Geraldine N. Nabeta
Emory University
Homologous recombinationCancerDNA repairFunction (biology)MutantMolecular biologyResectionReceptorPoly ADP ribose polymeraseKinaseSAMHD1Epidermal growth factor receptorGenome integrityControl cellCancer treatmentCancer researchRadiation therapyDNAMedicineBiologyCell biologyProtein kinase A
Publications 3
#1David S. YuH-Index: 22
Last. B. Kim
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#1Allyson E. Koyen (Emory University)H-Index: 5
#2Geraldine N. Nabeta (Emory University)H-Index: 1
Last. Waaqo Daddacha (Emory University)H-Index: 12
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Protein kinases play a vital role in the regulation of pathways that control cell growth, proliferation, survival, and differentiation. Epidermal growth factor receptor (EGFR) is a key protein kinase that when dysregulated, disrupts these pathways and, accordingly, is associated with several cancers. Thus, EGFR has been a focus of investigation as a therapeutic target for cancer treatment for the past several decades, with fair success. Despite this success, EGFR-targeted therapies are not unive...
#1Waaqo Daddacha (Emory University)H-Index: 12
#2Allyson E. Koyen (Emory University)H-Index: 5
Last. David S. Yu (Emory University)H-Index: 22
view all 28 authors...
Summary DNA double-strand break (DSB) repair by homologous recombination (HR) is initiated by CtIP/MRN-mediated DNA end resection to maintain genome integrity. SAMHD1 is a dNTP triphosphohydrolase, which restricts HIV-1 infection, and mutations are associated with Aicardi-Goutieres syndrome and cancer. We show that SAMHD1 has a dNTPase-independent function in promoting DNA end resection to facilitate DSB repair by HR. SAMHD1 deficiency or Vpx-mediated degradation causes hypersensitivity to DSB-i...
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