Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA - Wikidata - wikimedia - TriplyDB

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

http://www.wikidata.org/entity/Q27638483

about

Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells Structure of the uncomplexed DNA repair enzyme endonuclease VIII indicates significant interdomain flexibility.Structural insights into abasic site for Fpg specific binding and catalysis: comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues-containing DNA NEIL1 excises 3' end proximal oxidative DNA lesions resistant to cleavage by NTH1 and OGG1.The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution.A novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase I Structure of a trapped endonuclease III-DNA covalent intermediate DNA lesion recognition by the bacterial repair enzyme MutM Structure of the E. coli DNA Glycosylase AlkA Bound to the Ends of Duplex DNA: A System for the Structure Determination of Lesion-Containing DNA Structural Characterization of a Viral NEIL1 Ortholog Unliganded and Bound to Abasic Site-containing DNA 5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA glycosylases Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine Sculpting of DNA at Abasic Sites by DNA Glycosylase Homolog Mag2 Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNA Structural Characterization of Viral Ortholog of Human DNA Glycosylase NEIL1 Bound to Thymine Glycol or 5-Hydroxyuracil-containing DNA A novel nucleoid-associated protein specific to the actinobacteria Strandwise translocation of a DNA glycosylase on undamaged DNA Sequence-dependent Structural Variation in DNA Undergoing Intrahelical Inspection by the DNA glycosylase MutM Structural investigation of a viral ortholog of human NEIL2/3 DNA glycosylases Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis.Insights into the glycosylase search for damage from single-molecule fluorescence microscopy.Using shifts in amino acid frequency and substitution rate to identify latent structural characters in base-excision repair enzymes Proteomic approach to identification of proteins reactive for abasic sites in DNA.Characterization of the meningococcal DNA glycosylase Fpg involved in base excision repair.Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.An Improved Reaction Coordinate for Nucleic Acid Base Flipping Studies.A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modifications Recent advances in the structural mechanisms of DNA glycosylases Active destabilization of base pairs by a DNA glycosylase wedge initiates damage recognition Thermodynamic and kinetic basis for recognition and repair of 8-oxoguanine in DNA by human 8-oxoguanine-DNA glycosylase.Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA Modulation of the turnover of formamidopyrimidine DNA glycosylase.DNA damage in blood cells exposed to low-level lasers.Rapid determination of the active fraction of DNA repair glycosylases: a novel fluorescence assay for trapped intermediates.

P2860

Q24318591-3E3EF8FF-E242-48F6-BBCA-FC55416FCBD3 Q24563827-39E55AAE-3EB7-43B9-A700-56F07C9336EC Q24564283-39D63AA9-9AF1-4505-A573-25D0656F4F62 Q24650179-C19966A3-CE37-43CA-9128-7E491898BAA6 Q24811220-1B7C12EE-ADE6-4DCB-B9B8-E534ADAC2DBF Q24816127-6F3CEA3F-82BA-453A-8BB3-9434470E87EB Q24816871-C215C8C8-666C-416B-832D-12CF269AAF96 Q27021912-C1AABAD1-0902-4736-969D-86EF3196257B Q27640255-48CD9074-5C69-425F-B3C0-BAA459035593 Q27640782-91A90136-3D9A-45CA-B3F0-78883611013C Q27641607-4BEBA2A1-B1E0-4E95-BE1E-412F0FA11DC9 Q27642268-65CC171F-8FC8-47E7-A2C8-3C5CECDB053C Q27651423-AE896F44-E126-433A-8529-11477E667717 Q27656645-6F175313-24B4-4C04-938E-50D0B6393B0A Q27667498-C4D42592-0A68-4463-8278-7A4B748CB063 Q27670719-3423EBB4-053D-472D-A999-CA0195DAF488 Q27675515-49C49459-EC7F-4433-862E-C276D5B3E495 Q27675877-ED36CFF1-3597-4B7A-932F-249BBACFEEDE Q27676196-EE16E644-23C9-4D61-BAA3-30CF78B5E52F Q27676494-8AA45455-90B9-4465-AC0B-64C2ADF37504 Q27676544-2AC7EE36-6D3E-477A-8737-94DAEA33F272 Q27678278-46ED4763-C2AA-4B8C-A922-BE4CC9053F7D Q27680235-7758F4B9-9632-4F3A-99A8-8E65CB7EF327 Q28279961-959F29E2-569D-44C5-8597-7CFF42C95FAA Q28487547-AC8022AA-1C93-4A2A-AEB7-6622CB43D062 Q30356048-0F2420B7-D544-4EE3-9464-C28C1FB372BC Q30585004-DED23B13-CD45-4D82-A253-59BC2E2E7543 Q31036870-450818AC-4D33-4830-A742-CBC73D6465FC Q33233778-AEC2DF4F-A05D-4CAC-9721-293BE7A18DDA Q33398811-8DF35BE7-EBF5-4074-99C1-BC5FB937C504 Q33665271-9FAE057C-D3C7-42CE-B9A7-AAE242E02897 Q33721314-EEB4CC80-1ACA-4350-9CE6-FE42EAEDB6A5 Q33823011-C6CA3F06-A1D6-4123-BA79-9A18196E02B6 Q34306735-5730FF29-1349-4BFA-934D-DB41229CF32E Q34883466-E8C79F05-90BC-48FD-82CB-2F3D257546C7 Q35040930-144328F2-9DC9-4F57-A94C-F1666A0EE6C2 Q35224383-4D381C5C-D33B-465D-B805-FEEE753AC289 Q35235101-47117DE5-AB2E-4D06-8FC1-D5DBE42604A4 Q35571846-AD31BA9E-16A5-4DA9-9B59-9F40171343F9 Q35781828-92CE2038-656C-464D-90D4-D7B4B901486A

P2860

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

http://www.wikidata.org/entity/Q27638483

description

2002 nî lūn-bûn

@nan

2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@ast

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@en

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@nl

type

label

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@ast

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@en

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@nl

prefLabel

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@ast

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@en

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@nl

P1433

Q27638483-C8569956-4957-4CB0-BCB1-440C828AEAF7

P1476

Q27638483-9DC4E2E0-E521-41AF-ADC3-7C2C52206595

P2093

Q27638483-00A74860-9F92-495B-A3FE-A7C372A68E2A

Q27638483-0BFEA65A-6FC6-4C53-AD9B-5F9E153EC5BA

Q27638483-20168C74-7BEA-4D60-AFDE-6C9C93165231

Q27638483-50A3C7F5-7524-4CAB-94D2-B2B8392D338D

Q27638483-5BF76FEA-E1B1-41B4-8920-A5E5368A5AC9

Q27638483-82A1952E-422D-4277-BC26-7150C1404822

Q27638483-B07656AC-0B68-4E39-B5FA-00B91E7F58BA

Q27638483-C4B55547-42B9-4D8F-A4E2-AAF625D74C73

Q27638483-CE49A2AE-9637-47C1-9282-2E9502A01827

P2860

Q27638483-0A4FA92F-F56C-4F31-8D5D-860B01A61C0C

Q27638483-2A2B9358-17E4-49FF-A280-5776691B3FBE

Q27638483-32D16E31-3B99-4D17-8E83-0AAF30152DAB

Q27638483-33B26D9F-3791-4D79-8A8B-BD3DFB6D0F24

Q27638483-378A98B3-53AC-43B1-89E5-566B7C6798BD

Q27638483-386AFEFE-A82F-456D-821F-BE36A08C8B65

Q27638483-449C9D5E-B428-4CFA-A7D9-A08D0AEACCAC

Q27638483-459B0A5E-3E73-4641-B026-13D418F2AEF0

Q27638483-47F7EC7C-D8E7-4572-9687-78C587BBF4AD

Q27638483-489F97BC-A72D-46F1-B9B9-823D458109C0

P304

Q27638483-FD59B9E0-DFC0-42A8-B96F-00BB01F84634

P31

Q27638483-D2AA9F4F-37B0-4E36-9662-9A9DCA7B6729

P3181

Q27638483-C5906477-40AC-46E4-AA8A-775E107E3FBD

P356

Q27638483-03E35E0D-26FF-4940-BF2A-733A8A90F464

P407

Q27638483-90A4D95A-27B8-40B1-9173-F96A96437F3B

P433

Q27638483-07823F80-AF6C-4DC3-AF9C-D988FEEDE836

P478

Q27638483-63B3623F-4A5F-4CEE-9939-93BBBDAB18ED

P577

Q27638483-28685591-951B-44EE-BB91-448A3E776996

P698

Q27638483-D1A11279-097C-4A81-8A40-0F172190C50F

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA

@en

P2093

Andrea S Fernandes

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

Arthur P Grollman

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

Dmitry O Zharkov

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

Eileen Matz

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

Gali Golan

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

Gil Shoham

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

Jadwiga H Kycia

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

Rotem Gilboa

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

Sue Ellen Gerchman

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

P2860

Structural analysis of an Escherichia coli endonuclease VIII covalent reaction intermediate.

The COG database: new developments in phylogenetic classification of proteins from complete genomes

Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8

Improved methods for building protein models in electron density maps and the location of errors in these models

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Processing of X-ray diffraction data collected in oscillation mode

A structural snapshot of base-pair opening in DNA

DNA bending and a flip-out mechanism for base excision by the helix–hairpin–helix DNA glycosylase, Escherichia coli AlkA

Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA

Stressing-out DNA? The contribution of serine-phosphodiester interactions in catalysis by uracil DNA glycosylase

P304

19811-6

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

P31

scholarly article

P3181

2957796

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

P356

10.1074/JBC.M202058200

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

P407

P433

22

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

P478

277

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

P577

2002-05-31T00:00:00Z

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

P698

11912217

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