RECONSTRUCTING RETINAL VISUAL IMAGES FROM 3T FMRI DATA ENHANCED BY UNSUPERVISED LEARNING.

The reconstruction of human visual inputs from brain activity, particularly through functional Magnetic Resonance Imaging (fMRI), holds promising avenues for unraveling the mechanisms of the human visual system. Despite the significant strides made by deep learning methods in improving the quality and interpretability of visual reconstruction, there remains a substantial demand for high-quality, long-duration, subject-specific 7-Tesla fMRI experiments. The challenge arises in integrating diverse smaller 3-Tesla datasets or accommodating new subjects with brief and low-quality fMRI scans.

Polyamine regulation of porcine reproductive and respiratory syndrome virus infection depends on spermidine-spermine acetyltransferase 1.

Like obligate intracellular parasites, viruses co-opt host cell resources to establish productive infections. Polyamines are key aliphatic molecules that perform important roles in cellular growth and proliferation. They are also needed for the successful multiplication of various viruses.

and double-knockout pigs are resistant to PRRSV and TGEV and exhibit decreased susceptibility to PDCoV while maintaining normal production performance.

Porcine reproductive and respiratory syndrome virus (PRRSV) and transmissible gastroenteritis virus (TGEV) are two highly infectious and lethal viruses causing major economic losses to pig production. Here, we report generation of double-gene-knockout (DKO) pigs harboring edited knockout alleles for known receptor proteins CD163 and pAPN and show that DKO pigs are completely resistant to genotype 2 PRRSV and TGEV. We found no differences in meat-production or reproductive-performance traits between wild-type and DKO pigs, but detected increased iron in DKO muscle.

Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association.

Sec1/Munc18-family (SM) proteins are required for SNARE-mediated membrane fusion, but their mechanism(s) of action remain controversial. Using single-molecule force spectroscopy, we found that the SM protein Munc18-1 catalyzes step-wise zippering of three synaptic SNAREs (syntaxin, VAMP2, and SNAP-25) into a four-helix bundle. Catalysis requires formation of an intermediate template complex in which Munc18-1 juxtaposes the N-terminal regions of the SNARE motifs of syntaxin and VAMP2, while keeping their C-terminal regions separated.