Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection
about
New insights into an X-traordinary viral proteinMechanism of allosteric activation of SAMHD1 by dGTPStructural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolaseIntrinsic host restriction factors of human cytomegalovirus replication and mechanisms of viral escapeStructural basis of lentiviral subversion of a cellular protein degradation pathwayMechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalisThe mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTPFunctional organization of human SAMHD1 and mechanisms of HIV-1 restrictionThe ribonuclease activity of SAMHD1 is required for HIV-1 restrictionGTP activator and dNTP substrates of HIV-1 restriction factor SAMHD1 generate a long-lived activated stateEffects of human SAMHD1 polymorphisms on HIV-1 susceptibility.SAMHD1 specifically affects the antiviral potency of thymidine analog HIV reverse transcriptase inhibitorsdNTP pool modulation dynamics by SAMHD1 protein in monocyte-derived macrophages.Structural basis of cellular dNTP regulation by SAMHD1.SAMHD1 prevents autoimmunity by maintaining genome stability.A continuous enzyme-coupled assay for triphosphohydrolase activity of HIV-1 restriction factor SAMHD1SAMHD1-mediated HIV-1 restriction in cells does not involve ribonuclease activitySAMHD1 is a biomarker for cytarabine response and a therapeutic target in acute myeloid leukemia.Substrates and Inhibitors of SAMHD1.Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.Host factor SAMHD1 restricts DNA viruses in non-dividing myeloid cellsEvolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1.Identification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradationStructure of Escherichia coli dGTP triphosphohydrolase: a hexameric enzyme with DNA effector molecules.SAMHD1 specifically restricts retroviruses through its RNase activity.Phospho-dependent Regulation of SAMHD1 Oligomerisation Couples Catalysis and Restriction.CyclinA2-Cyclin-dependent Kinase Regulates SAMHD1 Protein Phosphohydrolase Domain.SAMHD1 is a single-stranded nucleic acid binding protein with no active site-associated nuclease activityImpaired dNTPase activity of SAMHD1 by phosphomimetic mutation of Thr-592The SAMHD1 dNTP Triphosphohydrolase Is Controlled by a Redox Switch.Structural Insights into the High-efficiency Catalytic Mechanism of the Sterile α-Motif/Histidine-Aspartate Domain-containing Protein.Heterozygous colon cancer-associated mutations of SAMHD1 have functional significanceThe Cleavage and Polyadenylation Specificity Factor 6 (CPSF6) Subunit of the Capsid-recruited Pre-messenger RNA Cleavage Factor I (CFIm) Complex Mediates HIV-1 Integration into Genes.Restrictive influence of SAMHD1 on Hepatitis B Virus life cycle.HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradationInterferon regulatory factor 3 is a key regulation factor for inducing the expression of SAMHD1 in antiviral innate immunity.Deoxynucleoside triphosphate (dNTP) synthesis and destruction regulate the replication of both cell and virus genomes.Effects of T592 phosphomimetic mutations on tetramer stability and dNTPase activity of SAMHD1 can not explain the retroviral restriction defect.Restriction of virus infection but not catalytic dNTPase activity is regulated by phosphorylation of SAMHD1.Antagonism of SAMHD1 is actively maintained in natural infections of simian immunodeficiency virus
P2860
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P2860
Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection
description
2013 nî lūn-bûn
@nan
2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@ast
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@en
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@nl
type
label
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@ast
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@en
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@nl
prefLabel
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@ast
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@en
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@nl
P2093
P2860
P3181
P356
P1476
Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection
@en
P2093
Chuanping Wang
Jacek Skowronski
Jennifer Mehrens
Jinwoo Ahn
Junpeng Yan
Marcin Golczak
Maria DeLucia
Sarabpreet Kaur
P2860
P304
P3181
P356
10.1074/JBC.M112.443796
P407
P577
2013-04-12T00:00:00Z