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Nucleotide excision repair: from E. coli to man.
Petit C, Sancar A. Petit C, et al. Biochimie. 1999 Jan-Feb;81(1-2):15-25. doi: 10.1016/s0300-9084(99)80034-0. Biochimie. 1999. PMID: 10214906 Review.
Nucleotide excision repair is both a 'wide spectrum' DNA repair pathway and the sole system for repairing bulky damages such as UV lesions or benzo[a]pyrene adducts. ...Thus, the excinuclease mode of action is well conserved throughout evolution, but not the biochem …
Nucleotide excision repair is both a 'wide spectrum' DNA repair pathway and the sole system for repairing bulky damages such as UV le …
Human nucleotide excision nuclease removes thymine dimers from DNA by incising the 22nd phosphodiester bond 5' and the 6th phosphodiester bond 3' to the photodimer.
Huang JC, Svoboda DL, Reardon JT, Sancar A. Huang JC, et al. Proc Natl Acad Sci U S A. 1992 Apr 15;89(8):3664-8. doi: 10.1073/pnas.89.8.3664. Proc Natl Acad Sci U S A. 1992. PMID: 1314396 Free PMC article.
By using a human cell-free system capable of nucleotide excision repair, a synthetic substrate consisting of a plasmid containing four thymidine dimers at unique locations, and deoxyribonucleoside 5'-[alpha-thio]triphosphates for repair synthesis, we obtained …
By using a human cell-free system capable of nucleotide excision repair, a synthetic substrate consisting of a plasmid …
Purification of PCNA as a nucleotide excision repair protein.
Nichols AF, Sancar A. Nichols AF, et al. Nucleic Acids Res. 1992 Jul 11;20(13):2441-6. doi: 10.1093/nar/20.10.2441. Nucleic Acids Res. 1992. PMID: 1352873 Free PMC article.
The extract is readily separated into two fractions by chromatography on a DEAE column. Neither the low salt (0.1 M KCl) nor the high salt (0.8 M KCl) fractions are capable of repair synthesis but the combination of the two restore the repair synthesis activity. Using the …
The extract is readily separated into two fractions by chromatography on a DEAE column. Neither the low salt (0.1 M KCl) nor the high …
Electron microscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex.
Shi Q, Thresher R, Sancar A, Griffith J. Shi Q, et al. J Mol Biol. 1992 Jul 20;226(2):425-32. doi: 10.1016/0022-2836(92)90957-l. J Mol Biol. 1992. PMID: 1386387
Using electron microscopy, we investigated the structures of these early A, A-B intermediates on DNA containing ultraviolet light photoproducts. UvrA, which is known to bind to DNA as a dimer and produce a DNase I footprint of 33 base-pairs does not ch …
Using electron microscopy, we investigated the structures of these early A, A-B intermediates on DNA containing ultraviolet li …
Active site of (A)BC excinuclease. I. Evidence for 5' incision by UvrC through a catalytic site involving Asp399, Asp438, Asp466, and His538 residues.
Lin JJ, Sancar A. Lin JJ, et al. J Biol Chem. 1992 Sep 5;267(25):17688-92. J Biol Chem. 1992. PMID: 1387639
To investigate the role of UvrC in the nuclease activity a subset of His, Asp, and Glu residues in the C-terminal half of the protein were mutagenized in vitro. ...Our data suggest that UvrC makes the 5' incision by employing a mechanism whereby the three carboxylat …
To investigate the role of UvrC in the nuclease activity a subset of His, Asp, and Glu residues in the C-terminal half of the protein …
Active site of (A)BC excinuclease. II. Binding, bending, and catalysis mutants of UvrB reveal a direct role in 3' and an indirect role in 5' incision.
Lin JJ, Phillips AM, Hearst JE, Sancar A. Lin JJ, et al. J Biol Chem. 1992 Sep 5;267(25):17693-700. J Biol Chem. 1992. PMID: 1387640
UvrB plays a central role in (A)BC excinuclease. To study its role in the incision reactions, conserved His and Asp residues in this subunit were mutagenized. ...UvrB which is missing the carboxyl-terminal 43 amino acids binds to, and kinks DNA but is unable to make …
UvrB plays a central role in (A)BC excinuclease. To study its role in the incision reactions, conserved His and Asp residues i …
(A)BC excinuclease: the Escherichia coli nucleotide excision repair enzyme.
Lin JJ, Sancar A. Lin JJ, et al. Mol Microbiol. 1992 Aug;6(16):2219-24. doi: 10.1111/j.1365-2958.1992.tb01398.x. Mol Microbiol. 1992. PMID: 1406264 Review.
(A)BC excinuclease is the nuclease activity which initiates nucleotide excision repair in Escherichia coli. In this review, we focus on current understanding of the structure-function of the enzyme and the reaction mechanism of the repair pathway. ...
(A)BC excinuclease is the nuclease activity which initiates nucleotide excision repair in Escherichia coli. In this review, we focus …
In vitro characterization of repair synthesis initiated by T4 endonuclease V on a synthetic DNA substrate.
Sibghat-Ullah, Sancar A. Sibghat-Ullah, et al. Indian J Biochem Biophys. 1992 Jun;29(3):227-30. Indian J Biochem Biophys. 1992. PMID: 1512008
A 48-bp DNA containing a pyrimidine dimer at a defined location was labelled in the damaged strand and incubated with T4 endo V and E. coli endonuclease IV. ...Analysis of the reaction products on a sequencing gel revealed a ladder of only 4-oli
A 48-bp DNA containing a pyrimidine dimer at a defined location was labelled in the damaged strand and incubated with T
Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I.
Orren DK, Selby CP, Hearst JE, Sancar A. Orren DK, et al. J Biol Chem. 1992 Jan 15;267(2):780-8. J Biol Chem. 1992. PMID: 1530937
UvrA, UvrB, and UvrC initiate nucleotide excision repair by incising a damaged DNA strand on each side of the damaged nucleotide. ...The specific binding of UvrB to a psoralen adduct in DNA inhibits psoralen-mediated DNA-DNA cross-linking, yet promotes the formation …
UvrA, UvrB, and UvrC initiate nucleotide excision repair by incising a damaged DNA strand on each side of the damaged nucleotide. ... …
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