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Phosphorylation of SAMHD1 Thr592 increases C-terminal domain dynamics, tetramer dissociation and ssDNA binding kinetics
SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 (SAMHD1) is driven into its activated tetramer form by binding of GTP activator and dNTP activators/substrates. In addition, the inactive monomeric and dimeric forms of the enzyme bind to single-stranded (ss) nucleic aci...
Autores principales: | Orris, Benjamin, Huynh, Kevin W, Ammirati, Mark, Han, Seungil, Bolaños, Ben, Carmody, Jason, Petroski, Matthew D, Bosbach, Benedikt, Shields, David J, Stivers, James T |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9303311/ https://www.ncbi.nlm.nih.gov/pubmed/35801923 http://dx.doi.org/10.1093/nar/gkac573 |
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