@article{oai:oist.repo.nii.ac.jp:00002168,
 author = {Stepanova, Vita and Moczulska, Kaja Ewa and Vacano, Guido N and Kurochkin, Ilia and Ju, Xiangchun and Riesenberg, Stephan and Macak, Dominik and Maricic, Tomislav and Dombrowski, Linda and Schörnig, Maria and Anastassiadis, Konstantinos and Baker, Oliver and Naumann, Ronald and Khrameeva, Ekaterina and Vanushkina, Anna and Stekolshchikova, Elena and Egorova, Alina and Tkachev, Anna and Mazzarino, Randall and Duval, Nathan and Zubkov, Dmitri and Giavalisco, Patrick and Wilkinson, Terry G and Patterson, David and Khaitovich, Philipp and Pääbo, Svante},
 journal = {eLife},
 month = {May},
 note = {We analyze the metabolomes of humans, chimpanzees, and macaques in muscle, kidney and three different regions of the brain. Although several compounds in amino acid metabolism occur at either higher or lower concentrations in humans than in the other primates, metabolites downstream of adenylosuccinate lyase, which catalyzes two reactions in purine synthesis, occur at lower concentrations in humans. This enzyme carries an amino acid substitution that is present in all humans today but absent in Neandertals. By introducing the modern human substitution into the genomes of mice, as well as the ancestral, Neandertal-like substitution into the genomes of human cells, we show that this amino acid substitution contributes to much or all of the reduction of de novo synthesis of purines in humans.},
 title = {Reduced purine biosynthesis in humans after their divergence from Neandertals},
 volume = {10},
 year = {2021}
}