Cysteine residues contribute to the dimerization and enzymatic activity of human nuclear dUTP nucleotidohydrolase (nDut)-Reference-Cited by-同舟云学术

Cysteine residues contribute to the dimerization and enzymatic activity of human nuclear dUTP nucleotidohydrolase (nDut)

Published:2018-09-24 Issue:10 Volume:27 Page:1797-1809
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Rotoli Shawna M.¹,Jones Julia L.²,Caradonna Salvatore J.¹

Affiliation:

1. Department of Molecular Biology; Rowan University, School of Osteopathic Medicine and Graduate School of Biomedical Sciences; New Jersey 08084 Stratford

2. Department of Cell Biology; Rowan University, School of Osteopathic Medicine and Graduate School of Biomedical Sciences; Stratford New Jersey 08084

Funder

New Jersey Health Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.3481/fullpdf

Reference29 articles.

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4. Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases;Vertessy;Acc Chem Res,2009

5. Evolution of the dUTPase gene of mammalian and avian herpesviruses;McGeehan;Curr Protein Pept Sci,2001

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