Unannotated Open Reading Frame in Encodes Protein Localizing to the Endoplasmic Reticulum.

There are thousands of unannotated translated open reading frames (ORFs) in the genome. Previous investigation into one such unannotated ORF, which was systemically labeled YGR016C-A based on its genomic coordinates, showed that replacing the ORF's ATG start codon with AAG led to a change in cellular fitness under different stress conditions (Wacholder et al., 2023).

Control of electronic topology in a strongly correlated electron system.

It is becoming increasingly clear that breakthrough in quantum applications necessitates materials innovation. In high demand are conductors with robust topological states that can be manipulated at will. This is what we demonstrate in the present work.

Optimizing the PBS1 Decoy System to Confer Resistance to Potyvirus Infection in and Soybean.

The resistance protein RPS5 is activated by proteolytic cleavage of the protein kinase PBS1 by the effector protease AvrPphB. We have previously shown that replacing seven amino acids at the cleavage site of PBS1 with a motif cleaved by the NIa protease of turnip mosaic virus (TuMV) enables RPS5 activation upon TuMV infection. However, this engineered resistance conferred a trailing necrosis phenotype indicative of a cell-death response too slow to contain the virus.

Electron Trapping Mechanism in LaAlO_{3}/SrTiO_{3} Heterostructures.

In LaAlO_{3}/SrTiO_{3} heterostructures, a still poorly understood phenomenon is that of electron trapping in back-gating experiments. Here, by combining magnetotransport measurements and self-consistent Schrödinger-Poisson calculations, we obtain an empirical relation between the amount of trapped electrons and the gate voltage. The amount of trapped electrons decays exponentially away from the interface.

Reactivation of Epstein-Barr virus by a dual-responsive fluorescent EBNA1-targeting agent with Zn-chelating function.

Epstein-Barr nuclear antigen 1 (EBNA1) plays a vital role in the maintenance of the viral genome and is the only viral protein expressed in nearly all forms of Epstein-Barr virus (EBV) latency and EBV-associated diseases, including numerous cancer types. To our knowledge, no specific agent against EBV genes or proteins has been established to target EBV lytic reactivation. Here we report an EBNA1- and Zn-responsive probe (ZRLP) which alone could reactivate the EBV lytic cycle through specific disruption of EBNA1.