Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA.
about
The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNAA novel cytoplasmic GTPase XAB1 interacts with DNA repair protein XPACentrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.Nucleotide excision repair by mutant xeroderma pigmentosum group A (XPA) proteins with deficiency in interaction with RPAFormation of a ternary complex by human XPA, ERCC1, and ERCC4(XPF) excision repair proteinsReconstitution of human excision nuclease with recombinant XPF-ERCC1 complexMutational analysis of the human nucleotide excision repair gene ERCC1UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylationNucleotide excision repair- and polymerase eta-mediated error-prone removal of mitomycin C interstrand cross-linksHuman xeroderma pigmentosum group G gene encodes a DNA endonucleaseSpecific association between the human DNA repair proteins XPA and ERCC1Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAKERCC4 (XPF) encodes a human nucleotide excision repair protein with eukaryotic recombination homologsAn interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repairAdvances in carcinogenic metal toxicity and potential molecular markersInteractions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studiesStructural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPAStructural Basis for Bulky-Adduct DNA-Lesion Recognition by the Nucleotide Excision Repair Protein Rad14Solution structure of the DNA- and RPA-binding domain of the human repair factor XPAFormation and repair of interstrand cross-links in DNAA multistep damage recognition mechanism for global genomic nucleotide excision repairAberrant mobility phenomena of the DNA repair protein XPASequestration of mammalian Rad51-recombination protein into micronucleiIn vitro analysis of the zinc-finger motif in human replication protein AReplication protein A (RPA) binding to duplex cisplatin-damaged DNA is mediated through the generation of single-stranded DNA.Recognition of nonhybridizing base pairs during nucleotide excision repair of DNAStopped-flow kinetic analysis of replication protein A-binding DNA: damage recognition and affinity for single-stranded DNA reveal differential contributions of k(on) and k(off) rate constants.Damaged DNA-binding protein DDB stimulates the excision of cyclobutane pyrimidine dimers in vitro in concert with XPA and replication protein A.Triplex-induced recombination in human cell-free extracts. Dependence on XPA and HsRad51.Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair.Photocrosslinking locates a binding site for the large subunit of human replication protein A to the damaged strand of cisplatin-modified DNAQuantitative analysis of the binding affinity of poly(ADP-ribose) to specific binding proteins as a function of chain lengthUltraviolet light selection assay to optimize oligonucleotide correction of mutations in endogenous xeroderma pigmentosum genes.Removal of oxygen free-radical-induced 5',8-purine cyclodeoxynucleosides from DNA by the nucleotide excision-repair pathway in human cellsSite-directed recombination via bifunctional PNA-DNA conjugates.DNA damage in the nucleosome core is refractory to repair by human excision nuclease.Binding and repair of mismatched DNA mediated by Rhp14, the fission yeast homologue of human XPA.DNA-XPA interactions: a (31)P NMR and molecular modeling study of dCCAATAACC association with the minimal DNA-binding domain (M98-F219) of the nucleotide excision repair protein XPA.Xeroderma pigmentosum complementation group A protein (XPA) modulates RPA-DNA interactions via enhanced complex stability and inhibition of strand separation activity.Psoralen interstrand cross-link repair is specifically altered by an adjacent triple-stranded structure
P2860
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P2860
Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Preferential binding of the xe ...... enting protein to damaged DNA.
@en
type
label
Preferential binding of the xe ...... enting protein to damaged DNA.
@en
prefLabel
Preferential binding of the xe ...... enting protein to damaged DNA.
@en
P356
P1433
P1476
Preferential binding of the xe ...... menting protein to damaged DNA
@en
P2093
P304
12096-12104
P356
10.1021/BI00096A021
P407
P577
1993-11-01T00:00:00Z