The Administrative Core of the Program Project, Structure and Funcfion of DNA Repair Enzymes, will be responsible for coordinating all of the administrative aspects of the program and for facilitating interactions among the Project and Core Directors, Senior Investigators, and their laboratory members. The overall goal is to insure the successful conduct of the research proposed in this application. The management of the DNA Repair Program will be coordinated by the Principal Investigator/Administrative Core Director, Dr. Susan Wallace, with an Executive Committee comprised of Drs. Bond, Doubli6, Morrical, Pederson and Sweasy. Specifically the aims ofthe Core are:
Aim 1. To provide administrative support for the Projects and Cores A and B, Aim 2. To monitor the scientific progress of the Projects by facilitafing monthly meefings of the Program Project participants.
Aim 3. To facilitate meefings with the External and Internal Advisory Boards.

Public Health Relevance

The studies resulfing from this Program will provide insight into how the BER and RAD51 variants in the in the normal population and in tumors may contribute to altereed DNA repair capacity. Hence, this project will both contribute to our understanding of laasic cancer biology and may provide the basis for new approaches to cancer therapy.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Program Projects (P01)
Project #
5P01CA098993-09
Application #
8543555
Study Section
Special Emphasis Panel (ZCA1-RPRB-0)
Project Start
Project End
Budget Start
2013-09-01
Budget End
2014-08-31
Support Year
9
Fiscal Year
2013
Total Cost
$139,925
Indirect Cost
$89,515
Name
University of Vermont & St Agric College
Department
Type
DUNS #
066811191
City
Burlington
State
VT
Country
United States
Zip Code
05405
Lee, Andrea J; Wallace, Susan S (2016) Visualizing the Search for Radiation-damaged DNA Bases in Real Time. Radiat Phys Chem Oxf Engl 1993 128:126-133
Prakash, Aishwarya; Cao, Vy Bao; Doublié, Sylvie (2016) Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase. PLoS One 11:e0157860
Cannan, Wendy J; Pederson, David S (2016) Mechanisms and Consequences of Double-Strand DNA Break Formation in Chromatin. J Cell Physiol 231:3-14
Marsden, Carolyn G; Jensen, Ryan B; Zagelbaum, Jennifer et al. (2016) The Tumor-Associated Variant RAD51 G151D Induces a Hyper-Recombination Phenotype. PLoS Genet 12:e1006208
Silva, Michelle C; Morrical, Milagros D; Bryan, Katie E et al. (2016) RAD51 variant proteins from human lung and kidney tumors exhibit DNA strand exchange defects. DNA Repair (Amst) 42:44-55
Zhou, Jia; Fleming, Aaron M; Averill, April M et al. (2015) The NEIL glycosylases remove oxidized guanine lesions from telomeric and promoter quadruplex DNA structures. Nucleic Acids Res 43:4039-54
Chen, Jianhong; Morrical, Milagros D; Donigan, Katherine A et al. (2015) Tumor-associated mutations in a conserved structural motif alter physical and biochemical properties of human RAD51 recombinase. Nucleic Acids Res 43:1098-111
Morrical, Scott W (2015) DNA-pairing and annealing processes in homologous recombination and homology-directed repair. Cold Spring Harb Perspect Biol 7:a016444
Prakash, Aishwarya; Doublié, Sylvie (2015) Base Excision Repair in the Mitochondria. J Cell Biochem 116:1490-9
Prakash, Aishwarya; Carroll, Brittany L; Sweasy, Joann B et al. (2014) Genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase: activity, structure, and the effect of editing. DNA Repair (Amst) 14:17-26

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