Results 211 to 220 of about 131,570 (298)
Pyridoxal 5′‐phosphate (PLP) homeostasis relies on salvage enzymes, yet key metabolic branches remain undefined. We identify AKR1C isozymes as previously undescribed contributors that convert pyridoxal into pyridoxine or 4‐pyridoxolactone through reductase and dehydrogenase activities.
Nayu Kito +8 more
wiley +1 more source
Human IDO2 exhibits unique binding affinities distinct to those of human IDO1
Although indoleamine 2,3‐dioxygenase 2 (IDO2) is highly homologous to IDO1, it displays markedly lower catalytic activity. We found that IDO2 binds L‐tryptophan (L‐Trp) in a flipped orientation stabilized by the IDO2‐specific residue His143. Replacement of His143 with the IDO1‐equivalent tyrosine restored an IDO1‐like binding mode and increased ...
Shunsuke Nogi +8 more
wiley +1 more source
Coordinating Calvin Cycle and Glycolysis in <i>Escherichia coli</i>. [PDF]
Lin YJ, Chen HT, Lin PY, Lai YJ, Li SY.
europepmc +1 more source
Human RNase 7 is known to exert antimicrobial activity in epithelial tissues. Here, using SH‐SY5Y and U‐87 MG, neuroblastoma and glioblastoma cell lines, respectively, we found that RNase 7 enhances immune responses to LPS stimulation by reducing the expression of pro‐inflammatory cytokines, nitric oxide, and ROS.
Rosanna Culurciello +9 more
wiley +1 more source
Reprogrammed SimCells for antimicrobial therapy. [PDF]
Dong Y +6 more
europepmc +1 more source
KU80 suppresses endonuclease G activity to preserve genomic integrity
Under normal conditions, EndoG remains restricted to mitochondria and the genome remains intact. When KU80 is absent, EndoG translocates into the nucleus, where it promotes DNA fragmentation and genomic instability. Thus, this work highlights the importance of KU80 in tightly controlling EndoG localization to preserve genome stability.
Jargalan Batsaikhan +8 more
wiley +1 more source
Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent. [PDF]
Abdelrazek NA +4 more
europepmc +1 more source
Human NAD(P)H:quinone oxidoreductase 1 is a homodimeric flavoenzyme crucial for redox metabolism and linked to significant health issues. Point mutations at Tyr126 and Tyr128 demonstrate their essential roles in optimizing substrate binding geometry for catalysis, as well as in half‐site reactivity and conformational dynamics during the enzyme's ...
Maribel Rivero +8 more
wiley +1 more source
Insights into the Performance of CusF as a Solubility Tag for Recombinant Protein Expression. [PDF]
Oscorbin IP +3 more
europepmc +1 more source

