Substitution of Asp-210 in HAP1 (APE/Ref-1) eliminates endonuclease activity but stabilises substrate binding.
about
Biochemical characterization of human tyrosyl-DNA phosphodiesterase 2 (TDP2/TTRAP): a Mg(2+)/Mn(2+)-dependent phosphodiesterase specific for the repair of topoisomerase cleavage complexesCleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme AXRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactionsUracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanismsTotal sequence decomposition distinguishes functional modules, "molegos" in apurinic/apyrimidinic endonucleasesAP endonuclease paralogues with distinct activities in DNA repair and bacterial pathogenesisConserved Structural Chemistry for Incision Activity in Structurally Non-homologous Apurinic/Apyrimidinic Endonuclease APE1 and Endonuclease IV DNA Repair EnzymesStructure of human apurinic/apyrimidinic endonuclease 1 with the essential Mg2+cofactorRole of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1A quantitative model of human DNA base excision repair. I. Mechanistic insights.Unusual role of a cysteine residue in substrate binding and activity of human AP-endonuclease 1.Mutations in the alpha8 loop of human APE1 alter binding and cleavage of DNA containing an abasic site.Reconstitution of the base excision repair pathway for 7,8-dihydro-8-oxoguanine with purified human proteinsMechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: bypass of the AP lyase activity stepStructural insights by molecular dynamics simulations into specificity of the major human AP endonuclease toward the benzene-derived DNA adduct, pBQ-C.Effect of protein binding on ultrafast DNA dynamics: characterization of a DNA:APE1 complex.High-resolution crystal structures reveal plasticity in the metal binding site of apurinic/apyrimidinic endonuclease I.B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil.Formation and repair of tobacco carcinogen-derived bulky DNA adductsIdentification of a residue critical for the excision of 3'-blocking ends in apurinic/apyrimidinic endonucleases of the Xth family.Transient-state kinetics of apurinic/apyrimidinic (AP) endonuclease 1 acting on an authentic AP site and commonly used substrate analogs: the effect of diverse metal ions and base mismatches.Heat shock protein 70 binds to human apurinic/apyrimidinic endonuclease and stimulates endonuclease activity at abasic sites.The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease.MD simulation and experimental evidence for Mg²+ binding at the B site in human AP endonuclease 1.Human apurinic/apyrimidinic endonuclease (Ape1) and its N-terminal truncated form (AN34) are involved in DNA fragmentation during apoptosis.The exonuclease activity of human apurinic/apyrimidinic endonuclease (APE1). Biochemical properties and inhibition by the natural dinucleotide Gp4G.A genetic variation in APE1 is associated with gastric cancer survival in a Chinese population.Chinese hamster AP endonuclease operates by a two-metal ion assisted catalytic mechanism.
P2860
Q24294083-4606706A-5E83-4828-ACBC-03B572C40E9FQ24338600-2BF57BBA-E1CD-4EF5-A564-61C45F3876E7Q24535921-9E1A9F9D-B742-4912-91B2-1F1A2635A484Q24672089-0780FFC0-111C-4E3D-9B2F-59526C214080Q24797920-98048354-0B51-49DC-BC27-76CAF909675FQ27643887-296B0285-5537-4FA0-9E14-D2601C03492EQ27676022-AD8FC018-D7E3-423A-944F-F367A80B9D48Q27680779-16CF49FA-6561-464A-9D4A-38225D9FA8C7Q28203088-B5F515D0-4DBC-49B3-A278-8999EC958293Q28646701-5EE660F2-E8C1-4AC2-9958-39E9B22D72BCQ30439240-857A0DC0-C9AA-4F8F-8F85-CD63B7503E43Q31156442-ADFDAE13-4B20-4080-9AFF-54BC8955AD7FQ33857767-B34D21B1-0F76-459D-9409-3FD05975185EQ34286685-45C6F43E-D948-456B-A75B-08EA1DE05825Q34333638-8A66AC48-968D-4088-823D-6EA3053078AFQ34352534-1486D879-8517-497A-9401-6686471BD921Q34379637-DC0291AE-C9FD-4657-9885-0DB7AEAA2D40Q34427857-62EE4FFE-E1E1-4955-9EA8-5CDB94B6090BQ34475702-DF724BCA-1572-4580-803D-06BE3EC9E106Q37149762-2A6FD14A-B9A8-4E95-B72B-804C7B24E044Q37385029-1CBC01FC-134F-4271-B114-3C5D54736EB8Q38304998-DEB2591C-52A6-4089-9001-E007EF14E37BQ39115723-C45DBD09-4120-4CE6-B91B-951E7ED80288Q39175286-DDD3FC5E-42BD-4AA8-83A8-685581A33C64Q42169230-0FEFA607-44C4-44FD-952A-8552D053F5AFQ44353890-D48C3B95-4925-45D3-B4C2-054DF0756849Q45220062-34B2CDC0-62D6-4F95-9822-DB01A0C183CBQ50505059-0F41B2F9-98AB-4F5D-A56D-909B12B98340
P2860
Substitution of Asp-210 in HAP1 (APE/Ref-1) eliminates endonuclease activity but stabilises substrate binding.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Substitution of Asp-210 in HAP ...... stabilises substrate binding.
@ast
Substitution of Asp-210 in HAP ...... stabilises substrate binding.
@en
type
label
Substitution of Asp-210 in HAP ...... stabilises substrate binding.
@ast
Substitution of Asp-210 in HAP ...... stabilises substrate binding.
@en
prefLabel
Substitution of Asp-210 in HAP ...... stabilises substrate binding.
@ast
Substitution of Asp-210 in HAP ...... stabilises substrate binding.
@en
P2093
P2860
P356
P1476
Substitution of Asp-210 in HAP ...... t stabilises substrate binding
@en
P2093
P2860
P304
P356
10.1093/NAR/28.11.2207
P407
P577
2000-06-01T00:00:00Z