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Lim Liang Zhong

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Full Name
Lim Liang Zhong
Variants
Lim, Liang Zhong
Lim, L.
Lim, Liangzhong
 
Main Affiliation
 
Faculty
 
Email
dbsliml@nus.edu.sg
 

Publications

Results 1-16 of 16 (Search time: 0.013 seconds).

Issue DateTitleAuthor(s)
12019A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acidsKang, J.; Lim, L. ; Lu, Y. ; Song, J. 
22016ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43Lim L. ; Wei Y.; Lu Y. ; Song J. 
32019ATP binds and inhibits the neurodegeneration-associated fibrillization of the FUS RRM domainKang, J.; Lim, L. ; Song, J. 
42015Dynamic principle for designing antagonistic/agonistic molecules for EphA4 receptor, the only known ALS modifierQin, Haina ; Lim, Liang Zhong ; Song, Jianxing 
52014Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domainLim L. ; Shi J.; Mu Y.; Song J.
6Feb-2011Dynamically-driven inactivation of the catalytic machinery of the sars 3C-like protease by the N214A mutation on the extra domainShi, J. ; Han, N.; Lim, L. ; Lua, S.; Sivaraman, J. ; Wang, L.; Mu, Y.; Song, J. 
72015Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutationsLim, Liang Zhong 
82015NMR and MD studies reveal that the isolated dengue NS3 protease is an intrinsically disordered chymotrypsin fold which absolutely requests NS2B for correct folding and functional dynamicsGARVITA GUPTA ; Lim L. ; Song J. 
916-Aug-2013NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1Wang, W.; Lim, L. ; Baskaran, Y.; Manser, E.; Song, J. 
1025-Jan-2012Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulationsQin, H. ; Lim, L. ; Song, J. 
112014Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesSong J. ; Qin H. ; Lim L. ; Wei Y. ; Gupta G. 
122017RRM domain of ALS/FTD-causing FUS characteristic of irreversible unfolding spontaneously self-assembles into amyloid fibrils /631/1647/2258/878/1263 /631/535/878/1263 /101 /101/6 articleLu, Y ; Lim, L ; Song, J 
132017Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plantsRoy A. ; Lim L. ; Srivastava S.; Lu Y. ; Song J. 
141-Nov-2011Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulationsLua, S.; Qin, H. ; Lim, L. ; Shi, J. ; Gupta, G.; Song, J. 
152018TMEM106B, a risk factor for FTLD and aging, has an intrinsically disordered cytoplasmic domainKang J.; Lim L. ; Song J. 
1624-Sep-2013Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD SimulationsHuan, X.; Shi, J. ; Lim, L. ; Mitra, S.; Zhu, W.; Qin, H. ; Pasquale, E.B.; Song, J.