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| 001 | 638309 | ||
| 005 | 20251119161754.0 | ||
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| 100 | 1 | _ | |a Kloskowski, Patrick |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Nucleotide-bound crystal structures of the SARS-CoV-2 helicase NSP13 |
| 260 | _ | _ | |a Oxford [u.a.] |c 2025 |b Blackwell |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 500 | _ | _ | |a Funding for this research was provided by the DeutscheForschungsgemeinschaft (Germany’s Excellence StrategyEXC 2067/1-390729940 to RF and grant No. INST186/1117 toRF). |
| 520 | _ | _ | |a Nucleotide-bound crystal structures of SARS-CoV-2 NSP13 in ADP- and ATP-bound states were resolved to 1.8 and 1.9 Å, respectively. The ADP-bound model captures a state immediately following ATP hydrolysis, with both ADP and orthophosphate still present in the active site. Further comparative analysis revealed that crystal packing influences NSP13 by stabilizing the nucleotide-binding site, underscoring the importance of accounting for these effects in structure-based drug design targeting NSP13. |
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| 700 | 1 | _ | |a Neumann, Piotr |b 1 |
| 700 | 1 | _ | |a Berndt, Annette |b 2 |
| 700 | 1 | _ | |a Ficner, Ralf |0 P:(DE-H253)PIP1018222 |b 3 |e Corresponding author |
| 773 | _ | _ | |a 10.1107/S2053230X25005266 |g Vol. 81, no. 8, p. 338 - 347 |0 PERI:(DE-600)2175956-X |n 8 |p 338 - 347 |t Acta crystallographica / Section F |v 81 |y 2025 |x 1744-3091 |
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