3-methyladenine DNA glycosylases: structure, function, and biological importance - Wikidata - wikimedia - TriplyDB

3-methyladenine DNA glycosylases: structure, function, and biological importance

3-methyladenine DNA glycosylases: structure, function, and biological importance

http://www.wikidata.org/entity/Q28141634

about

Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG Some Provocative Thoughts on Damage and Repair of DNA.Overview of base excision repair biochemistry DNA bending and a flip-out mechanism for base excision by the helix–hairpin–helix DNA glycosylase, Escherichia coli AlkA A novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase I DNA oligonucleotides with A, T, G or C opposite an abasic site: structure and dynamics Structure of Escherichia coli AlkA in Complex with Undamaged DNA Structural Basis for the Inhibition of Human Alkyladenine DNA Glycosylase (AAG) by 3,N4-Ethenocytosine-containing DNA Substrate specificity and sequence-dependent activity of the Saccharomyces cerevisiae 3-methyladenine DNA glycosylase (Mag)Transcriptional networks in S. cerevisiae linked to an accumulation of base excision repair intermediates.Involvement of Iron-Containing Proteins in Genome Integrity in Arabidopsis Thaliana Investigation of the substrate spectrum of the human mismatch-specific DNA N-glycosylase MED1 (MBD4): fundamental role of the catalytic domain Biphasic kinetics of the human DNA repair protein MED1 (MBD4), a mismatch-specific DNA N-glycosylase Base excision and DNA binding activities of human alkyladenine DNA glycosylase are sensitive to the base paired with a lesion Protein tolerance to random amino acid change Oxanine DNA glycosylase activity from Mammalian alkyladenine glycosylase Genetic and biochemical characterization of human AP endonuclease 1 mutants deficient in nucleotide incision repair activity Early Chk1 phosphorylation is driven by temozolomide-induced, DNA double strand break- and mismatch repair-independent DNA damage Alkylpurine glycosylase D employs DNA sculpting as a strategy to extrude and excise damaged bases Recent progress in the biology, chemistry and structural biology of DNA glycosylases.Substrate binding pocket residues of human alkyladenine-DNA glycosylase critical for methylating agent survival Both RAD5-dependent and independent pathways are involved in DNA damage-associated sister chromatid exchange in budding yeast.A novel method for detecting 7-methyl guanine reveals aberrant methylation levels in Huntington disease Overexpression of enzymes that repair endogenous damage to DNA.Frameshift mutagenesis and microsatellite instability induced by human alkyladenine DNA glycosylase.Imbalanced base excision repair increases spontaneous mutation and alkylation sensitivity in Escherichia coli.Role of MED1 (MBD4) Gene in DNA repair and human cancer.Characterization of a conserved interaction between DNA glycosylase and ParA in Mycobacterium smegmatis and M. tuberculosis.Recent advances in the structural mechanisms of DNA glycosylases Homologous DNA recombination in vertebrate cells.DNA glycosylase activity and cell proliferation are key factors in modulating homologous recombination in vivo.Uncoupling of the base excision and nucleotide incision repair pathways reveals their respective biological roles.Homologous recombination prevents methylation-induced toxicity in Escherichia coli.The formation and biological significance of N7-guanine adducts Cloning and characterization of a wheat homologue of apurinic/apyrimidinic endonuclease Ape1L DNA repair is indispensable for survival after acute inflammation.Enforced presentation of an extrahelical guanine to the lesion recognition pocket of human 8-oxoguanine glycosylase, hOGG1.Identification of alkA gene related to virulence of Shigella flexneri 2a by mutational analysis.Genomic sequence of 'Candidatus Liberibacter solanacearum' haplotype C and its comparison with haplotype A and B genomes.

P2860

Q24647355-5E1766BE-CA17-4829-A9BE-6C6D250496B8 Q24669704-35415054-F610-4EE7-9B29-CE5A789C55A8 Q24793345-2D06699B-D4D1-4850-882D-925FD3B18C2E Q27021659-ED3EC000-4957-4226-B1E0-7A0367256ACF Q27621390-D81E950F-8F4D-4D66-9A24-267A6E9FAAE6 Q27640782-C1E51297-8F0D-4B72-B7DF-FE6E184FC896 Q27649103-31E3648D-262C-4983-A6A2-7F47D24030F5 Q27664515-7BA10164-229C-4A5A-A0F3-7A72E69E2A1D Q27667051-C4C213C5-E06C-4508-994B-C5BEFAD60550 Q27937334-4125AE86-33B3-49A4-90B4-4D5A8CCD7C70 Q27938847-F96C5D16-D94F-4DC4-9C13-BD5FAFA3DFEE Q28084415-B0F4F4B5-0C46-474E-84BB-AA46B3D14EFC Q28142508-079C838C-FBFD-4048-A85A-E3CDD412E6CC Q28142841-555AB0B1-85E6-43E4-9161-867FF1EA1847 Q28208151-1ECFF53F-3C16-46F5-9409-7656C357E733 Q28266927-3EDA02B2-98D3-4931-A759-E4D7048A2304 Q28271368-271B9D9C-BE8F-42DB-A58E-3B1A1FD5D1DB Q28475182-5A50A285-6AD8-49B2-91A7-1A7796524A45 Q28487714-29ED3E26-F20D-465D-90D3-6EB3305855C1 Q31172508-5C1CE747-6A33-4C3E-9E1E-909595347ED6 Q32063493-28BB401A-8B9F-4336-BFF2-B450C9CBEED0 Q33360502-D83E82FE-DFCE-4B92-8BF1-0C6CAB0BC5B6 Q33768750-955C5074-38DE-40F7-B0A3-00020C6D1180 Q33874603-706805D1-D8CE-4AFD-BAB4-DC784035953A Q33888666-D42EB793-CB6E-4A79-9ED3-241F164395CC Q33951115-E1A2BA0D-1FCB-45FD-88B2-314287E588F8 Q33993117-BD3EC593-EAE3-45DF-8078-C6BC6B755D5C Q34194512-B0E790F7-326A-4649-86EC-F009F09F40A6 Q34295789-5200DD74-5A27-416B-BBB7-3EA68038E150 Q34306735-5DFB67E1-ECE2-4199-A560-58B3477DF735 Q34311675-9D160ACB-D0EC-4102-A72C-7318EBCFEB01 Q34434917-5379B2E6-27B0-476E-8DF1-9D3670AB6B8F Q34479493-0FA9DB01-9FE4-4ED8-87B2-126FBB4ED641 Q34588314-B3103FE3-5A54-45D5-A5BB-E9478403FE60 Q34982742-EC428D34-D76F-45D7-B268-83C372C3BCDA Q35131211-8C42AE63-AEF1-4F3B-84DA-7A81BAD5675E Q36068346-8F770278-5DD2-48CD-BE08-F447977B78EA Q36127010-ABF8EA20-027B-45B5-9A61-49C1797B94CC Q36180500-1339BCCD-6A58-496F-9CA3-AAB74AE95674 Q36270047-486B5E70-15D1-4308-AA69-05E32B4597A8

P2860

3-methyladenine DNA glycosylases: structure, function, and biological importance

http://www.wikidata.org/entity/Q28141634

description

1999 nî lūn-bûn

@nan

1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի օգոստոսին 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

3-methyladenine DNA glycosylases: structure, function, and biological importance

@ast

3-methyladenine DNA glycosylases: structure, function, and biological importance

@en

3-methyladenine DNA glycosylases: structure, function, and biological importance

@nl

type

label

3-methyladenine DNA glycosylases: structure, function, and biological importance

@ast

3-methyladenine DNA glycosylases: structure, function, and biological importance

@en

3-methyladenine DNA glycosylases: structure, function, and biological importance

@nl

prefLabel

3-methyladenine DNA glycosylases: structure, function, and biological importance

@ast

3-methyladenine DNA glycosylases: structure, function, and biological importance

@en

3-methyladenine DNA glycosylases: structure, function, and biological importance

@nl

P1433

Q28141634-923D71F4-28A3-467A-B6C1-3CFE1C258719

P1476

Q28141634-E48FD659-D7CA-4570-A126-F49D3FC6DEB6

P2093

Q28141634-4D5FD02F-5731-4191-B554-CA3CFDA4822A

Q28141634-54B05F54-E599-4432-AE40-DE034A5C80B0

Q28141634-9974EE2A-3E7E-47EB-AB1D-DC7B1A175829

Q28141634-AB5019B5-AF41-491F-9D80-903B98CAE2BB

Q28141634-B4805FF7-C88F-44A1-A7E0-6A566343DC73

P2860

Q28141634-0910F2C4-7967-41E1-8FA0-79219CC28B25

Q28141634-37DAB9FD-4DEE-4BFB-9263-51B5A4E2D97E

Q28141634-D29AEBFB-B5DD-4DEC-A31C-C34A35949EE6

P304

Q28141634-F0D92AD6-7240-4B27-A1A5-E149CFAEDC94

P31

Q28141634-DC72EFE3-EAE2-4F73-BFA5-ADD8EA96DB39

P3181

Q28141634-34CBB34F-2CB9-4231-B7B0-2BC829C71A1F

P356

Q28141634-36EC3D04-56F0-4758-A1BD-665DB54DDC80

Q28141634-D8C82F22-89F1-4166-BFFA-FD64438D5A01

P407

Q28141634-AC2E88B7-14F8-4CEC-99E2-9FCADAFC17DC

P433

Q28141634-945B9A37-E639-4F75-B64B-51F314A27F35

P478

Q28141634-1084119B-BE1B-443E-AD73-905E9175FE7C

P577

Q28141634-569441CC-C3F5-4840-80FE-1938AABE13E0

P698

Q28141634-AA825357-2128-4B4B-A8B4-EB53E61EE0D3

P3181

P356

(SICI)1521-1878(199908)21:8%3C668::AID-BIES6%3E3.0.CO;2-D

(SICI)1521-1878(199908)21:8%3C668::AID-BIES6%3E3.3.CO;2-4

P1433

P1476

3-methyladenine DNA glycosylases: structure, function, and biological importance

@en

P2093

A Y Lau

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

J M Allan

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

L D Samson

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

M D Wyatt

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

T E Ellenberger

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

P2860

Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: an alternative pathway of base excision DNA repair

Developmental expression of a DNA repair gene in Arabidopsis.

Cellular role of yeast Apn1 apurinic endonuclease/3'-diesterase: repair of oxidative and alkylation DNA damage and control of spontaneous mutation

P304

668-76

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

P31

scholarly article

P3181

5019328

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

P356

10.1002/(SICI)1521-1878(199908)21:8<668::AID-BIES6>3.0.CO;2-D

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

10.1002/(SICI)1521-1878(199908)21:8<668::AID-BIES6>3.3.CO;2-4

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

P407

P433

8

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

P478

21

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

P577

1999-08-01T00:00:00Z

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

P698

10440863

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