| Carlson, Russell | E-mail: rcarlson@ccrc.uga.edu | | Dr. Carlson's research is directed toward characterizing the molecular basis for the interaction between a bacterium and a plant or animal host cell. One system under examination is the nitrogen-fixing symbiotic infection of legumes by rhizobia. These nitrogen-fixing soil bacteria contain genes that are activated by flavonoid molecules produced by the host plant. These genes encode enzymes which synthesize a glycolipid which is an acylated chitin oligosaccharide. In most cases, the glycolipids produced by each Rhizobium species are structurally modified which results in their ability to interact only with a specific legume plant. This molecular recognition process results in the stimulation of cell division in the legume root causing a nodule to form. The cells in this nodule are invaded by the rhizobia and are where nitrogenase is produced which reduces dinitrogen to ammonia. Other molecules on the surface of rhizobia that are required for the invasion of the root nodule cells by these bacteria are the outer membrane capsular and lipopolysaccharides. Specific structural changes occur in these molecules in response to the host plant which are crucial for infection. These structural changes, and the genes that are responsible for them, are presently under investgation. Dr. Carlson also has projects directed toward characterizing the role that bacterial lipopolysaccharides and lipooligosaccharides play in determining the pathogenicity of such organisms as Salmonella enteritidis, Neiserria meningiditis, and Hemophilus influenzae. Both the plant symbiont and animal pathogen work are being done in collaboration with several research groups in other universities. Dr. Carlson's research is currently funded by two grants from the USDA, one grant from the NSF, and one grant from the NIH. | | Keywords: The structures and roles of bacterial glycoconjugates in microbe-plant and -animal interactions |
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| Dailey, Harry | E-mail: hdailey@uga.edu | | Heme is a key and essential compound for the vast majority of living organisms. Heme, as a cofactor in a variety of proteins, is widely acknowledged to be essential for gas transport, respiration, xenobiotic detoxification, peroxide production and destruction, fatty acid desaturation, and a variety of one electron transfer reactions. Over the past decade the number of roles identified for heme has grown substantially. It has become clear that heme is also an important intracellular regulatory ligand. Among the list of biological processes for which higher eucaryotic heme-binding proteins have now been implicated is regulation of circadian rhythm, adipogenesis, glucose homeostasis, microRNA processing, gas sensing, control of ion channels, and intra- and intercellular signal transduction. The list of bacterial heme-binding sensors seems to grow with each new journal publication, and the role of the heme-containing DevS-DevR proteins of Mycobacterium tuberculosis as regulators of passage into the dormant stage has attracted considerable attention for obvious biomedical reasons. Dietary heme also serves as a significant source of iron for many organisms including pathogenic bacteria. A search of PubMed for “heme” yields over 2500 listed publications in the past year.
The Dailey lab’s research focuses on the enzymes responsible for heme biosynthesis. Current studies involve structure/function investigations of the terminal enzymes of heme biosynthesis and their relationship to the human genetic diseases known as porphyrias, biochemical characterization of the enzymes from both eukaryotic and prokaryotic organisms, identification and characterization of novel and previously unidentified genes involved in heme synthesis and transport, protein-protein interactions among heme synthesis enzymes, and regulation of expression and translocation of heme synthetic enzymes.
| | Keywords: Studies on the regulation of heme synthesis and structure/function of heme pathway enzymes |
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| Dalton, Stephen | E-mail: sdalton@uga.edu | | For further information go to www.daltonlab.uga.edu and www.sestemcells.uga.edu
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Our work focuses on the generation of therapeutically useful cell types that can be used to treat cardiovascular disease, diabetes, stroke, autoimmune disease, spinal cord injury and neurological diseases. | | Keywords: stem cells,
cell therapy,
diabetes,
cardiovascular disease,
developmental biology.
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| Hajduk, Stephen | E-mail: shajduk@bmb.uga.edu | | Analysis of the function of RNA editing in the mitochondrion of African trypanosomes using a combination of biochemical, proteomic, informatic and molecular approaches. Evaluation of the mechanism of human innate immunity to African trypanosomes. | | Keywords: RNA Editing; Mitochondrial Biogenesis; African Trypanosomes; Innate Immunity; High Density Lipoproteins |
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| Kannan, Natarajan | E-mail: kannan@bmb.uga.edu | | Research in my lab is at the intersection of genome biology, evolutionary biology and computational structural biology. We combine techniques and approaches from these diverse disciplines to understand the underlying mechanisms of signaling proteins in atomic detail. | | Keywords: genomics, cancer informatics, evolutionary systems biology, computational structural biology, protein phosphorylation |
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| Moremen, Kelley | E-mail: moremen@uga.edu | | Research in the Moremen lab focuses on the structure, enzymology, regulation, and localization of enzymes involved in the biosynthesis, recognition, and catabolism of mammalian glycoproteins. Carbohydrate structures on glycoproteins contribute to many biological recognition events between molecules and between cells in an organism. Alterations in the synthesis and degradation of these structures can also occur in human genetic disease. Work in the Moremen lab is focused on (1) the characterization of enzymes involved in mammalian glycoprotein biosynthesis and catabolism and the functionally defective forms of these enzymes involved in human genetic disease and (2) the identification and characterization of carbohydrate-binding proteins and their roles in vertebrate development and physiology. | | Keywords: Biochemistry, molecular, and structural biology of mammalian glycoprotein biosynthesis and catabolism |
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| Przybyla, Alan | E-mail: przybyla@bmb.uga.edu | | | Keywords: Our laboratory employs recombinant technology to investigate the role of beta amyloid peptide fibrilization in the onset of Alzheimer |
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| Rose, John | E-mail: rose@bcl4.bmb.uga.edu | | X-ray structural biology, the mitochondrial inner membrane space transport system, structure based vaccine and therapeutic design, improved/automated methods for synchrotron SAD data collection and structure determination. | | Keywords: mitochondrial inner membrane transport, structure assisted vaccine and therapeutic design, improved/automated methods for SAD structure determination |
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| Sabatini, Robert | E-mail: rsabatini@bmb.uga.edu | | We are trying understand how the protozoan parasite, Trypanosoma brucei, regulates telomeric gene expression and evades the host immune response. Our current focus is on the role of the novel DNA base, base J, in regulating telomeric homologous recombination events (a major mechanism | | Keywords: Biosynthesis and function of modified DNA. Regulation of gene expression, DNA recombination and parasite pathogenesis. African and South American Trypanosomes. |
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| Schmidt, Walter | E-mail: wschmidt@bmb.uga.edu | | Research in our lab is focused on proteases:
The CaaX proteases: Rce1 and Ste24 mediate a proteolytic cleavage event associated with the maturation of proteins that contain a covalently attached isoprenyl lipid at their C-terminus (e.g. Ras, nuclear lamins, fungal pheromones). We are investigating the mechanism and specificity of these proteases in an effort to better understand their role in human disease (e.g. Ras and cancer; lamins and progeria).
The M16A proteases: Ste23 and Axl1 yeast members of the M16A subfamily of metalloproteases. This subfamily includes the human insulin-degrading enzyme, which mediates degradation of amyloidogenic peptides such as the Abeta peptide associated with Alzheimer’s disease. We are investigating the mechanism and specificity of these enzymes to better understand their physiological role in the cell. | | Keywords: proteases, CaaX proteins, isoprenylation, cancer, Alzheimer's disease, yeast |
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| Steet, Richard | E-mail: rsteet@ccrc.uga.edu | | Our laboratory utilizes multiple model systems including zebrafish to study the developmental consequences of impaired lysosomal catabolism of glycoproteins. We are focused on understanding how the mislocalization and inappropriate activity of specific enzymes impacts the normal development and function of several tissues including cartilage. | | Keywords: Pathogenic mechanisms of lysosomal storage disorders, Golgi trafficking, cartilage biology. |
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| Terns, Michael | E-mail: mterns@bmb.uga.edu | Two major research projects in the Terns Lab:
- Telomerase and cancer: We are investigating the regulation of the biogenesis and transport of the telomerase RNP, a key molecule in the processes of aging and cancer. Telomerase maintains telomeres at the ends of chromosomes. Telomerase activity and telomere length are lost with aging, resulting in cell senescence and death. In order to be able to grow indefinitely, nearly all cancer cells re-activate telomerase. Thus telomerase is a promising target for anti-cancer and anti-aging therapies. In cancer cells, we have found that the two essential components of telomerase (telomerase RNA and TERT) travel distinct, cell cycle-regulated pathways within the nucleus that culminate in co-localization at telomeres during S phase for telomere synthesis. We are working to identify the factors responsible for the regulated activity of telomerase in normal and cancer cells.
- Virus defense in prokaryotes: All bacteria (including human pathogens) are subject to attack by viruses and other genome invaders. We are working to delineate a newly-identified RNA-mediated pathway that protects bacteria and archaea from viruses and other invaders. The pathway appears to parallel the eukaryotic RNAi pathway and is referred to as "prokaryotic RNAi". This is a very exciting new research area with significant biomedical and biotechnological importance.
| | Keywords: non-coding RNAs, RNA-protein complexes, regulation of telomerase, cancer, RNAi, virus defense |
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| Urbauer, Jeffrey | E-mail: urbauer@chem.uga.edu | | Our research focuses on protein structure and function and protein-protein interactions. We employ an approach combining modern analytical, biophysical and molecular biology techniques, with an emphasis on biomolecular NMR spectroscopy. Our core projects include the study of gene regulation and novel regulators of transcription initiation in bacteria, oxidative stress and calcium signaling, steroid hormone (estrogen) receptor activation, and regulation of biofilm formation and pathogenesis in Pseudomonas aeruginosa. These projects are important fundamentally, and they important biomedically with respect to antibiotic target development, oxidative stress and biological aging, and diseases such as breast cancer and cystic fibrosis. | | Keywords: Transcription regulation, steroid hormone receptors, estrogen receptor, breast cancer, oxidative stress, calcium signaling, calmodulin, NMR spectroscopy, physical biochemistry |
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| Wang, Lianchun | E-mail: lwang@ccrc.uga.edu | | Research in the Wang laboratory focuses on the structure and function of heparan sulfate proteoglycans in vasculature and cancer biology. Heparan sulfate proteoglycans are glycoconjugates which are abundant on the cell surface and in the extracellular matrix. In vitro studies have suggested that heparan sulfate proteoglycans interact with growth factors, growth factor binding proteins, extracellular proteases, protease inhibitors, chemokines, morphogens, and cell adhesive proteins to modulate cell differentiation, proliferation, migration, blood coagulation, lipid metabolism, and leukocyte trafficking. However, the biological and pathological functions of heparan sulfate proteoglycans in vivo are still largely unknown. Using techniques, including conditional mouse gene targeting, embryonic stem (ES) cell differentiation, primary cell culture, and mouse models, the Wang lab is aiming to understand the roles and the underlying mechanisms of heparan sulfate proteoglycan in vascular development, cancer biology and blood coagulation in vivo, and to develop novel approaches to cure the related pathological conditions. | | Keywords: Heparan sulfate proteoglycan, angiogenesis, tumorigenesis, tumor metastasis, stem cell, coagulation |
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| Wells, Lance | E-mail: lwells@ccrc.uga.edu | | Our laboratory is interested in how post-translational modifications of proteins increase functional diversity. Primarily, we are interested in glycosylation, with a focus on 1. O-GlcNAc in Type II diabetes and stem cell biology , 2. O-Mannosylation in Congenital Muscular Dystrophy and viral entry into host cells, 3. Glycoproteins as biomarkers in human disease, specifically pancreatic cancer and metabolic syndrome, 4. Development of technology-based approaches, primarily mass-spectrometry, for quantitive proteomics/glycomics/glycoproteomics. | | Keywords: O-glycoslyation, type II diabetes, congenital muscular dystrophy, cancer, glyco/proteomics. |
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| Woods, Robert | E-mail: rwoods@ccrc.uga.edu | | The focus of my group's research is to examine the relationships between carbohydrate conformation and biological recognition and activity. We are particularly interested in the mechanisms of carbohydrate recognition in the immune system. Current research projects include examinations of bacterial antigen-antibody interactions, as well as other carbohydrate-protein interactions. The carbohydrate antigens associated with bacteria, such as Salmonella paratyphi B and group B Streptococcus are being studied in order to quantify the contributions made by hydrophobic and hydrophilic interactions. In conjunction with experimental methods (NMR and X-ray), we apply molecular dynamics simulations with the GLYCAM parameters and the AMBER force field. | | Keywords: Immunological carbohydrate-protein interactions studied by computational simulation and experimental methods |
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