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Yildiz, M.

Publications and source records attributed to Yildiz, M..

2 recordsLinked to original sources

Insights from the IronTract challenge: optimal methods for mapping brain pathways from multi-shell diffusion MRI

Limitations in the accuracy of brain pathways reconstructed by diffusion MRI (dMRI) tractography have received considerable attention. While the technical advances spearheaded by the Human Connectome Project (HCP) led to significant improvements in dMRI data quality, it remains unclear how these data should be analyzed to maximize tractography accuracy. Over a period of two years, we have engaged the dMRI community in the IronTract Challenge, which aims to answer this question by leveraging a unique dataset. Macaque brains that have received both tracer injections and ex vivo dMRI at high spatial and angular resolution allow a comprehensive, quantitative assessment of tractography accuracy on state-of-the-art dMRI acquisition schemes. We find that, when analysis methods are carefully optimized, the HCP scheme can achieve similar accuracy as a more time-consuming, Cartesian-grid scheme. Importantly, we show that simple pre- and post-processing strategies can improve the accuracy and robustness of many tractography methods. Finally, we find that fiber configurations that go beyond crossing (e.g., fanning, branching) are the most challenging for tractography. The IronTract Challenge remains open and we hope that it can serve as a valuable validation tool for both users and developers of dMRI analysis methods.

neuroscience↗

An Accurate Free Energy Method for Solvation of Organic Compounds and Binding to Proteins

Here, we introduce a new strategy to estimate free energies using single end-state molecular dynamics simulation trajectories. The method is adopted from ANI-1ccx neural network potentials (Machine Learning) for the Atomic Simulation Environment (ASE) and predicts the single point energies at the accuracy of CCSD(T)/CBS level for the entire configurational space that is sampled by Molecular Dynamics (MD) simulations. Our preliminary results show that the method can be as accurate as Bennet-Acceptance-Ration (BAR) with much reduced computational cost. Not only does it enable to calculate solvation free energies of small organic compounds, but it is also possible to predict absolute and relative binding free energies in ligand-protein complex systems. Rapid calculation also enables to screen small organic molecules from databases as potent inhibitors to any drug targets.

biophysics↗