Varaico: Literature-Extracted Genetic Variants

Gene:SAMHD1
Variant:p.H206R
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SAMHD1

NM_015474.4:p.H206R

Associated Papers

Biochemical functions and structure of Caenorhabditis elegans ZK177.8 protein: Aicardi-Goutières syndrome SAMHD1 dNTPase ortholog.

Maehigashi T et al.

The Journal of Biological Chemistry, 2023

SAMHD1 in cancer: curse or cure?

Schott K et al.

Journal of Molecular Medicine (berlin, Germany), 2022

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

Crystal structures of SAMHD1 inhibitor complexes reveal the mechanism of water-mediated dNTP hydrolysis.

Morris ER et al.

Nature Communications, 2020

The dNTPase activity of SAMHD1 is important for its suppression of innate immune responses in differentiated monocytic cells.

Qin Z et al.

The Journal of Biological Chemistry, 2020

Structural characterization and directed modification of Sus scrofa SAMHD1 reveal the mechanism underlying deoxynucleotide regulation.

Kong J et al.

The Febs Journal, 2019

The missing link: allostery and catalysis in the anti-viral protein SAMHD1.

Morris ER et al.

Biochemical Society Transactions, 2019

A Cyclin-Binding Motif in Human SAMHD1 Is Required for Its HIV-1 Restriction, dNTPase Activity, Tetramer Formation, and Efficient Phosphorylation.

St Gelais C et al.

Journal of Virology, 2018

A Putative Cyclin-binding Motif in Human SAMHD1 Contributes to Protein Phosphorylation, Localization, and Stability.

St Gelais C et al.

The Journal of Biological Chemistry, 2016

Impaired dNTPase activity of SAMHD1 by phosphomimetic mutation of Thr-592.

Tang C et al.

The Journal of Biological Chemistry, 2015

Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.

Koharudin LM et al.

The Journal of Biological Chemistry, 2014

SAMHD1 is mutated recurrently in chronic lymphocytic leukemia and is involved in response to DNA damage.

Clifford R et al.

Blood, 2014

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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."