The TREX1 double-stranded DNA degradation activity is defective in dominant mutations associated with autoimmune disease. - Wikidata - wikimedia - TriplyDB

The TREX1 double-stranded DNA degradation activity is defective in dominant mutations associated with autoimmune disease.

The TREX1 double-stranded DNA degradation activity is defective in dominant mutations associated with autoimmune disease.

http://www.wikidata.org/entity/Q42151409

about

Aicardi-Goutieres syndrome and related phenotypes: linking nucleic acid metabolism with autoimmunity Cap binding and immune evasion revealed by Lassa nucleoprotein structure Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation Defects in DNA degradation revealed in crystal structures of TREX1 exonuclease mutations linked to autoimmune disease Structures of Arenaviral Nucleoproteins with Triphosphate dsRNA Reveal a Unique Mechanism of Immune Suppression Recognition and processing of double-stranded DNA by ExoX, a distributive 3'-5' exonuclease Cytoplasmic DNA innate immune pathways Aicardi-Goutieres syndrome gene and HIV-1 restriction factor SAMHD1 is a dGTP-regulated deoxynucleotide triphosphohydrolase.Aicardi-Goutières syndrome protein TREX1 suppresses L1 and maintains genome integrity through exonuclease-independent ORF1p depletion The Arg-62 residues of the TREX1 exonuclease act across the dimer interface contributing to catalysis in the opposing protomers.Genetic factors predisposing to systemic lupus erythematosus and lupus nephritis.A genomic approach to human autoimmune diseases.RNaseH2 mutants that cause Aicardi-Goutieres syndrome are active nucleases The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1.Simple and convenient G-quadruplex-based turn-on fluorescence assay for 3' → 5' exonuclease activity.Functional consequences of the RNase H2A subunit mutations that cause Aicardi-Goutieres syndrome.Evaluation of the TREX1 gene in a large multi-ancestral lupus cohort Dominant mutation of the TREX1 exonuclease gene in lupus and Aicardi-Goutieres syndrome.Exonuclease TREX1 degrades double-stranded DNA to prevent spontaneous lupus-like inflammatory disease.The TREX1 exonuclease R114H mutation in Aicardi-Goutières syndrome and lupus reveals dimeric structure requirements for DNA degradation activity.Human DNA Exonuclease TREX1 Is Also an Exoribonuclease That Acts on Single-stranded RNA.Chromothripsis and Kataegis Induced by Telomere Crisis ExoMeg1: a new exonuclease from metagenomic library.Cytosolic Nuclease TREX1 Regulates Oligosaccharyltransferase Activity Independent of Nuclease Activity to Suppress Immune Activation Multifaceted role of TREX2 in the skin defense against UV-induced skin carcinogenesis.Genetics of SLE: functional relevance for monocytes/macrophages in disease TREX1 acts in degrading damaged DNA from drug-treated tumor cells.DNA binding induces active site conformational change in the human TREX2 3'-exonuclease The TREX1 C-terminal region controls cellular localization through ubiquitination.Rare variants in the TREX1 gene and susceptibility to autoimmune diseases Early onset of autoimmune disease by the retroviral integrase inhibitor raltegravir.Rheumatic manifestations of skin disease.Endogenous retroelements and autoimmune disease.Pathogenesis of cutaneous lupus erythematosus: common and different features in distinct subsets.Human disease phenotypes associated with mutations in TREX1.Towards precision radiotherapy for use with immune checkpoint blockers.Restriction of Human Cytomegalovirus Replication by ISG15, a Host Effector Regulated by cGAS-STING Double-Stranded-DNA Sensing.Luminescent Strategies for Label-free G-quadruplex-based Enzyme Activity Sensing.Different mutations in three prime repair exonuclease 1 and ribonuclease H2 genes affect clinical features in Aicardi-Goutieres syndrome.A nationwide survey of Aicardi-Goutières syndrome patients identifies a strong association between dominant TREX1 mutations and chilblain lesions: Japanese cohort study.

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P2860

The TREX1 double-stranded DNA degradation activity is defective in dominant mutations associated with autoimmune disease.

http://www.wikidata.org/entity/Q42151409

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

The TREX1 double-stranded DNA ...... iated with autoimmune disease.

@en

The TREX1 double-stranded DNA ...... iated with autoimmune disease.

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type

label

The TREX1 double-stranded DNA ...... iated with autoimmune disease.

@en

The TREX1 double-stranded DNA ...... iated with autoimmune disease.

@nl

prefLabel

The TREX1 double-stranded DNA ...... iated with autoimmune disease.

@en

The TREX1 double-stranded DNA ...... iated with autoimmune disease.

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

The TREX1 double-stranded DNA ...... ciated with autoimmune disease

@en

P2093

Duane A Lehtinen

http://www.w3.org/2001/XMLSchema#string

Fred W Perrino

http://www.w3.org/2001/XMLSchema#string

Scott Harvey

http://www.w3.org/2001/XMLSchema#string

Thomas Hollis

http://www.w3.org/2001/XMLSchema#string

P2860

Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3'-->5' exonucleases

A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.

Structure and expression of the TREX1 and TREX2 3' --> 5' exonuclease genes

Excision of 3' termini by the Trex1 and TREX2 3'-->5' exonucleases. Characterization of the recombinant proteins

Trex1 prevents cell-intrinsic initiation of autoimmunity

Clinical and molecular phenotype of Aicardi-Goutieres syndrome

The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering

Structure of the dimeric exonuclease TREX1 in complex with DNA displays a proline-rich binding site for WW Domains

The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death

Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 cause Aicardi-Goutières syndrome at the AGS1 locus

P304

31649-31656

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scholarly article

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10.1074/JBC.M806155200

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46

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283

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Matthew Mulcahy

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2008-09-18T00:00:00Z

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18805785

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2581595

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