The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase  and increases its DNA substrate utilisation efficiency: implications for DNA repair

By Toueille Magali   El-Andaloussi Nazim   Frouin Isabelle   Freire Raimundo  

Nucleic Acids Research, Vol. 32, Iss. 11, 2004-01 ,pp. : 3316-3324

Oxford University Press

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Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1

By Rappas Mathieu   Oliver Antony W.   Pearl Laurence H.  

Nucleic Acids Research, Vol. 41, Iss. 8, 2013-04 ,pp. : 4741-4741

Oxford University Press

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Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1

By Rappas Mathieu  

Nucleic Acids Research, Vol. 39, Iss. 1, 2011-01 ,pp. : 313-324

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 

By Post Sean M.   Tomkinson Alan E.   Lee Eva Y.‐H. P.  

Nucleic Acids Research, Vol. 31, Iss. 19, 2003-10 ,pp. : 5568-5575

Oxford University Press

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The human Rad9 checkpoint protein stimulates the carbamoyl phosphate synthetase activity of the multifunctional protein CAD

By Lindsey-Boltz Laura A.  

Nucleic Acids Research, Vol. 32, Iss. 15, 2004-01 ,pp. : 4524-4530

Oxford University Press

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