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Micha Kornreich

Publications and source records attributed to Micha Kornreich.

4 recordsLinked to original sources

Inpainting Pathology in Lumbar Spine MRI with Latent Diffusion

Data driven models for automated diagnosis in radiology suffer from insufficient and imbalanced datasets due to low representation of pathology in a population and the cost of expert annotations. Datasets can be bolstered through data augmentation. However, even when utilizing a full suite of transformations during model training, typical data augmentations do not address variations in human anatomy. An alternative direction is to synthesize data using generative models, which can potentially craft datasets with specific attributes. While this holds promise, commonly used generative models such as Generative Adversarial Networks may inadvertently produce anatomically inaccurate features. On the other hand, diffusion models, which offer greater stability, tend to memorize training data, raising concerns about privacy and generative diversity. Alternatively, inpainting has the potential to augment data through directly inserting pathology in medical images. However, this approach introduces a new challenge: accurately merging the generated pathological features with the surrounding anatomical context. While inpainting is a well established method for addressing simple lesions, its application to pathologies that involve complex structural changes remains relatively unexplored. We propose an efficient method for inpainting pathological features onto healthy anatomy in MRI through voxelwise noise scheduling in a latent diffusion model. We evaluate the method's ability to insert disc herniation and central canal stenosis in lumbar spine sagittal T2 MRI, and it achieves superior Frechet Inception Distance compared to state-of-the-art methods.

eess.IV

Universal and accessible entropy estimation using a compression algorithm

Entropy and free-energy estimation are key in thermodynamic characterization of simulated systems ranging from spin models through polymers, colloids, protein structure, and drug-design. Current techniques suffer from being model specific, requiring abundant computation resources and simulation at conditions far from the studied realization. Here, we present a universal scheme to calculate entropy using lossless compression algorithms and validate it on simulated systems of increasing complexity. Our results show accurate entropy values compared to benchmark calculations while being computationally effective. In molecular-dynamics simulations of protein folding, we exhibit unmatched detection capability of the folded states by measuring previously undetectable entropy fluctuations along the simulation timeline. Such entropy evaluation opens a new window onto the dynamics of complex systems and allows efficient free-energy calculations.

cond-mat.stat-mech

Phosphorylation-induced mechanical regulation of intrinsically disordered neurofilament protein assemblies

The biological function of protein assemblies was conventionally equated with a unique three-dimensional protein structure and protein-specific interactions. However, in the past 20 years it was found that some assemblies contain long flexible regions that adopt multiple structural conformations. These include neurofilament (NF) proteins that constitute the stress-responsive supportive network of neurons. Herein, we show that NF networks macroscopic properties are tuned by enzymatic regulation of the charge found on the flexible protein regions. The results reveal an enzymatic (phosphorylation) regulation of macroscopic properties such as orientation, stress-response and expansion in flexible protein assemblies. Together with a model explaining the attractive electrostatic interactions induced by enzymatically added charges, we demonstrate that phosphorylation-regulation is far richer and versatile than previously considered.

physics.bio-ph

Neurofilaments function as shock absorbers: compression response arising from disordered proteins

What can cells gain by using disordered, rather than folded, proteins in the architecture of their skeleton? Disordered proteins take multiple co-existing conformations, and often contain segments which act as random-walk-shaped polymers. Using X-ray scattering we measure the compression response of disordered protein hydrogels, which are the main stress-responsive component of neuron cells. We find that at high compression their mechanics are dominated by gas-like steric and ionic repulsions. At low compression, specific attractive interactions dominate. This is demonstrated by the considerable hydrogel expansion induced by the truncation of critical short protein segments. Accordingly, the floppy disordered proteins form a weakly cross-bridged hydrogel, and act as shock absorbers that sustain large deformations without failure.

cond-mat.soft