% pubman genre = article
@article{item_3658031,
title = {{Muscle AMP deaminase activity was lower in Neandertals than in modern humans}},
author = {Macak, Dominik and Lee, Shin-Yu and Nyman, Tomas and Ampah-Korsah, Henry and Strandback, Emilia and P{\"a}{\"a}bo, Svante and Zeberg, Hugo},
language = {eng},
issn = {2041-1723},
doi = {10.1038/s41467-025-61605-4},
year = {2025},
abstract = {{The enzyme AMPD1 is expressed in skeletal muscle and is involved in ATP production. All available Neandertal genomes carry a lysine-to-isoleucine substitution at position 287 in AMPD1. This variant, which occurs at an allele frequency of 0{\textendash}8{\textpercent} outside Africa, was introduced to modern humans by gene flow from Neandertals. Here, we show that the catalytic activity of the purified Neandertal AMPD1 is {\textasciitilde}25{\textpercent} lower than the ancestral enzyme, and when introduced in mice, it reduces AMPD activity in muscle extracts by {\textasciitilde}80{\textpercent}. Among present-day Europeans, another AMPD1 variant encoding a stop codon occurs at an allele frequency of 9{\textendash}14{\textpercent}. Individuals heterozygous for this variant are less likely to be top-performing athletes in various sports, but otherwise reduced AMPD1 activity is well tolerated in present-day humans. While being conserved among vertebrates, AMPD1 seems to have become less functionally important among Neandertals and modern humans.}},
journal = {{Nature Communications}},
volume = {16},
eid = {6371},
}