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Skip to Search Results- 37Graduate and Postdoctoral Studies (GPS), Faculty of
- 37Graduate and Postdoctoral Studies (GPS), Faculty of/Theses and Dissertations
- 4Biological Sciences, Department of
- 4Biological Sciences, Department of/Journal Articles (Biological Sciences)
- 4Biochemistry, Department of
- 4Biochemistry, Department of/Journal Articles (Biochemistry)
- 12Department of Chemistry
- 9Department of Agricultural, Food, and Nutritional Science
- 3Department of Food Science
- 3Faculty of Pharmacy and Pharmaceutical Sciences
- 2Department of Agricultural, Food and Nutritional Science
- 2Department of Chemical and Materials Engineering
- 5Vederas, John (Chemistry)
- 4McMullen, Lynn (Agricultural, Food and Nutritional Science)
- 3Vederas, John C. (Chemistry)
- 2Unsworth, Larry (Chemical and Materials Engineering)
- 1Bressler, David (Agricultural, Food, and Nutritional Science)
- 1Bressler, David (Department of Agricultural, Food and Nutritional Science)
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Spring 2011
Several obstacles to widespread use of bacteriocins in food have been identified, including lack of specific, rapid quantitation methods, and little data on their efficacy in food systems. The first objective of this study was to develop a specific, rapid quantitation method for bacteriocins...
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2006
RNA helicases function as molecular motors that rearrange RNA secondary structure, potentially performing roles in any cellular process involving RNA metabolism. Although RNA helicase association with a range of cellular functions is well documented, their importance in response to abiotic stress...
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RNA structural rearrangement via unwinding and annealing by the cyanobacterial RNA helicase, CrhR
Download2005
Owttrim, George W., Chamot, Danuta, Kujat-Choy, Sonya L., Colvin, Kimberley R.
Rearrangement of RNA secondary structure is crucial for numerous biological processes. RNA helicases participate in these rearrangements through the unwinding of duplex RNA. We report here that the redox-regulated cyanobacterial RNA helicase, CrhR, is a bona fide RNA helicase possessing both...
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Structural and functional analysis of transmembrane segment VI of the NHE1 isoform of the na+/H+ exchanger
Download2009-01-01
Tzeng, Jennifer, Lee, Brian L., Sykes, Brian D., Fliegel, Larry
The Na+/H+ exchanger isoform 1 is a ubiquitously expressed integral membrane protein. It resides on the plasma membrane of cells and regulates intracellular pH in mammals by extruding an intracellular H+ in exchange for one extracellular Na+. We characterized structural and functional aspects of...
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Structural and functional analysis of transmembrane XI of the NHE1 isoform of the na+/H+ exchanger
Download2009-01-01
Lee, Brian L., Li, Xiuju J., Liu, Yongsheng, Sykes, Brian D., Fliegel, Larry
The Na+/H+ exchanger isoform 1 is a ubiquitously expressed integral membrane protein that regulates intracellular pH in mammals by extruding an intracellular H+ in exchange for one extracellular Na+. We characterized structural and functional aspects of the critical transmembrane (TM) segment XI...
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Structural and functional characterization of transmembrane segment IV of the NHE1 isoform of the na+/H+ exchanger
Download2005-01-01
Slepkov, Emily R., Rainey, Jan K., Li, Xiuju J., Liu, Yonghsheng S., Cheng, Florence J., Lindhout, Darrin A., Sykes, Brian D., Fliegel, Larry
The Na+/H+ exchanger isoform 1 is a ubiquitously expressed integral membrane protein that regulates intracellular pH in mammals. We characterized the structural and functional aspects of the critical transmembrane (TM) segment IV. Each residue was mutated to cysteine in cysteine-less NHE1. TM IV...
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Structural and functional characterization of transmembrane segment VII of the na+/H+ exchanger isoform 1
Download2006-01-01
Ding, Jie, Rainey, Jan K., Xu, Caroline, Sykes, Brian D., Fliegel, Larry
The Na+/H+ exchanger isoform 1 is an integral membrane protein that regulates intracellular pH by exchanging one intracellular H+ for one extracellular Na+. It is composed of an N-terminal membrane domain of 12 transmembrane segments and an intracellular C-terminal regulatory domain. We...
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Spring 2016
The lipopeptides, tridecaptin A1, tridecaptin B1 and cerexin A1 were isolated from Paenibacillus terrae NRRL B-30644, Paenibacillus polymyxa NRRL B-30507 and Bacillus mycoides ATCC 21929, respectively. A combination of chemical synthesis, peptide derivatization, high performance liquid...
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Fall 2014
Paenibacillus polymyxa NRRL B-30509, Paenibacillus terrae NRRL B-30644 and P. polymyxa NRRL B-30507 were found to produce several bacteriocins and non-ribosomal peptides. All three strains produce tridecaptins, non-ribosomal lipopeptides antimicrobially active against food pathogen Campylobacter...
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Fall 2012
Thuricin CD, a two-component bacteriocin produced by Bacillus thuringiensis DPC 6431, exhibits potent activity against the hospital superbug Clostridium difficile ribotype O27. The two peptides (Trn-α and Trn-β) that constitute thuricin CD operate synergistically to kill sensitive bacteria at...