Associated Papers
Accurate affinity models for SH2 domains from peptide binding assays and free-energy regression.
Gagoski D et al.
Protein Science : a Publication of the Protein Society, 2025
41088778 (PubMed )
Supplement: PRO-34-e70317-s008.xlsx › _S6_-_PTMVar_-_Lyn
Accurate sequence-to-affinity models for SH2 domains from multi-round peptide binding assays coupled with free-energy regression.
Gagoski D et al.
Biorxiv : the Preprint Server for Biology, 2025
39764007 (PubMed )
Supplement: media-1.xlsx › _S6_-_PTMVar_-_Lyn
SAMHD1 in cancer: curse or cure?
Schott K et al.
Journal of Molecular Medicine (berlin, Germany), 2022
34480199 (PubMed )
Supplement: 109_2021_2131_MOESM1_ESM.xlsx › Tabelle1
Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins.
Bowen NE et al.
The Journal of Biological Chemistry, 2021
Dual roles of SAMHD1 in tumor development and chemoresistance to anticancer drugs.
Chen Z et al.
Oncology Letters, 2021
Defective modulation of LINE-1 retrotransposition by cancer-associated SAMHD1 mutants.
Gao W et al.
Biochemical and Biophysical Research Communications, 2019
Molecular dynamics characterization of the SAMHD1 Aicardi-Goutières Arg145Gln mutant: structural determinants for the impaired tetramerization.
Cardamone F et al.
Journal of Computer-aided Molecular Design, 2018
Uncovering allostery and regulation in SAMHD1 through molecular dynamics simulations.
Patra KK et al.
Proteins, 2017
A SAMHD1 mutation associated with Aicardi-Goutières syndrome uncouples the ability of SAMHD1 to restrict HIV-1 from its ability to downmodulate type I interferon in humans.
White TE et al.
Human Mutation, 2017
Characterization of human disease phenotypes associated with mutations in TREX1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, ADAR, and IFIH1.
Crow YJ et al.
American Journal of Medical Genetics. Part A, 2015
25604658 (PubMed )
Supplement: supplement_1.docx
SAMHD1 is mutated recurrently in chronic lymphocytic leukemia and is involved in response to DNA damage.
Clifford R et al.
Blood, 2014
Mechanism of allosteric activation of SAMHD1 by dGTP.
Ji X et al.
Nature Structural & Molecular Biology, 2013
SAMHD1 is a nucleic-acid binding protein that is mislocalized due to aicardi-goutières syndrome-associated mutations.
Goncalves A et al.
Human Mutation, 2012
HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase.
Goldstone DC et al.
Nature, 2011
Mutations involved in Aicardi-Goutières syndrome implicate SAMHD1 as regulator of the innate immune response.
Rice GI et al.
Nature Genetics, 2009
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