A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
about
Structure and expression of the TREX1 and TREX2 3' --> 5' exonuclease genesExcision of 3' termini by the Trex1 and TREX2 3'-->5' exonucleases. Characterization of the recombinant proteinsDeficiency in 3'-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1)A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathwaysTrex1 prevents cell-intrinsic initiation of autoimmunityEarly steps in the DNA base excision/single-strand interruption repair pathway in mammalian cellsAicardi-Goutieres syndrome and related phenotypes: linking nucleic acid metabolism with autoimmunityBiochemical and cellular characteristics of the 3' -> 5' exonuclease TREX2The Werner syndrome protein operates in base excision repair and cooperates with DNA polymerase beta.RPA and Rad51 constitute a cell intrinsic mechanism to protect the cytosol from self DNAThe crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partneringStructure of the dimeric exonuclease TREX1 in complex with DNA displays a proline-rich binding site for WW DomainsDefects in DNA degradation revealed in crystal structures of TREX1 exonuclease mutations linked to autoimmune diseaseMutations in the gene encoding the 3'-5' DNA exonuclease TREX1 cause Aicardi-Goutières syndrome at the AGS1 locusThe human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysisAicardi-Goutieres syndrome gene and HIV-1 restriction factor SAMHD1 is a dGTP-regulated deoxynucleotide triphosphohydrolase.The SET complex acts as a barrier to autointegration of HIV-1New roles for the major human 3'-5' exonuclease TREX1 in human disease.The Arg-62 residues of the TREX1 exonuclease act across the dimer interface contributing to catalysis in the opposing protomers.RNaseH2 mutants that cause Aicardi-Goutieres syndrome are active nucleasesIdentification and cloning of Kidins220, a novel neuronal substrate of protein kinase D.Evidence for extrinsic exonucleolytic proofreading.Base excision repair in a network of defence and tolerance.Simple and convenient G-quadruplex-based turn-on fluorescence assay for 3' → 5' exonuclease activity.The 3'-5' DNA exonuclease TREX1 directly interacts with poly(ADP-ribose) polymerase-1 (PARP1) during the DNA damage response.Gaining a foothold: how HIV avoids innate immune recognition.Functional consequences of the RNase H2A subunit mutations that cause Aicardi-Goutieres syndrome.HIV DNA is heavily uracilated, which protects it from autointegrationRepair of endogenous DNA damage.The exonuclease activity of hPMC2 is required for transcriptional regulation of the QR gene and repair of estrogen-induced abasic sitesDominant 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.Aspects of innate immunity in Sjögren's syndrome.The TREX1 exonuclease R114H mutation in Aicardi-Goutières syndrome and lupus reveals dimeric structure requirements for DNA degradation activity.Gene-targeted mice lacking the Trex1 (DNase III) 3'-->5' DNA exonuclease develop inflammatory myocarditis.Heterozygous mutations in TREX1 cause familial chilblain lupus and dominant Aicardi-Goutieres syndrome.Human DNA Exonuclease TREX1 Is Also an Exoribonuclease That Acts on Single-stranded RNA.WRN exonuclease activity is blocked by DNA termini harboring 3' obstructive groups.Identification and characterization of the novel nuclease activity of human phospholipid scramblase 1The role of DNA exonucleases in protecting genome stability and their impact on ageing.
P2860
Q24291021-5C113E19-248A-4BA0-A963-9848C2E53555Q24291054-6C5B4F0B-C0A0-47BF-AAD6-1B6772758060Q24557437-80C9BD0D-5248-4D1A-8475-AB0C42E0FB68Q24594082-B1D83DD4-F032-41DA-8872-BCA988B8CBDEQ24648757-AFC1488D-16CF-4CF9-895A-D1CC8D83B9D1Q24650179-F1C5405F-D504-4E61-A64F-35074BA63359Q24655886-7AA322E9-970E-42E4-9358-603D1186605BQ24677826-093FB973-2952-468A-90D2-C567A1040923Q25257806-2E1DEB45-BB0D-4372-A88F-1B557B0A1EB6Q27314893-6E3FBC25-24A2-465B-987D-D60A327B4419Q27643804-85BA28A7-D576-4A19-8142-5DEF41D17FD1Q27644048-6D8DA449-3AF3-4B86-B376-8A187A4E69ACQ27675483-F8C85503-E426-46CF-9019-F19140688C49Q28252435-E9DEFF07-5D6A-401A-A412-6843E20F93CAQ28303398-F42F00C6-E0C8-4A25-89DB-01CDD4D3C76DQ29871440-74424A12-188A-42D0-8AD1-89E01EFD2E13Q33415459-FC11DAA1-0CB8-47A4-B7CD-7149959DF243Q33671295-61FD9D6C-5171-4158-8C7E-011FAAEF08D8Q33676423-A1E6CD43-372B-4E38-B00F-EC54F64BDF8EQ33779326-3F654516-DD63-44A7-8956-7CBD0166C334Q33918643-6B6C5AB4-8905-43C4-9305-06AAF63DC93DQ34010452-04CD6AB5-225A-4F92-903C-BD7FAF4FE22DQ34283911-B59E5838-BDC7-4831-9DDC-42D775EB0F44Q34494171-65E5EADC-0139-45BA-8883-63CAD2312CFFQ34552582-7E87D5C9-4789-4C07-9A27-7FB21696D417Q34590321-79C34D93-5383-41B1-B866-FDAD582F1F4EQ34947859-C5AB1D82-0FD5-42BF-A7D0-BF58627FF44BQ35022023-D2006018-515C-482B-8D54-E4B66EB3678FQ35132488-A1EF10AA-76C0-4442-A488-8623DD4CD50FQ35179559-291C3A28-AD79-4100-97CB-F4E41A1BBED9Q35213485-724DF491-2934-4D37-A871-7DFF0612BA4AQ35549308-4BE36471-8CD7-444D-B8E5-19434C83681EQ35557792-4BCBBA3C-B6FA-4296-A83B-0CB244D3F490Q35562735-2476187F-8E25-49EE-B7A2-2D15DC9819DEQ35663520-EDF59ABD-DEF1-48BA-A974-D55689381EA4Q35752487-32D3BD16-C525-4B09-BDDD-C76583ED7112Q35860984-2367C570-C03E-4989-8BC3-C023ED20D2F0Q35895249-1502CC82-9EFE-4AA0-BD33-3175EB23BE87Q36024272-24345DD8-A007-45A3-9283-09E5112F4782Q36483126-DFC3C083-9239-47AC-B220-2DC03705549E
P2860
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein
@nl
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@ast
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@en
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@en-gb
type
label
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein
@nl
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@ast
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@en
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@en-gb
prefLabel
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein
@nl
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@ast
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@en
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@en-gb
P2093
P921
P3181
P356
P1433
P1476
A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein.
@en
P2093
P304
P3181
P356
10.1093/EMBOJ/18.13.3868
P407
P577
1999-07-01T00:00:00Z