Millie M. Georgiadis

Rutgers University, New Brunswick, New Brunswick, NJ, United States 
"Millie Georgiadis"
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Wilson DM, Deacon AM, Duncton MAJ, et al. (2020) Fragment- and structure-based drug discovery for developing therapeutic agents targeting the DNA Damage Response. Progress in Biophysics and Molecular Biology
Georgiadis MM, Chen Q, Meng J, et al. (2016) Small molecule activation of apurinic/apyrimidinic endonuclease 1 reduces DNA damage induced by cisplatin in cultured sensory neurons. Dna Repair. 41: 32-41
He H, Singh I, Wek SA, et al. (2014) Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals. The Journal of Biological Chemistry. 289: 15023-34
Zhang J, Luo M, Marasco D, et al. (2013) Inhibition of apurinic/apyrimidinic endonuclease I's redox activity revisited. Biochemistry. 52: 2955-66
Luo M, Zhang J, He H, et al. (2012) Characterization of the redox activity and disulfide bond formation in apurinic/apyrimidinic endonuclease. Biochemistry. 51: 695-705
Kelley MR, Georgiadis MM, Fishel ML. (2012) APE1/Ref-1 role in redox signaling: translational applications of targeting the redox function of the DNA repair/redox protein APE1/Ref-1. Current Molecular Pharmacology. 5: 36-53
Kim YJ, Kim D, Illuzzi JL, et al. (2011) S-glutathionylation of cysteine 99 in the APE1 protein impairs abasic endonuclease activity. Journal of Molecular Biology. 414: 313-26
Onyango DO, Naguleswaran A, Delaplane S, et al. (2011) Base excision repair apurinic/apyrimidinic endonucleases in apicomplexan parasite Toxoplasma gondii. Dna Repair. 10: 466-75
Su D, Delaplane S, Luo M, et al. (2011) Interactions of apurinic/apyrimidinic endonuclease with a redox inhibitor: evidence for an alternate conformation of the enzyme. Biochemistry. 50: 82-92
Kelley MR, Luo M, Reed A, et al. (2011) Functional analysis of novel analogues of E3330 that block the redox signaling activity of the multifunctional AP endonuclease/redox signaling enzyme APE1/Ref-1. Antioxidants & Redox Signaling. 14: 1387-401
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