화학공학소재연구정보센터
검색결과 : 16건
No. Article
1 ATP is a cryptic binder of TDP-43 RRM domains to enhance stability and inhibit ALS/AD-associated fibrillation
Dang M, Kang J, Lim LZ, Li YF, Wang L, Song JX
Biochemical and Biophysical Research Communications, 522(1), 247, 2020
2 A novel mechanism for ATP to enhance the functional oligomerization of TDP-43 by specific binding
Wang L, Lim LZ, Dang M, Song JX
Biochemical and Biophysical Research Communications, 514(3), 809, 2019
3 TDP-43 NTD can be induced while CTD is significantly enhanced by ssDNA to undergo liquid-liquid phase separation
Wang L, Kang J, Lim LZ, Wei YY, Song JX
Biochemical and Biophysical Research Communications, 499(2), 189, 2018
4 ATP enhances at low concentrations but dissolves at high concentrations liquid-liquid phase separation (LLPS) of ALS/FTD-causing FUS
Kang J, Lim LZ, Song JX
Biochemical and Biophysical Research Communications, 504(2), 545, 2018
5 The alteration of serine transporter activity in a cell line model of amyotrophic lateral sclerosis (ALS)
Lee NY, Kim Y, Ryu H, Kang YS
Biochemical and Biophysical Research Communications, 483(1), 135, 2017
6 ALS-causing cleavages of TDP-43 abolish its RRM2 structure and unlock CTD for enhanced aggregation and toxicity
Wei YY, Lim LZ, Wang L, Song JX
Biochemical and Biophysical Research Communications, 485(4), 826, 2017
7 An easy method for bacterial expression and purification of wild-type and mutant superoxide dismutase 1 (SOD1)
Tachu BJ, Wusten KA, Garza MC, Wille H, Tamguney G
Protein Expression and Purification, 134, 63, 2017
8 Inter-domain interactions of TDP-43 as decoded by NMR
Wei YY, Lim LZ, Wang L, Song JX
Biochemical and Biophysical Research Communications, 473(2), 614, 2016
9 Brain-Specific Cytoskeletal Damage Markers in Cerebrospinal Fluid: Is There a Common Pattern between Amyotrophic Lateral Sclerosis and Primary Progressive Multiple Sclerosis?
Abdelhak A, Junker A, Brettschneider J, Kassubek J, Ludolph AC, Otto M, Tumani H
International Journal of Molecular Sciences, 16(8), 17565, 2015
10 ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its beta-sandwich fold into lipid-interacting helical conformations
Qin HN, Wang W, Song JX
Biochemical and Biophysical Research Communications, 431(3), 398, 2013