About: Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase

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About: Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	article (en) հոդված (hy) wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1995 (uk) im Januar 1995 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q57942555-A56CBD8F-C8F0-432C-A4BF-9702A55D1C72
publication date	1995-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57942555-AB44255D-CAE5-4AD1-864A-B64460E4F94A
language of work or name	English
author name string	wds:Q57942555-7CF15E63-47B7-4EFE-9379-6EF6679CE107 wds:Q57942555-92EAC000-57A9-443D-BF41-33E15CAD6F84 wds:Q57942555-960A391A-8002-4A44-AD95-DF4F9B207AA6 wds:Q57942555-B0205AF9-F0FC-46E3-AC71-A25808527EC1 wds:Q57942555-DC26FCF5-BBD7-4741-A69E-DB853503989B
author name string	B Kavli T Haug S Bharati D W Levine N M Helle
rdfs:label	Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase (en) Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase (nl)
skos:prefLabel	Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase (en) Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase (nl)
name	Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase (en) Properties of a Recombinant Human Uracil-DNA Glycosylase from the UNG Gene and Evidence that UNG Encodes the Major Uracil-DNA Glycosylase (nl)
author	wds:Q57942555-0115F80C-2189-4875-ACBA-33549EDC3652 wds:Q57942555-DCE8DDA2-BB8E-456C-82D8-1B2B43481ADC wds:Q57942555-DD8DFC33-E431-4329-BF52-D538E3859DF6
author	Hans Einar Krokan Geir Slupphaug Ingrid Eftedal
title	wds:Q57942555-4C3962FE-1E42-4435-85DC-41DE2F827556
title	Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase (en)
page(s)	wds:Q57942555-BDACDD86-DB85-4224-8788-86A9030F84F0
page(s)	128-138
instance of	wds:Q57942555-06DDE8E9-457A-474A-8B85-9C37F887D339
instance of	scholarly article
PubMed ID	wds:Q57942555-DA2CDC24-3266-49B7-AEBA-5B3FB461528A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7819187
PubMed ID	7819187
published in	wds:Q57942555-6F797212-5D0D-4A91-B03D-C6A0B1B1C850
published in	Biochemistry
issue	wds:Q57942555-A394ACE9-FDF8-45F2-8324-88AD20F9330F
volume	wds:Q57942555-D103A91F-4176-4D5F-AF51-40BE351C7949
issue	1
volume	34
DOI	wds:Q57942555-BD320432-9E2D-4287-8C94-31578DE53CA8
DOI	http://dx.doi.org/10.1021/BI00001A016
DOI	10.1021/BI00001A016
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57942555
is cites work of	DNA glycosylases in the base excision repair of DNA Mutational analysis of arginine 276 in the leucine-loop of human uracil-DNA glycosylase Physical and functional interaction of human nuclear uracil-DNA glycosylase with proliferating cell nuclear antigen Direct interaction between XRCC1 and UNG2 facilitates rapid repair of uracil in DNA by XRCC1 complexes Human cytomegalovirus uracil DNA glycosylase is required for the normal temporal regulation of both DNA synthesis and viral replication Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase Specific interaction of DNA polymerase beta and DNA ligase I in a multiprotein base excision repair complex from bovine testis Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate. Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair Fidelity of uracil-initiated base excision DNA repair in DNA polymerase beta-proficient and -deficient mouse embryonic fibroblast cell extracts Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). Lessons learned from structural results on uracil-DNA glycosylase Binding of specific DNA base-pair mismatches by N-methylpurine-DNA glycosylase and its implication in initial damage recognition Localization of the deoxyribose phosphate lyase active site in human DNA polymerase iota by controlled proteolysis. Uracil-DNA glycosylase acts by substrate autocatalysis Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein Mutagenesis dependent upon the combination of activation-induced deaminase expression and a double-strand break Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene Regulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylase A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A Base excision repair of oxidative DNA damage activated by XPG protein Recent progress in the biology, chemistry and structural biology of DNA glycosylases A phylogenomic study of DNA repair genes, proteins, and processes Human DNA polymerase beta initiates DNA synthesis during long-patch repair of reduced AP sites in DNA Human DNA polymerase theta possesses 5'-dRP lyase activity and functions in single-nucleotide base excision repair in vitro Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. The Werner syndrome protein stimulates DNA polymerase beta strand displacement synthesis via its helicase activity Regulation of WRN helicase activity in human base excision repair Isolation of a small molecule inhibitor of DNA base excision repair. Bipartite substrate discrimination by human nucleotide excision repair Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest Enzymatic capture of an extrahelical thymine in the search for uracil in DNA Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA. Characterization of the uracil-DNA glycosylase activity of Epstein-Barr virus BKRF3 and its role in lytic viral DNA replication Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme Functional analysis of the amino-terminal 8-kDa domain of DNA polymerase beta as revealed by site-directed mutagenesis. DNA binding and 5'-deoxyribose phosphate lyase activities Mapping of the 5'-2-deoxyribose-5-phosphate lyase active site in DNA polymerase beta by mass spectrometry The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs The uracil DNA glycosylase UdgB of Mycobacterium smegmatis protects the organism from the mutagenic effects of cytosine and adenine deamination Expression and activity of the DNA repair enzyme uracil DNA glycosylase during organogenesis in the rat conceptus and following methotrexate exposure in vitro HMGB1 is a cofactor in mammalian base excision repair DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA Mitochondrial DNA repair and association with aging--an update Highly efficient base excision repair (BER) in human and rat male germ cells Uracil residues dependent on the deaminase AID in immunoglobulin gene variable and switch regions Uracil in DNA--occurrence, consequences and repair hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup

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