2 from Latrodectus hesperus
NA Oktaviani, AD Malay, M Goto, T Nagashima, F Hayashi, K Numata
Biomolecular NMR Assignments 17 (2), 249-255, 2023
12023
Comprehensive determination of protein tyrosine pKa values using indirect 13C NMR spectroscopy: an application to photoactive yellow protein
NA Oktaviani, TJ Pool, H Kamikubo, J Slager, RM Scheek, M Kataoka, ...
NMR studies of folded and unfolded proteins: method developments and …, 2014
2014
An optimal paramagnetic relaxation agent for NMR spectroscopy of intrinsically disordered proteins
NA Oktaviani, YH Lee, RP Megens, Y Goto, RM Scheek, T Ikegami, ...
NMR studies of folded and unfolded proteins: method developments and …, 2014
2014
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Articles 1–20