The human checkpoint sensor Rad9–Rad1–Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase

By Guan Xin   Madabushi Amrita   Chang Dau-Yin   Fitzgerald Megan E.   Shi Gouli   Drohat Alexander C.   Lu A-Lien  

Nucleic Acids Research, Vol. 35, Iss. 18, 2007-09 ,pp. : 6207-6218

Oxford University Press

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The J Domain of Tpr2 Regulates Its Interaction with the Proapoptotic and Cell-Cycle Checkpoint Protein, Rad9

By Xiang S-L.   Kumano T.   Iwasaki S-i.   Sun X.   Yoshioka K.   Yamamoto K-c.  

Biochemical and Biophysical Research Communications, Vol. 287, Iss. 4, 2001-10 ,pp. : 932-940

Elsevier

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The checkpoint Saccharomyces cerevisiae Rad9 protein contains a tandem tudor domain that recognizes DNA

By Lancelot Nathalie  

Nucleic Acids Research, Vol. 35, Iss. 17, 2007-09 ,pp. : 5898-5912

Oxford University Press

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The human checkpoint Rad protein Rad17 is chromatin‐associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase 

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Nitrogen Excretion and Expression of Carbamoyl-phosphate Synthetase III Activity and mRNA in Extrahepatic Tissues of Largemouth Bass (Micropterus salmoides)

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Archives of Biochemistry and Biophysics, Vol. 350, Iss. 2, 1998-02 ,pp. : 157-168

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