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
about
Reconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteins3-Methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteinsRBT1, a novel transcriptional co-activator, binds the second subunit of replication protein AStructure of RPA32 bound to the N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteinsAn alternative form of replication protein a expressed in normal human tissues supports DNA repairRegulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylaseEarly steps in the DNA base excision/single-strand interruption repair pathway in mammalian cellsUracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanismsHuman cytomegalovirus uracil DNA glycosylase associates with ppUL44 and accelerates the accumulation of viral DNA.RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage responseStructural basis for uracil DNA glycosylase interaction with uracil: NMR study.Structural Analysis of Replication Protein A Recruitment of the DNA Damage Response Protein SMARCAL1Characteristics and concepts of dynamic hub proteins in DNA processing machinery from studies of RPAThe RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domainUracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognitionExcision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylaseA dynamic model for replication protein A (RPA) function in DNA processing pathwaysInteractions of the papovavirus DNA replication initiator proteins, bovine papillomavirus type 1 E1 and simian virus 40 large T antigen, with human replication protein AMechanism underlying replication protein a stimulation of DNA ligase I.Autoimmunity to the M(r) 32,000 subunit of replication protein A in breast cancerFunctions of human replication protein A (RPA): from DNA replication to DNA damage and stress responsesThe multi-replication protein A (RPA) system--a new perspective.Replication protein A: directing traffic at the intersection of replication and repair.Molecular interaction map of the mammalian cell cycle control and DNA repair systems.Predicting protein-DNA interactions by full search computational docking.Recruitment of the nuclear form of uracil DNA glycosylase into virus particles participates in the full infectivity of HIV-1.Base excision repair in a network of defence and tolerance.B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil.Repair of oxidative DNA base lesions induced by fluorescent light is defective in xeroderma pigmentosum group A cellsArchitecture and ssDNA interaction of the Timeless-Tipin-RPA complex.Uracil DNA glycosylase interacts with the p32 subunit of the replication protein A complex to modulate HIV-1 reverse transcription for optimal virus dissemination.Replication protein A and more: single-stranded DNA-binding proteins in eukaryotic cells.Human single-stranded DNA binding proteins: guardians of genome stability.Expression and purification of active mouse and human NEIL3 proteins.Combining H/D exchange mass spectroscopy and computational docking reveals extended DNA-binding surface on uracil-DNA glycosylase.Detection of uracil within DNA using a sensitive labeling method for in vitro and cellular applications.Origin of endogenous DNA abasic sites in Saccharomyces cerevisiaeRepair of U/G and U/A in DNA by UNG2-associated repair complexes takes place predominantly by short-patch repair both in proliferating and growth-arrested cells.HIV-1 Vpr-a still "enigmatic multitasker".Functions of disordered regions in mammalian early base excision repair proteins.
P2860
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P2860
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
description
1997 nî lūn-bûn
@nan
1997 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մարտին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
A sequence in the N-terminal r ...... bunit of replication protein A
@ast
A sequence in the N-terminal r ...... bunit of replication protein A
@en
A sequence in the N-terminal r ...... bunit of replication protein A
@nl
type
label
A sequence in the N-terminal r ...... bunit of replication protein A
@ast
A sequence in the N-terminal r ...... bunit of replication protein A
@en
A sequence in the N-terminal r ...... bunit of replication protein A
@nl
prefLabel
A sequence in the N-terminal r ...... bunit of replication protein A
@ast
A sequence in the N-terminal r ...... bunit of replication protein A
@en
A sequence in the N-terminal r ...... bunit of replication protein A
@nl
P2093
P2860
P50
P3181
P356
P1476
A sequence in the N-terminal r ...... bunit of replication protein A
@en
P2093
K F Keshav
R Benarous
T A Nagelhus
P2860
P304
P3181
P356
10.1074/JBC.272.10.6561
P407
P577
1997-03-07T00:00:00Z