Crystal structure ofEscherichia coliUvrB C-terminal domain, and a model for UvrB-UvrC interaction-Reference-Cited by-同舟云学术

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Crystal structure ofEscherichia coliUvrB C-terminal domain, and a model for UvrB-UvrC interaction

Published:2000-01-14 Issue:2-3 Volume:465 Page:161-164
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Sohi Maninder,Alexandrovich Alexander,Moolenaar Geri,Visse Rob,Goosen Nora,Vernede Xavier,Fontecilla-Camps Juan C.,Champness John,Sanderson Mark R.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(99)01690-7/fullpdf

Reference21 articles.

1. DNA EXCISION REPAIR

2. Nucleotide excision repair in Escherichia coli

3. The C-terminal Region of the UvrB Protein of Escherichia coli Contains an Important Determinant for UvrC Binding to the Preincision Complex but Not the Catalytic Site for 3′-Incision

4. Characterization of the Escherichia coliDamage-independent UvrBC Endonuclease Activity

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1. Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER;Nucleic Acids Research;2023-03-03

2. Helicases required for nucleotide excision repair: structure, function and mechanism;History of The Enzymes, Current Topics and Future Perspectives;2023

3. A Peek Inside the Machines of Bacterial Nucleotide Excision Repair;International Journal of Molecular Sciences;2021-01-19

4. Deciphering the essentiality and function of SxSx motif in Mycobacterium tuberculosis UvrB;Biochimie;2020-03

5. A combined structural and biochemical approach reveals translocation and stalling of UvrB on the DNA lesion as a mechanism of damage verification in bacterial nucleotide excision repair;DNA Repair;2020-01

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