Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2-Reference-Cited by-同舟云学术

Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2

Published:2017-09-06 Issue:1 Volume:12 Page:15-22
ISSN:1874-2718
Container-title:Biomolecular NMR Assignments
language:en
Short-container-title:Biomol NMR Assign

Author:

Buchinger Edith,Wiik Siv Å.,Kusnierczyk Anna,Rabe Renana,Aas Per. A.,Kavli Bodil,Slupphaug Geir,Aachmann Finn L.^ORCID

Funder

Norges Forskningsråd

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Structural Biology

Link

http://link.springer.com/article/10.1007/s12104-017-9772-5/fulltext.html

Reference15 articles.

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2. Blatny JM, Brautaset T, WintherLarsen HC, Karunakaran P, Valla S (1997) Improved broad-host-range RK2 vectors useful for high and low regulated gene expression levels in gram-negative bacteria. Plasmid 38:35–51

3. Hagen L et al (2008) Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA. EMBO J 27:51–61. doi: 10.1038/sj.emboj.7601958

4. Kavli B et al (2002) hUNG2 Is the Major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup. J Biol Chem 277:39926–39936. doi: 10.1074/jbc.M207107200

5. Keller R (2004) Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance. Assignment CANTINA Verlag, Zürich

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