AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models.
AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models.
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AlphaFold蛋白质结构数据库:通过高精度模型大规模扩展蛋白质序列空间的结构覆盖范围。
DOI:
10.1093/nar/gkab1061
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发表时间:
2022-01-07
影响因子:
14.9
通讯作者:
Velankar S
中科院分区:
文献类型:
--
作者:
Varadi M;Anyango S;Deshpande M;Nair S;Natassia C;Yordanova G;Yuan D;Stroe O;Wood G;Laydon A;Žídek A;Green T;Tunyasuvunakool K;Petersen S;Jumper J;Clancy E;Green R;Vora A;Lutfi M;Figurnov M;Cowie A;Hobbs N;Kohli P;Kleywegt G;Birney E;Hassabis D;Velankar S
The AlphaFold Protein Structure Database (AlphaFold DB, https://alphafold.ebi.ac.uk) is an openly accessible, extensive database of high-accuracy protein-structure predictions. Powered by AlphaFold v2.0 of DeepMind, it has enabled an unprecedented expansion of the structural coverage of the known protein-sequence space. AlphaFold DB provides programmatic access to and interactive visualization of predicted atomic coordinates, per-residue and pairwise model-confidence estimates and predicted aligned errors. The initial release of AlphaFold DB contains over 360,000 predicted structures across 21 model-organism proteomes, which will soon be expanded to cover most of the (over 100 million) representative sequences from the UniRef90 data set. The AlphaFold Protein Structure Database (AlphaFold DB, https://alphafold.ebi.ac.uk) is an extensive, public database of highly accurate protein structure models. The models are the products of AlphaFold2, an Artificial Intelligence algorithm developed by DeepMind. AlphaFold enabled scientists to investigate an unprecedented number of protein structures. The database we describe here provides access to these predicted models and information on their accuracy. The first version of AlphaFold DB contains over 360,000 models of 21 biologically essential species.
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影响因子:
14.9
作者:
Blum M;Chang HY;Chuguransky S;Grego T;Kandasaamy S;Mitchell A;Nuka G;Paysan-Lafosse T;Qureshi M;Raj S;Richardson L;Salazar GA;Williams L;Bork P;Bridge A;Gough J;Haft DH;Letunic I;Marchler-Bauer A;Mi H;Natale DA;Necci M;Orengo CA;Pandurangan AP;Rivoire C;Sigrist CJA;Sillitoe I;Thanki N;Thomas PD;Tosatto SCE;Wu CH;Bateman A;Finn RD
通讯作者:
Finn RD
影响因子:
14.9
作者:
Mistry J;Chuguransky S;Williams L;Qureshi M;Salazar GA;Sonnhammer ELL;Tosatto SCE;Paladin L;Raj S;Richardson LJ;Finn RD;Bateman A
通讯作者:
Bateman A
影响因子:
64.8
作者:
Tunyasuvunakool K;Adler J;Wu Z;Green T;Zielinski M;Žídek A;Bridgland A;Cowie A;Meyer C;Laydon A;Velankar S;Kleywegt GJ;Bateman A;Evans R;Pritzel A;Figurnov M;Ronneberger O;Bates R;Kohl SAA;Potapenko A;Ballard AJ;Romera-Paredes B;Nikolov S;Jain R;Clancy E;Reiman D;Petersen S;Senior AW;Kavukcuoglu K;Birney E;Kohli P;Jumper J;Hassabis D
通讯作者:
Hassabis D
影响因子:
16.6
作者:
Hiranuma N;Park H;Baek M;Anishchenko I;Dauparas J;Baker D
通讯作者:
Baker D
影响因子:
64.8
作者:
Jumper J;Evans R;Pritzel A;Green T;Figurnov M;Ronneberger O;Tunyasuvunakool K;Bates R;Žídek A;Potapenko A;Bridgland A;Meyer C;Kohl SAA;Ballard AJ;Cowie A;Romera-Paredes B;Nikolov S;Jain R;Adler J;Back T;Petersen S;Reiman D;Clancy E;Zielinski M;Steinegger M;Pacholska M;Berghammer T;Bodenstein S;Silver D;Vinyals O;Senior AW;Kavukcuoglu K;Kohli P;Hassabis D
通讯作者:
Hassabis D