Yuanyuan Wei

Singapore, 169857, Singapore

Last Updated: 09/26/2026

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Found 8 publications

Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.

Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.

Journal: Scientific reports
Published: September 02, 2025

Structural transitions in kinesin minus-end directed microtubule motility.

Structural transitions in kinesin minus-end directed microtubule motility.

Journal: bioRxiv : the preprint server for biology
Published: August 12, 2024

TDP-43 NTD can be induced while CTD is significantly enhanced by ssDNA to undergo liquid-liquid phase separation.

TDP-43 NTD can be induced while CTD is significantly enhanced by ssDNA to undergo liquid-liquid phase separation.

Journal: Biochemical and biophysical research communications
Published: March 05, 2018

ALS-causing cleavages of TDP-43 abolish its RRM2 structure and unlock CTD for enhanced aggregation and toxicity.

ALS-causing cleavages of TDP-43 abolish its RRM2 structure and unlock CTD for enhanced aggregation and toxicity.

Journal: Biochemical and biophysical research communications
Published: February 22, 2017

Inter-domain interactions of TDP-43 as decoded by NMR.

Inter-domain interactions of TDP-43 as decoded by NMR.

Journal: Biochemical and biophysical research communications
Published: March 25, 2016

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.

Journal: PLoS biology
Published: May 22, 2015

TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA.

TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA.

Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: December 16, 2014

Resolving 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 membranes.

Resolving 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 membranes.

Journal: F1000Research
Published: January 01, 2013
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Last Updated: 09/26/2026