EBSR: Enhanced Binary Neural Network for Image Super-Resolution

While the performance of deep convolutional neural networks for image super-resolution (SR) has improved significantly, the rapid increase of memory and computation requirements hinders their deployment on resource-constrained devices. Quantized networks, especially binary neural networks (BNN) for SR have been proposed to significantly improve the model inference efficiency but suffer from large performance degradation. We observe the activation distribution of SR networks demonstrates very large pixel-to-pixel, channel-to-channel, and image-to-image variation, which is important for high performance SR but gets lost during binarization. To address the problem, we propose two effective methods, including the spatial re-scaling as well as channel-wise shifting and re-scaling, which augments binary convolutions by retaining more spatial and channel-wise information. Our proposed models, dubbed EBSR, demonstrate superior performance over prior art methods both quantitatively and qualitatively across different datasets and different model sizes. Specifically, for x4 SR on Set5 and Urban100, EBSRlight improves the PSNR by 0.31 dB and 0.28 dB compared to SRResNet-E2FIF, respectively, while EBSR outperforms EDSR-E2FIF by 0.29 dB and 0.32 dB PSNR, respectively.

Deep manifold learning reveals hidden dynamics of proteasome autoregulation

The 2.5-MDa 26S proteasome maintains proteostasis and regulates myriad cellular processes. How polyubiquitylated substrate interactions regulate proteasome activity is not understood. Here we introduce a deep manifold learning framework, named AlphaCryo4D, which enables atomic-level cryogenic electron microscopy (cryo-EM) reconstructions of nonequilibrium conformational continuum and reconstitutes hidden dynamics of proteasome autoregulation in the act of substrate degradation. AlphaCryo4D integrates 3D deep residual learning with manifold embedding of free-energy landscapes, which directs 3D clustering via an energy-based particle-voting algorithm. In blind assessments using simulated heterogeneous cryo-EM datasets, AlphaCryo4D achieved 3D classification accuracy three times that of conventional method and reconstructed continuous conformational changes of a 130-kDa protein at sub-3-angstrom resolution. By using AlphaCryo4D to analyze a single experimental cryo-EM dataset, we identified 64 conformers of the substrate-bound human 26S proteasome, revealing conformational entanglement of two regulatory particles in the doubly capped holoenzymes and their energetic differences with singly capped ones. Novel ubiquitin-binding sites are discovered on the RPN2, RPN10 and Alpha5 subunits to remodel polyubiquitin chains for deubiquitylation and recycle. Importantly, AlphaCryo4D choreographs single-nucleotide-exchange dynamics of proteasomal AAA-ATPase motor during translocation initiation, which upregulates proteolytic activity by allosterically promoting nucleophilic attack. Our systemic analysis illuminates a grand hierarchical allostery for proteasome autoregulation.