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CGK733 was reported as a compound that inhibited ATM/ATR kinase activities and blocked their checkpoint signaling pathways with great selectivity. However, this paper was subsequently retracted, and the truth about the activity of CGK733 remains unclear. We synthesized various analogs of CGK733 with a modification of the carboxylic acid moiety and/or the aniline derivative moiety to accumulate knowledge of the structure-activity relationship of this compound. Growth inhibitory activity of CGK733 and novel 35 analogs against HeLa S3 cells was evaluated, and the structure-activity relationship revealed that analogs with the 2-naphthyl or 4-fluorophenyl group instead of the benzhydryl group have activity comparable to CGK733 and that the 3-nitro group on the aniline moiety significantly affects the activity.Graphical AbstractSynthesis of 35 novel analogs of CGK733 and structure-activity relationship of CGK733.

Streptomycessp. SN-593, a reveromycin producer, was previously thought to belong to the genus Streptomycesbased on its morphological and chemotaxonomic characteristics. In this paper, we re-considered its taxonomic position according to the current criteria. Phylogenetic analysis using 16S rRNA gene sequences showed that the strain belongs to the genus Actinacidiphila. In multilocus sequence and phylogenomic analyses, the strain SN-593 represented a distinct evolutionary lineage within this genus, and its closest neighbor was A. yanglinensis. Digital DNA-DNA hybridization indicated that the strain shares less than 32% DNA-DNA relatedness with the type strains of closely related species, confirming this strain is a novel genomospecies. According to its phenotypic distinctiveness from the closest neighbor, we propose Actinacidiphila reveromycinicasp. nov. for the strain SN-593T. Additionally, as Streptomyces acidipaludisbelonged to the genus Actinacidiphilain these analyses, it should be transferred to the genus, for which Actinacidiphila acidipaludiscomb. nov. is proposed.Graphical AbstractStreptomycessp. SN-593, a reveromycin-producer, was reclassified as a new species of the genus Actinacidiphila, for which the name Actinacidiphila reveromycinicasp. nov. is proposed.

Long-term intake of procyanidins has been suggested to reduce the risk of cardiovascular disease, dementia, and sensory function decline associated with aging. However, most of the ingested procyanidins are not absorbed and are excreted in the feces, so the mechanism of their beneficial impact is unknown. Procyanidins are the components of astringency in plant foods and their stimulation appears to be directly transmitted to the central nervous system via sensory nerves. Recent attention has been focused on the taste receptors expressed in the extra-oral gastrointestinal tract may regulate homeostasis via the neuroendocrine system. In this paper, we have reviewed recent findings on the relationship between the astringency of procyanidins and their bioregulatory effects.Graphical AbstractPossible mechanisms of procyanidin in improving brain function and circulation via TRP channel.

The YggS/PLPBP protein (also called COG0325 or PLPHP) is a conserved pyridoxal 5ʹ-phosphate (PLP)-binding protein present in all 3 domains of life. Recent studies have demonstrated that disruption or mutation of this protein has multifaceted effects in various organisms, including vitamin B6-dependent epilepsy in humans. In Escherichia coli, disruption of this protein—encoded by yggS—perturbs Thr-Ile/Val metabolism, one-carbon metabolism, coenzyme A synthesis, and vitamin B6homeostasis. This protein is critical for maintaining low levels of pyridoxine 5ʹ-phosphate (PNP) in various organisms. In the yggS-deficient E. colistrain, inhibition of PLP-dependent enzymes, such as the glycine cleavage system by PNP, is the root cause of metabolic perturbation. Our data suggest that the YggS/PLPBP protein may be involved in the balancing of B6vitamers by mediating efficient turnover of protein-bound B6vitamers. This paper reviews recent findings on the function of the YggS/PLPBP protein.Graphical AbstractRole of YggS/PLPBP protein in vitamin B6and amino acid homeostasis.