Talk abstracts
Wednesday 09:00-09:15am: Dynamic Control of DNA Origami Nanostructures Via Gold Nanoparticles
Joshua Johnson (Biophysics Program), Abhilasha Dehankar (Department of Chemical and Biochemical Engineering), Jessica Winter (Department of Chemical and Biochemical Engineering and Department of BIomedical Engineering), Carlos Castro (Departments of Mechanical and Aerospace Engineering)
Abstract:
A major direction of research in DNA origami is the folding of DNA into complex 3D shapes with the inclusion of flexible regions to form dynamic nanomachines that approximate macroscale machine elements. These types of dynamic nanostructures are typically actuated via the addition DNA “fuel” strands that form new connections to reconfigure a structure, or via the selective removal of DNA components via strand displacement. Previous work has shown that DNA origami mechanisms can be actuated on relatively slow time scales usually requiring several minutes to several hours to transition between states. The goal of this work is to enable novel actuation methods with distinct, and potentially faster, triggering mechanisms based on incorporating other nanomaterial components. While DNA origami has been used in combination with other nanomaterials such as gold nanoparticles there has yet to be a demonstration of nanoparticles used for the precise control of nanostructure actuation. Using a DNA origami hinge mechanism we have included single-stranded DNA overhangs extending from the arms, which bind to a DNA-conjugated gold nanoparticle to latch the hinge closed. By varying where the nanoparticle is incorporated (distance from the hinge vertex) and the nanoparticle size we have shown that not only the average angles but also the angular distributions of the hinge are highly controllable as verified by transmission electron microscopy. In addition, tuning the nanoparticle binding affinity of the bottom arm relative to the top arm allows for actuation of the hinge via DNA melting without releasing the nanoparticle entirely, thereby enabling rapid and reversible temperature-based actuation. Particle binding and hinge actuation were monitored via a two color fluorescence quenching setup to reveal that the kinetics of actuation occur on the seconds timescale and is ultimately limited by heat diffusion into the sample volume. Actuating the hinge over several cycles shows no significant loss of function demonstrating that the nanoparticle hinge assembly is a robust tool for nanoscale manipulation. Future work will explore light-based actuation mediated by local plasmonic heating of the nanoparticles in both bulk fluorescence and single molecule experiments.
References:
1) Castro, Carlos Ernesto, et al. "A primer to scaffolded DNA origami." Nature methods 8.3 (2011): 221-229.
2) Castro, Carlos E., et al. "Mechanical design of DNA nanostructures."Nanoscale 7.14 (2015): 5913-5921.
3) Marras, Alexander E., et al. "Programmable motion of DNA origami mechanisms." Proceedings of the National Academy of Sciences 112.3 (2015): 713-718.
4) Gerling, Thomas, et al. "Dynamic DNA devices and assemblies formed by shape-complementary, non–base pairing 3D components." Science 347.6229 (2015): 1446-1452.
Keywords: DNA origami, nanotechnology, nanoparticles
Wednesday 09:15-09:30am: Unexpected mechanistic features of a multifunctional tRNA methyltransferase.
Aiswarya Krishnamohan (Ohio State Biochemistry Program), Jane Jackman (Department of Chemistry and Biochemistry, The Ohio State University)
Abstract not available online - please check the printed booklet.
Wednesday 09:30-09:45am: Pnrc2 promotes rapid clearance of oscillating transcripts through 3’UTR interactions
Kiel T. Tietz (Molecular, Cellular and Developmental Biology), Thomas L. Gallagher (Molecular Genetics, The Ohio State University, Columbus), Nicolas L. Derr (Molecular Genetics, The Ohio State University, Columbus), zachary T. Morrow (molecular Genetics, The Ohio State University, Columbus)
Abstract:
Vertebrate segmentation is regulated by the segmentation clock, a biological oscillator that controls embryonic segmentation (somitogenesis). This molecular oscillator generates cyclic gene expression in the tissue that generates somites, called the presomitic mesoderm (PSM), and has the same periodicity as somite formation. Molecular components of the clock include the hairy/Enhancer of split-related (her/Hes) family of transcriptional repressors, but additional transcripts also cycle. Maintenance of clock oscillations requires that transcriptional activation and repression, RNA turnover, translation, and protein degradation are all rapid (e.g., one cycle is 30 minutes in the zebrafish). We previously isolated a zebrafish segmentation clock mutant, tortuga, that have elevated cyclic transcript levels. We show that loss of proline-rich nuclear receptor coactivator protein Pnrc2 is responsible for cyclic transcript accumulation in tortuga deletion mutants by creating a new pnrc2 loss-of-function mutation and showing that cyclic transcript accumulation is identical in pnrc2 and tortuga mutants. pnrc2 mRNA is maternally provided and zygotically expressed, but Pnrc2 protein is not detected until just before somitogenesis begins. In maternal-zygotic pnrc2 mutants, cyclic transcripts perdure even longer, indicating that maternally-provided pnrc2 functions to promote cyclic transcript turnover. We show that the her1 3’UTR confers instability to otherwise stable transcripts in vivo in a Pnrc2-dependent manner, supporting our hypothesis that the 3’UTR of cyclic transcripts is critical for Pnrc2-mediated decay. To identify elements and factors required for rapid cyclic transcript turnover, we are defining minimal her1 3’UTR regions that are necessary and sufficient for rapid transcript decay. Our work will uncover post-transcriptional mechanisms regulating oscillation dynamics and cell fate during somitogenesis that may also be relevant for other biological patterns generated by oscillatory gene expression.
Keywords: her1, RNA Decay, 3UTR
Wednesday 09:45-10:00am: Title not available online - please see the printed booklet.
Daniel B. McKim (Neuroscience Graduate Program), Jonathan P. Godbout (Department of Neuroscience), John F. Sheridan (College of Dentistry)
Abstract not available online - please check the printed booklet.
Wednesday 10:20-10:40am: Contribution of prefrontal GABAergic transmission to neurodevelopmental and neuropsychiatric disorders
Laurence Coutellier (Speaker selected by Neuroscience Graduate Program students)
Abstract:
The prefrontal cortex (PFC) exerts a top-down control on various limbic and sub-cortical regions that regulate emotion, reward processing and cognitive functions. Prefrontal disturbances are thus believed to contribute to multiple aspects of neurodevelopmental and neuropsychiatric conditions, including attention and contextual information processing deficits in schizophrenia, hyperactivity in autism, or lack of motivation and anhedonia in depression. Disruptions of prefrontal functions can occur either during development or during adulthood through the action of genetic or environmental insults. In adolescence, the PFC undergoes drastic functional and structural changes, defining a period of extreme vulnerability. In adulthood, the PFC is also known to be particularly sensitive to the effects of stress. Because the functioning of the PFC is determined by the fine tuning of network oscillations that are mostly orchestrated by local GABAergic inhibitory interneurons, it is likely that disruption of the prefrontal GABAergic system contributes to abnormal communication between the PFC and downstream regions and to behavioral abnormalities characteristic of psychiatric disorders. In this talk I will present experimental evidence in mice demonstrating that genetic- or environmental-induced disturbances of the prefrontal GABAergic system during adolescence and adulthood contribute to cognitive and emotional impairments.
Keywords:
Wednesday 10:40-11:00am: Elongation factor P - dependent regulation of gene expression
Michael Ibba (Speaker selected by Biochemistry Graduate Program Students)
Abstract not available online - please check the printed booklet.
Wednesday 11:00-11:20am: Discovering a new role for NF-kB in cell migration during neonatal muscle development
Denis Guttridge (Speaker selected by Molecular, Cellular and Developmental Biology Graduate Program Students)
Abstract:
Skeletal muscle growth immediately following birth is a critical stage of development needed for proper body posture and locomotion. However, compared to embryogenesis and adulthood, the processes regulating the maturation of neonatal muscles is considerably less clear. Studies in the 1960s had predicted that muscle growth results from nuclear accretion of myoblasts preferentially at the tips of immature myofibers. Remarkably, since that time, little information has been added to resolve how myoblasts migrate to the ends of a fiber for nuclear accretion to occur. Here, we provide insight to this process by revealing a unique NF-κB dependent communication between NG2+ interstitial cells and myoblasts. NF-κB is active in NG2+ cells to promote myoblasts migration through cell-cell contact to the tips of growing myofibers. This occurs through expression of ephrinA5 from NG2+ cells, which we further deduce is an NF-κB target gene. Together, results suggest that NF-κB plays an important role in the development of newborn muscles to ensure proper myoblast migration for fiber growth.
Keywords:
Wednesday 11:20-11:40am: Magnetic Quantum Dots for Cancer Diagnostics
Jessica Winter (Speaker selected by Biophysics Graduate Program Students)
Abstract:
Methods employing fluorescence for biosensing are well established using organic dyes. However, quantum dots offer several advantages to fluorescent dyes, most notably the potential for the detection of multiple biomarkers through multiplexed imaging, which is enhanced by their narrow emission bandwidth. Quantum dot biosensing can be further enhanced by combination with magnetic separation methods via the recent development of magnetic quantum dots. An advantage of magnetic quantum dot (MQDs)-based separation to current approaches is the small size of MQDs, which are small enough to potentially interact with single biomarkers/cell surface receptors, thus enabling relative quantization of results. MQDs can be independently manipulated by engineering magnetic fields, and can also be used to isolate molecules and cells for downstream analysis. Early stage clinical results will be reported using detection of circulating tumor cells via Her-2 expression in metastatic breast cancer patients as a model. Collectively, these results indicate a promising future for potential commercialization of biosensing technologies based on quantum dots and their magnetic quantum dot counterparts.
Keywords:
Wednesday 03:00-03:15pm: Spinal cord injury suppresses cutaneous inflammation: implications for peripheral wound healing
Jessica M. Marbourg (Neuroscience Graduate Program), Anna Bratasz (Small Animal Imaging Shared Resources, Ohio State University), Xiaokui Mo (Center for Biostatistics, Ohio State University), Phillip G. Popovich (Department of Neuroscience, Ohio State University)
Abstract not available online - please check the printed booklet.
Wednesday 03:00-03:15pm: Title not available online - please see the printed booklet.
Sharon R. Cooper (MCDB), Michelle R. Emond, Brandon G. Liebau, Phan Q. Duy (Department of Neuroscience, Ohio State University), Marc A.Wolman (Department of Zoology, University of Wisconsin-Madison), James D. Jontes (Department of Neuroscience, Ohio State University), Marcos Sotomayor (Department of Chemistry and Biochemistry, Ohio State University)
Abstract not available online - please check the printed booklet.
Wednesday 03:15-03:30pm: Title not available online - please see the printed booklet.
Kaitlin Snider (Neuroscience Graduate Program), Heather Dziema (Department of Neuroscience, Ohio State University), Sydney Aten (Department of Neuroscience, Ohio State University), Jacob Loeser (Department of Neuroscience, Ohio State University), Frances E. Norona (Department of Neuroscience, Ohio State University), Karl Obrietan (Department of Neuroscience, Ohio State University)
Abstract not available online - please check the printed booklet.
Wednesday 03:15-03:30pm: Molecular mechanisms of inherited deafness due to missense mutations in cadherin-23
Avinash Jaiganesh (Biophysics graduate program, The Ohio State University)
Abstract not available online - please check the printed booklet.
Wednesday 03:30-03:45pm: NF-κB Regulates Suppression Of Macrophage Activity During Early Tumor Development
Nivedita M. Ratnam (Molecular, Cellular and Developmental Biology Program), Jennifer M. Peterson (Molecular Virology, Immunology and Medical Genetics), Benjamin J. Swanson (Department of Pathology), Terrance M. Williams (Department of Radiation Oncology), David J. Wang (Human Cancer genetics Program,Molecular Virology, Immunology and Medical Genetics), Denis C. Guttridge (Molecular Virology, Immunology and Medical Genetics)
Abstract not available online - please check the printed booklet.
Wednesday 03:30-03:45pm: RNA structure provides insights into mechanism of selective genome packaging by retroviral Gag
Erik D Olson (Ohio State Biochemistry Program, Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retroviral Research, The Ohio State University, Columbus, OH), William A Cantara (Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retroviral Research, The Ohio State University, Columbus, OH), Tiffiny Rye-McCurdy (Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retroviral Research, The Ohio State University, Columbus, OH), Brian R Thompson (Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retroviral Research, The Ohio State University, Columbus, OH), Ioulia Rouzina (Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retroviral Research, The Ohio State University, Columbus, OH), Karin Musier-Forsyth (Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retroviral Research, The Ohio State University, Columbus, OH)
Abstract not available online - please check the printed booklet.
Wednesday 03:45-04:00pm: Tumorigenic functions of splice variant MDM2-ALT1 in p53 wildtype and p53 null mouse models
Daniel Comiskey (MCDB), Aishwarya Jacob (MCDB), Brianne Sanford (MCDB), Aixa Tapia-Santos (MCDB), Dawn Chandler (MCDB)
Abstract not available online - please check the printed booklet.
Wednesday 03:45-04:00pm: Induced fit binding involving a dynamic helix confers specific recognition of mischarged Ala-tRNAPro by a bacterial trans-editing domain
Eric M. Danhart (Ohio State Biochemistry Program), Lexie Kuzmishin, Marina Bakhtina, Brianne Sanford (Department of Chemistry and Biochemistry, The Ohio State University), Marija Kosutic, Ronald L. Micura (Institute of Organic Chemistry and Center for Molecular Biosciences, Innsbruck CMBI Leopold Franzens University, Innsbruck, Austria), Karin Musier-Forsyth, Mark P. Foster (Department of Chemistry and Biochemistry, The Ohio State University)
Abstract:
Aminoacyl-tRNA synthetases catalyze the attachment of specific amino acids to cognate tRNAs. Mistakes in this process lead to errors in protein synthesis that can be deleterious or beneficial to cells. Prolyl-tRNA synthetase (ProRS) mischarges tRNAPro with Ala; this aberrant product is hydrolyzed by a cis-editing domain (INS) in most bacteria. Some bacteria that lack the INS domain encode a homologous free-standing trans-editing protein known as ProXp-ala that performs the same function. ProXp-ala displays acceptor stem specificity for tRNAPro, but how it discriminates between Pro-tRNAPro and Ala-tRNAPro is less clear. To establish the structural basis for this discrimination, NMR mapping studies were carried out with an uncharged microhelixPro substrate and with a non-hydrolyzable, amide-linked Ala-microhelixPro substrate analog. Chemical shift perturbations (CSPs) induced by each RNA allowed us to identify candidate residues of ProXp-ala involved in recognition of the Ala moiety. The largest CSPs were mapped to regions of the protein that surround a large electropositive area. 15N NMR relaxation experiments revealed a mobile α-helix (α2) that exhibits significant dynamics at the ps-ns timescale, which are attenuated in the presence of mischarged RNA. Deacylation assays showed only minor effect of mutating residues in helix α2 on activity, and computational studies support the conclusion that the dynamics are significantly attenuated only in the presence of the non-cognate aminoacyl-RNA moiety. Conserved residues proximal to helix α2 in 3D space that have significant effects on deacylation rates with little impact on RNA binding were also identified. Taken together, these results allow us to propose a mechanism for substrate recognition by ProXp-ala that involves Ala-specific induced-fit binding via a mobile helix.
Keywords: NMR, tRNA, Protein-RNA interaction
Wednesday 04:15-04:30pm: Ablation of the BRCA1-PALB2 interaction phenocopies Fanconi Anemia
Dongju Park (Molecular, Cellular & Developmental Biology), Stephen Bergin (Comprehensive Cancer Center), Christopher Koivisto (Comprehensive Cancer Center), Thomas Ludwig
Abstract:
Heterozygous mutations in the BRCA1 gene predispose women to breast and ovarian cancer, while biallelic BRCA1 (FANCS) mutations are a cause of Fanconi Anemia (FA). FA is a rare genetic disorder characterized by developmental abnormalities, early-onset bone marrow failure, increased risk of cancers, and hypersensitivity to DNA-crosslinking (ICL) agents. BRCA1 is critical for homology-directed repair (HDR) of DNA double strand breaks (DSBs). Through its coiled-coil domain, BRCA1 interacts with the adaptor protein PALB2 facilitating recruitment of BRCA2 and RAD51 to sites of DNA damage. Interestingly, missense mutations within the coiled-coil domain of BRCA1 (i.e. BRCA1 L1407P) that mediates the interaction with PALB2 have been reported among familial breast cancer patients.
Thus, we hypothesized that if PALB2 regulates and/or mediates BRCA1 tumor suppressor function, ablation of the BRCA1-PALB2 interaction may also elicit genomic instability and tumor susceptibility. To test this hypothesis and to examine the role of the BRCA1-PALB2 interaction in normal and malignant development, we have used a knock-in strategy and generated cells and mice that are defective for the BRCA1-PALB2 interaction (Brca1 L1363P in mice).
Homozygous mutant Brca1L1363P/L1363P pMEFs show impaired proliferation, spontaneous chromosomal aberrations and undergo premature senescence. In addition, mutant MEFs exhibit hypersensitivity to DNA damaging agents (MMC and Olaparib) and following ionizing radiation (IR), mutant cells fail to recruit Rad51 to sites of DNA damage.
Homozygous mutant Brca1L1363P/L1363P mice are viable but exhibit a variety of FA symptoms including growth retardation, hyper-/hypopigmentation, skeletal abnormalities, microphtalmia, and male and female infertility. Furthermore, hematological measurements on Brca1L1363P/L1363P mice showed all mutant animals exhibit macrocytosis and have either died due to bone marrow failure or the development of leukemia.
These results indicate that the BRCA1-PALB2 interaction is critical for the function of BRCA1 in HDR and ICL repair. Furthermore, the Brca1 L1363P knock-in mouse establishes a new disease model for FA.
Keywords: Fanconi Anemia (FA), BReast CAncer susceptibility gene 1 (BRCA1), Homology Directed Repair (HDR)
Wednesday 04:15-04:30pm: Characterization and Selection of Biophysically Optimized Antibody Fragments for Enhanced in vivo Tumor Imaging
Nick Emerson Long (OSBP), Brandon J. Sullivan (Ohio State Visiting Scholar), Thomas J. Magliery (Ohio State Department of Chemistry and Biochemistry)
Abstract not available online - please check the printed booklet.
Wednesday 04:30-04:45pm: Deciphering the roles of aspartate and histidine in the mechanism of the six-bladed β-propeller hydrolases
Timothy John Grunkemeyer (Ohio State Biochemistry Program), Kiran Doddapaneni (Department of Chemistry and Biochemistry), Srividya Murali (Department of Chemistry and Biochemistry), Gregory Friedberg (College of Arts and Sciences Neuroscience)
Abstract:
Each year over 3 million people are exposed to toxic organophosphorus compounds (OPs), which target the parasympathetic nervous system, leading to respiratory arrest and ultimately death. Since the current treatment is only moderately effective, we aim to generate a more effective therapeutic in the form of a catalytic bioscavenger. Paraoxonase-1 (PON1) has shown promise as a drug for OP treatment however, due to a plethora of conflicting evidence, its mechanism is poorly understood. This severely limits our abilities to engineer PON1 for improved activity and ultimately its therapeutic efficacy. In order to understand PON1’s mechanism, we aim to interrogate the active sites of the closely related six-bladed β-propeller hydrolases di-isopropylfluorophosphatase (DFPase), Drug responsive protein-35 (Drp35), and Senescence Marker Protein 30 (SMP30). We believe that all four enzymes operate via a common mechanism that can be elucidated through comparative enzymology and structural studies.
All four enzymes contain an upper calcium ligation sphere consisting of four residues: Asp, Glu, and two Asn. The residues of interest are this Asp and a His near the active site (His only present in PON1 and DFPase). It has been hypothesized that either of these residues can activate a water for substrate hydrolysis or attack the substrate directly forming an enzyme-substrate complex that is subsequently hydrolyzed. To test these hypotheses, we cloned, expressed, and purified a set of conservative mutations in all four enzymes. Subsequently, they were kinetically screened them against a panel of aryl esters, lactones, and OPs, and kcat/Km values were calculated to determine the effect on catalysis. In Asp to Asn mutations, we observe a complete loss in activity while the His to Phe mutants result in a 4x-8x increase in both kcat and Km in PON1 and DFPase. Interestingly, the His seems to be absent in both Drp35 and SMP30, being replaced with an Ala and Arg respectively. These observations argue against the His participating in catalysis, but supports its role in substrate binding. We believe these results support Asp being responsible for activity, whether directly or via water activation. Crystallographic analyses of notable mutants and 18O labeled water experiments are under way to decipher the Asp’s exact role in catalysis.
Keywords: hydrolase, organophosphate, bioscavenger
Wednesday 04:30-04:45pm: Title not available online - please see the printed booklet.
Nandini Shukla (The Ohio State Biochemistry Program, The Ohio State University ), Aysha H. Osmani (Dept. of Molecular Genetics, The Ohio State University ), Stephen A. Osmani (Dept. of Molecular Genetics, The Ohio State University )
Abstract not available online - please check the printed booklet.
Wednesday 04:45-05:00pm: MyoD Regulates Skeletal Muscle Oxidative Metabolism Cooperatively with Alternative NF-kB
Jonathan Shintaku (Molecular, Cellular, & Developmental Biology Graduate Program), Jennifer M. Peterson (Department of Molecular Virology, Immunology, & Medical Genetics, The Ohio State University), Jinmo Gu (Molecular, Cellular, & Developmental Biology Graduate Program), Ruoning Wang (Center for Childhood Cancer and Blood Diseases, The Research Institute at Nationwide Childrens Hospital), Vittorio Sartorelli (Laboratory of Muscle Stem Cells and Gene Regulation, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, Bethesda, Maryland), Denis C. Guttridge (Department of Molecular Virology, Immunology, & Medical Genetics, The Ohio State University)
Abstract not available online - please check the printed booklet.
Wednesday 04:45-05:00pm: The role of stromal estrogen receptor in mammary gland reprogramming following in utero BPA exposure
Andrea R. Patterson (Molecular, Cellular & Developmental Biology Program, Department of Molecular Genetics, and The Arthur G. James Comprehensive Cancer Center, Columbus, Ohio, USA ), Xiaokui Mo (Center for Biostatistics, Ohio State University Wexner Medical Center), Ali C. Shapiro (Department of Molecular Genetics, and The Arthur G. James Comprehensive Cancer Center, Columbus, Ohio, USA ), Hannah L. Helber, Nanditha Ravichandran (Department of Molecular Genetics, and The Arthur G. James Comprehensive Cancer Center, Columbus, Ohio, USA ), Claire E. Kovalchin (Life Sciences Education, The Ohio State University, Columbus, Ohio, USA), Craig J. Burd (Department of Molecular Genetics, and The Arthur G. James Comprehensive Cancer Center, Columbus, Ohio, USA )
Abstract:
In utero exposure to estrogenic compounds, collectively known as endocrine disrupting compounds (EDCs), is linked to increased risk for later life development of breast, uterine and cervical cancers. It is estimated that greater than 80% of breast cancers are attributable to environmental factors and significant evidence suggests that early life exposure to a known EDC, bisphenol A (BPA), is a contributor. While it is believed that activation of the estrogen receptor (ER) is critical for this pathogenesis, the molecular mechanisms are not defined. We utilized an in utero model to characterize the effects of BPA on mammary gland development. ERα expression was demonstrated to be strictly mesenchymal during early mammary bud formation despite evidence of epithelial defects in BPA-treated adult mammary glands. The gap between mesenchymal ER expression and later life epithelial defects led us to examine varied embryonic exposures to BPA in utero. We found that the different degrees of mammary gland defects were dependent on the varied embryonic exposure received. Further, we found early epithelial growth correlated to stromal proliferation. Gene expression and DNA methylation analyses of isolated adult mammary fibroblast, luminal and basal epithelial cell populations demonstrated cell type-specific effects of in utero BPA. Interestingly, extracellular signaling was a pathway significantly altered by BPA suggesting epithelial defects may be caused in part by inappropriate mesenchymal ER activation through paracrine-based signaling. These findings were supported by distinct epigenetic changes detected between these cell populations indicating discrete reprogramming mechanisms. Together, these data support a model by which mammary defects caused by in utero BPA results in reprogramming of the stroma distinct from epithelial cells. Later life defects in the epithelia may be a result of altered mesenchymal paracrine signals. Our analysis is the first of its kind to investigate alterations in the component cell populations of the mammary gland following in utero exposure to BPA and define the permanent epigenetic changes in the adult tissue. Our findings can later inform analysis of human populations, determining the mechanisms of deregulation that contribute to later life risk.
Keywords: endocrine disruption, bisphenol A, epigenetic
Wednesday 05:00-05:15pm: The N-terminal domains of DNA Polymerase Lambda regulate DNA damage response and repair
Anthony A. Stephenson (Chemistry and Biochemistry The Ohio State University), David J. Taggart (Chemistry and Biochemistry The Ohio State University), Shelby A. Newsad (Chemistry and Biochemistry The Ohio State University)
Abstract not available online - please check the printed booklet.
Wednesday 05:00-05:15pm: Title not available online - please see the printed booklet.
Catey Dominguez (MCDB), Dawn S. Chandler (MCDB)
Abstract not available online - please check the printed booklet.