Alkylpurine-DNA-N-glycosylase knockout mice show increased susceptibility to induction of mutations by methyl methanesulfonate.
about
Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatinN-methylpurine DNA glycosylase overexpression increases alkylation sensitivity by rapidly removing non-toxic 7-methylguanine adductsBase excision repair and cancerYNK1, the yeast homolog of human metastasis suppressor NM23, is required for repair of UV radiation- and etoposide-induced DNA damage.Expression of base excision, mismatch, and recombination repair genes in the organogenesis-stage rat conceptus and effects of exposure to a genotoxic teratogen, 4-hydroperoxycyclophosphamideHighly efficient base excision repair (BER) in human and rat male germ cellsRecognition and processing of a new repertoire of DNA substrates by human 3-methyladenine DNA glycosylase (AAG).In vivo repair of methylation damage in Aag 3-methyladenine DNA glycosylase null mouse cellsDNA breaks and chromosomal aberrations arise when replication meets base excision repair.Overexpression of enzymes that repair endogenous damage to DNA.Base excision repair of DNA in mammalian cells.DNA repair mechanisms and acute myeloblastic leukemia.Mutations associated with base excision repair deficiency and methylation-induced genotoxic stressDetection of PIGO-deficient cells using proaerolysin: a valuable tool to investigate mechanisms of mutagenesis in the DT40 cell systemBase excision repair in a network of defence and tolerance.Targeted deletion of mNth1 reveals a novel DNA repair enzyme activity.ATM regulates 3-methylpurine-DNA glycosylase and promotes therapeutic resistance to alkylating agents.Alkylation sensitivity screens reveal a conserved cross-species functionome.Formation and repair of tobacco carcinogen-derived bulky DNA adductsNeonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase beta.Chemopreventive n-3 polyunsaturated fatty acids reprogram genetic signatures during colon cancer initiation and progression in the rat.Attenuation of DNA polymerase beta-dependent base excision repair and increased DMS-induced mutagenicity in aged mice.Repair of exocyclic DNA adducts: rings of complexity.Commentary: DNA base excision repair defects in human pathologies.Eukaryotic Y-family polymerases bypass a 3-methyl-2'-deoxyadenosine analog in vitro and methyl methanesulfonate-induced DNA damage in vivoBalancing repair and tolerance of DNA damage caused by alkylating agentsMethylating agents and DNA repair responses: Methylated bases and sources of strand breaks.Human methyl purine DNA glycosylase and DNA polymerase beta expression collectively predict sensitivity to temozolomide.Glioblastoma, a brief review of history, molecular genetics, animal models and novel therapeutic strategies.1,N(2)-ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch-specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase.Mixed spermatogenic germ cell nuclear extracts exhibit high base excision repair activity.Initiation of the ATM-Chk2 DNA damage response through the base excision repair pathway.Differences in chimera formation and germline transmission between E14 and C2J embryonic stem cells in mice.Increased susceptibility to streptozotocin-induced beta-cell apoptosis and delayed autoimmune diabetes in alkylpurine-DNA-N-glycosylase-deficient mice.Interactions of the human, rat, Saccharomyces cerevisiae and Escherichia coli 3-methyladenine-DNA glycosylases with DNA containing dIMP residues.N-methylpurine DNA glycosylase plays a pivotal role in the threshold response of ethyl methanesulfonate-induced chromosome damage.Cells deficient in PARP-1 show an accelerated accumulation of DNA single strand breaks, but not AP sites, over the PARP-1-proficient cells exposed to MMS.DNA repair by MGMT, but not AAG, causes a threshold in alkylation-induced colorectal carcinogenesis.Base excision repair imbalance in colorectal cancer has prognostic value and modulates response to chemotherapyKinetic mechanism for the flipping and excision of 1,N(6)-ethenoadenine by human alkyladenine DNA glycosylase.
P2860
Q24647355-08C13F97-8782-4AA8-8820-B4016D595F89Q24805889-56C79599-FEA2-40CA-A01E-33EE5B4F8B5AQ27025537-03F07A28-C436-4DA4-8849-6C9D9FDF26FFQ27933894-E6B10E59-105A-46AC-9E61-9CBC6FA1FC67Q28569407-71111C14-ED49-4A93-8D92-13CBE8C296C0Q28580367-F710576A-67DC-498C-B922-27A02F768A94Q30858523-B4033EFE-64BA-47B1-9C25-578BBDB44878Q33786642-E0995620-641C-4D5E-BDF0-EF7885FE4DE2Q33859100-4CB3D920-AA2C-49E8-89E2-6B1D3570EA63Q33888666-9FE2F51D-537F-4024-82C2-D80A1056A59CQ33957142-5A43A8C5-B41C-4AE8-8501-523C9FE16FFDQ34057968-18F753B3-1AED-4C73-8811-EDF0FCDA699FQ34067688-48B6C119-A968-4972-A80C-12063D9CD4BBQ34201069-9431D50C-BC68-4C08-A03D-4D3EC8A308EDQ34283911-D60C28F8-D9C4-41C4-959B-61FB1EBB2CDBQ34285514-852A69F1-3458-4A99-8230-35210D67AC0BQ34287713-109ED938-A038-4615-BBB4-CFE4531C3940Q34434871-EF33BAC3-D8F3-4BCD-8128-EA86EA47E9A0Q34475702-11BE1E24-FE8B-4F48-8422-52F51DD1D453Q34668670-F8B3713D-8096-44C4-974C-0294F65998EAQ35695041-3AAC1926-CECB-4BDD-9F15-F2DF1E57893DQ35919383-E38C939F-F58D-4623-9BB1-CDB2C3BC8B3CQ35925261-6A8D59D4-13FD-403E-9137-404E97BEFE8FQ35932007-D4ADDA3E-A1C7-456E-82E3-43202D8F112BQ36633158-07CE47DF-AFDE-4D70-A56E-6FE16D4C3545Q36651488-F529C918-F63B-4B84-8A4C-2C283AE8E643Q36686012-313D689B-E0C9-4C38-8BD0-4B4B5F335E95Q37541592-1C589876-9D80-4954-A6C1-A2E554DEEE78Q38065976-B484467B-EEA9-4BBC-9675-B3F9A4CE3592Q38289103-F1398EEC-B15A-4042-95BC-EF660D9C1B95Q38660638-0BD04EF4-9E86-49C5-9159-A09962948EF4Q38869405-83BBE174-83FD-48C1-BCF0-A1AE05A8F4DEQ39313139-C66E2B1A-9407-4CDF-80E9-67AF1977968DQ39460713-4A2B624E-1F35-46ED-A124-18341230600FQ39586073-60A362D3-FA7B-4FA0-8AED-1B450DFA007CQ39632856-CD66C8EC-5D4A-45B3-877F-F5A207BB4AA6Q39795615-D6B9256C-CFA2-47F9-809B-5F9FE5B4A240Q40659969-2AA899ED-5791-4519-AF79-0C5C76BD7852Q41552855-7E662723-0150-40F8-B0A8-6C0B2DE90835Q42052547-AEDE8925-0403-482D-A0CB-2EB63A033A26
P2860
Alkylpurine-DNA-N-glycosylase knockout mice show increased susceptibility to induction of mutations by methyl methanesulfonate.
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Alkylpurine-DNA-N-glycosylase ...... ns by methyl methanesulfonate.
@ast
Alkylpurine-DNA-N-glycosylase ...... ns by methyl methanesulfonate.
@en
type
label
Alkylpurine-DNA-N-glycosylase ...... ns by methyl methanesulfonate.
@ast
Alkylpurine-DNA-N-glycosylase ...... ns by methyl methanesulfonate.
@en
prefLabel
Alkylpurine-DNA-N-glycosylase ...... ns by methyl methanesulfonate.
@ast
Alkylpurine-DNA-N-glycosylase ...... ns by methyl methanesulfonate.
@en
P2093
P2860
P356
P1476
Alkylpurine-DNA-N-glycosylase ...... ns by methyl methanesulfonate.
@en
P2093
A A van Zeeland
A J Watson
D P Cooper
G P Margison
J A Bailey
J A Rafferty
J G Jansen
K J Mynett
M A Willington
P2860
P304
P356
10.1128/MCB.18.10.5828
P407
P577
1998-10-01T00:00:00Z