Compression for Bayer CFA Images: Review and Performance Comparison.

Bayer color filter array (CFA) images are captured by a single-chip image sensor covered with a Bayer CFA pattern which has been widely used in modern digital cameras. In the past two decades, many compression methods have been proposed to compress Bayer CFA images. These compression methods can be roughly divided into the compression-first-based (CF-based) scheme and the demosaicing-first-based (DF-based) scheme. However, in the literature, no review article for the two compression schemes and their compression performance is reported. In this article, the related CF-based and DF-based compression works are reviewed first. Then, the testing Bayer CFA images created from the Kodak, IMAX, screen content images, videos, and classical image datasets are compressed on the Joint Photographic Experts Group-2000 (JPEG-2000) and the newly released Versatile Video Coding (VVC) platform VTM-16.2. In terms of the commonly used objective quality, perceptual quality metrics, the perceptual effect, and the quality-bitrate tradeoff metric, the compression performance comparison of the CF-based compression methods, in particular the reversible color transform-based compression methods and the DF-based compression methods, is reported and discussed.

A Few Charged Residues in Galectin-3's Folded and Disordered Regions Regulate Phase Separation.

Proteins with intrinsically disordered regions (IDRs) often undergo phase separation to control their functions spatiotemporally. Changing the pH alters the protonation levels of charged sidechains, which in turn affects the attractive or repulsive force for phase separation. In a cell, the rupture of membrane-bound compartments, such as lysosomes, creates an abrupt change in pH. However, how proteins' phase separation reacts to different pH environments remains largely unexplored. Here, using extensive mutagenesis, NMR spectroscopy, and biophysical techniques, it is shown that the assembly of galectin-3, a widely studied lysosomal damage marker, is driven by cation-π interactions between positively charged residues in its folded domain with aromatic residues in the IDR in addition to π-π interaction between IDRs. It is also found that the sole two negatively charged residues in its IDR sense pH changes for tuning the condensation tendency. Also, these two residues may prevent this prion-like IDR domain from forming rapid and extensive aggregates. These results demonstrate how cation-π, π-π, and electrostatic interactions can regulate protein condensation between disordered and structured domains and highlight the importance of sparse negatively charged residues in prion-like IDRs.