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Phosphorylation of SAMHD1 Thr592 increases C-terminal domain dynamics, tetramer dissociation, and ssDNA binding kinetics

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.04.05.486416Source: DataRank Database

Phosphorylation of SAMHD1 Thr592 increases C-terminal domain dynamics, tetramer dissociation, and ssDNA binding kinetics is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2022). On theSindex it has a DataRank of 0.

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (3 grants)OA: greenTopics (28)IDs (PubMed, OpenAlex)

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Authors (10)

Kevin W. Huynh ORCID,Mark Ammirati ORCID,Seungil Han ORCID,Ben Bolaños ORCID,Jason Carmody ORCID

Live enrichment

PubMed:19965766 OpenAlex:https://openalex.org/W4226290024

National Institutes of Health

Grant: 2T32CA009110-21

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCH

National Institutes of Health

Grant: 5R01CA233567-04

Discovery of Chemical Probes of SAMHD1 for Modulation of Cancer Therapy and the Immune System

National Institutes of Health

Grant: 5R01GM056834-02

MECHANISMS AND TRANSITION STATES FOR DNA GLYCOSYLASES

greenLicense: CC BY NC

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2022/04/06/2022.04.05.486416.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2022.04.05.486416

repositoryhttps://doi.org/10.1101/2022.04.05.486416

https://doi.org/10.1093/nar/gkac573

Fields of Study

DNA Repair MechanismsDNA and Nucleic Acid ChemistryRNA Research and Splicing0301 basic medicine0303 health sciences03 medical and health sciences

Keywords

TetramerPhosphorylationSAMHD1ChemistryDimerBiophysicsTrimerDNA replicationDNABinding domainBinding siteStereochemistryEnzymeBiochemistryBiologyRNASAM Domain and HD Domain-Containing Protein 1KineticsNucleic Acid EnzymesDNA, Single-StrandedGuanosine TriphosphateMonomeric GTP-Binding Proteins