The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage.
about
Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilusCrystal structure of reverse gyrase: insights into the positive supercoiling of DNACrystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexesDNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway.UvrAB activity at a damaged DNA site: is unpaired DNA present?A specific 3' exonuclease activity of UvrABC.Interactions of DNA helicases with damaged DNA: possible biological consequences.Localization of UvrA and effect of DNA damage on the chromosome of Bacillus subtilis.Modularity and specialization in superfamily 1 and 2 helicasesUvrA and UvrB suppress illegitimate recombination: synergistic action with RecQ helicase.Efficient processing of TFO-directed psoralen DNA interstrand crosslinks by the UvrABC nucleaseIdentification of residues within UvrB that are important for efficient DNA binding and damage processing.Clue to damage recognition by UvrB: residues in the beta-hairpin structure prevent binding to non-damaged DNA.Damage increases the flexibility of duplex DNAConservation and Divergence in Nucleotide Excision Repair Lesion Recognition.Stimulation of UvrD helicase by UvrAB.Base flipping in nucleotide excision repair.UvrB domain 4, an autoinhibitory gate for regulation of DNA binding and ATPase activity.
P2860
Q27619948-83D948ED-1A62-4604-8191-BA64BB4340B2Q27637557-6308040D-8CCC-4401-8494-A48A472676B0Q27670608-40252574-EDAB-4A12-9826-6C0D779810FEQ33473091-BD246EE3-0726-48B7-AB47-215B33CFFE7FQ33886156-25D5235A-DD32-4285-AB82-4381B9BC55E7Q33888156-1AEFA5EB-5AAE-41C3-96FD-A8F7BE357030Q34011942-5B07B096-2F53-41FD-BC3C-588F7864F68DQ34105903-A19BBF1B-9BEC-4509-8C31-BC9BC28EFF81Q34559075-155E9645-8614-4780-927D-69AC65317CBFQ35756609-D6290CF4-6BB2-4B36-9FEA-7A81515FCBA2Q37014694-01293E2C-A670-495A-BA4D-02F46D02C943Q38335962-A8B501A2-F74E-48C7-A09F-0924EF8A9D8AQ39646018-2E46926D-ADBC-4BDE-87A1-5EC00853CE58Q39727806-2D173E20-D1CF-4436-9B1C-C7DE918258A2Q41002702-27FB9E86-2632-480D-9057-55C461C727B7Q41960449-8F2BF7EF-F125-4AFA-A9EB-9CCC81E97EC8Q46799723-C1772ADF-C334-4ABA-AFBE-9FAD19643B1FQ53600241-E4589481-A91B-4283-89CE-243A215D70FB
P2860
The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage.
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին 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
The limited strand-separating ...... the recognition of DNA damage.
@ast
The limited strand-separating ...... the recognition of DNA damage.
@en
type
label
The limited strand-separating ...... the recognition of DNA damage.
@ast
The limited strand-separating ...... the recognition of DNA damage.
@en
prefLabel
The limited strand-separating ...... the recognition of DNA damage.
@ast
The limited strand-separating ...... the recognition of DNA damage.
@en
P2860
P356
P1433
P1476
The limited strand-separating ...... the recognition of DNA damage.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/16.4.889
P407
P577
1997-02-01T00:00:00Z