Pages that link to "Q33516611"
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The following pages link to Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations (Q33516611):
Displaying 12 items.
- Cooperative stabilization of transthyretin by clusterin and diflunisal. (Q35001154) (← links)
- Localized structural fluctuations promote amyloidogenic conformations in transthyretin (Q36675670) (← links)
- Chemodiversity and molecular plasticity: recognition processes as explored by property spaces (Q37894716) (← links)
- Cluster analysis of molecular simulation trajectories for systems where both conformation and orientation of the sampled states are important (Q42019473) (← links)
- Impact of deglycosylation and thermal stress on conformational stability of a full length murine IgG2a monoclonal antibody: observations from molecular dynamics simulations (Q44540221) (← links)
- Insights into the potential aggregation liabilities of the b12 Fab fragment via elevated temperature molecular dynamics (Q46170428) (← links)
- Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation. (Q46171494) (← links)
- Dynamics and Thermodynamics of Transthyretin Association from Molecular Dynamics Simulations. (Q55417366) (← links)
- A FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes (Q58731093) (← links)
- Molecular dynamics simulation study of AG10 and tafamidis binding to the Val122Ile transthyretin variant (Q89704877) (← links)
- Biophysical characterization and modulation of Transthyretin Ala97Ser (Q90012340) (← links)
- Exploration of the Misfolding Mechanism of Transthyretin Monomer: Insights from Hybrid-Resolution Simulations and Markov State Model Analysis (Q92152546) (← links)