about
HMGA2 exhibits dRP/AP site cleavage activity and protects cancer cells from DNA-damage-induced cytotoxicity during chemotherapyHuman DNA polymerase iota protects cells against oxidative stressComplementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2DNA polymerase family X: function, structure, and cellular rolesA polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cellYeast HMO1: Linker Histone ReinventedBase excision repairThe TAL effector PthA4 interacts with nuclear factors involved in RNA-dependent processes including a HMG protein that selectively binds poly(U) RNAHigh mobility group protein B1 enhances DNA repair and chromatin modification after DNA damageStoichiometry of base excision repair proteins correlates with increased somatic CAG instability in striatum over cerebellum in Huntington's disease transgenic miceHMG-box domain stimulation of RAG1/2 cleavage activity is metal ion dependent.Bioenergetic metabolites regulate base excision repair-dependent cell death in response to DNA damage.HMGB1: roles in base excision repair and related function.Dual functions of ASCIZ in the DNA base damage response and pulmonary organogenesisHMGB1: the jack-of-all-trades protein is a master DNA repair mechanic.XRCC1 coordinates disparate responses and multiprotein repair complexes depending on the nature and context of the DNA damagePol β associated complex and base excision repair factors in mouse fibroblasts.High mobility group box-1 (HMGB1) participates in the pathogenesis of alcoholic liver disease (ALD).Effect of the multifunctional proteins RPA, YB-1, and XPC repair factor on AP site cleavage by DNA glycosylase NEIL1.Posttranslational modification of mammalian AP endonuclease (APE1).Quantitative interaction screen of telomeric repeat-containing RNA reveals novel TERRA regulators.HMGB1 in health and disease.HMGB1 facilitates repair of mitochondrial DNA damage and extends the lifespan of mutant ataxin-1 knock-in mice.New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Proteomic profiling of adipose tissue from Zmpste24-/- mice, a model of lipodystrophy and premature aging, reveals major changes in mitochondrial function and vimentin processing.Mammalian Base Excision Repair: Functional Partnership between PARP-1 and APE1 in AP-Site Repair.DNA base excision repair: a mechanism of trinucleotide repeat expansion.CUX2 protein functions as an accessory factor in the repair of oxidative DNA damage.Special AT-rich Sequence-binding Protein 1 (SATB1) Functions as an Accessory Factor in Base Excision Repair.Genome-wide expression profiling in muscle and subcutaneous fat of lambs in response to the intake of concentrate supplemented with vitamin EThe nucleosome-binding protein HMGN2 modulates global genome repairEnhancement of NEIL1 protein-initiated oxidized DNA base excision repair by heterogeneous nuclear ribonucleoprotein U (hnRNP-U) via direct interaction.Trinucleotide repeat deletion via a unique hairpin bypass by DNA polymerase β and alternate flap cleavage by flap endonuclease 1.High-mobility group box 2 (HMGB2) modulates radioresponse and is downregulated by p53 in colorectal cancer cell.R152C DNA Pol β mutation impairs base excision repair and induces cellular transformationMutation of DNA Polymerase β R137Q Results in Retarded Embryo Development Due to Impaired DNA Base Excision Repair in MiceCardiac nuclear high mobility group box 1 prevents the development of cardiac hypertrophy and heart failureChromatin-associated proteins HMGB1/2 and PDIA3 trigger cellular response to chemotherapy-induced DNA damage.Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity.Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.
P2860
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P2860
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
HMGB1 is a cofactor in mammalian base excision repair
@ast
HMGB1 is a cofactor in mammalian base excision repair
@en
HMGB1 is a cofactor in mammalian base excision repair
@en-gb
HMGB1 is a cofactor in mammalian base excision repair
@nl
type
label
HMGB1 is a cofactor in mammalian base excision repair
@ast
HMGB1 is a cofactor in mammalian base excision repair
@en
HMGB1 is a cofactor in mammalian base excision repair
@en-gb
HMGB1 is a cofactor in mammalian base excision repair
@nl
prefLabel
HMGB1 is a cofactor in mammalian base excision repair
@ast
HMGB1 is a cofactor in mammalian base excision repair
@en
HMGB1 is a cofactor in mammalian base excision repair
@en-gb
HMGB1 is a cofactor in mammalian base excision repair
@nl
P2093
P2860
P921
P3181
P1433
P1476
HMGB1 is a cofactor in mammalian base excision repair
@en
P2093
Akira Yasui
Esther W Hou
Julie K Horton
Kenjiro Asagoshi
Kenneth B Tomer
Leesa J Deterding
Olga I Lavrik
Padmini S Kedar
Rajendra Prasad
Shin-Ichiro Kanno
P2860
P304
P3181
P356
10.1016/J.MOLCEL.2007.06.029
P407
P577
2007-09-01T00:00:00Z