The C-terminal region of Escherichia coli UvrC contributes to the flexibility of the UvrABC nucleotide excision repair system.
about
Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triadCrystal Structure of Bacillus stearothermophilus UvrA Provides Insight into ATP-Modulated Dimerization, UvrB Interaction, and DNA BindingInvolvement of a carboxylated lysine in UV damage endonucleaseCrystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexesUV damage endonuclease employs a novel dual-dinucleotide flipping mechanism to recognize different DNA lesionsProkaryotic nucleotide excision repair.Robust incision of Benoz[a]pyrene-7,8-dihyrodiol-9,10-epoxide-DNA adducts by a recombinant thermoresistant interspecies combination UvrABC endonuclease systemCho Endonuclease Functions during DNA Interstrand Cross-Link Repair in Escherichia coli.Base flipping in nucleotide excision repair.
P2860
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P2860
The C-terminal region of Escherichia coli UvrC contributes to the flexibility of the UvrABC nucleotide excision repair system.
description
2002 nî lūn-bûn
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2002年の論文
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2002年論文
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name
The C-terminal region of Esche ...... eotide excision repair system.
@en
The C-terminal region of Esche ...... eotide excision repair system.
@nl
type
label
The C-terminal region of Esche ...... eotide excision repair system.
@en
The C-terminal region of Esche ...... eotide excision repair system.
@nl
prefLabel
The C-terminal region of Esche ...... eotide excision repair system.
@en
The C-terminal region of Esche ...... eotide excision repair system.
@nl
P2093
P2860
P356
P1476
The C-terminal region of Esche ...... eotide excision repair system.
@en
P2093
Esther E A Verhoeven
Geri F Moolenaar
Gijs A van der Marel
Jacques H van Boom
John J Turner
Marian van Kesteren
Nora Goosen
P2860
P304
P356
10.1093/NAR/30.11.2492
P407
P577
2002-06-01T00:00:00Z