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You searched for +publisher:"Vanderbilt University" +contributor:("Richard N. Armstrong"). Showing records 1 – 18 of 18 total matches.

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Vanderbilt University

1. Nannemann, David Patrick. Directed Biosynthesis of the Nucleoside Analog Drug Didanosine.

Degree: PhD, Chemistry, 2011, Vanderbilt University

 Nucleoside analogs comprise a large therapeutic class applied to the treatment of HIV, hepatitis, and other diseases. Their broad use and applicability are in contrast… (more)

Subjects/Keywords: Enzyme Engineering; Bioretrosynthesis; Computational Enzyme Design; Directed Evolution; Purine Nucleoside Phosphorylase; Phosphopentomutase

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APA (6th Edition):

Nannemann, D. P. (2011). Directed Biosynthesis of the Nucleoside Analog Drug Didanosine. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu//available/etd-04042011-165321/ ;

Chicago Manual of Style (16th Edition):

Nannemann, David Patrick. “Directed Biosynthesis of the Nucleoside Analog Drug Didanosine.” 2011. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu//available/etd-04042011-165321/ ;.

MLA Handbook (7th Edition):

Nannemann, David Patrick. “Directed Biosynthesis of the Nucleoside Analog Drug Didanosine.” 2011. Web. 10 Jul 2020.

Vancouver:

Nannemann DP. Directed Biosynthesis of the Nucleoside Analog Drug Didanosine. [Internet] [Doctoral dissertation]. Vanderbilt University; 2011. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu//available/etd-04042011-165321/ ;.

Council of Science Editors:

Nannemann DP. Directed Biosynthesis of the Nucleoside Analog Drug Didanosine. [Doctoral Dissertation]. Vanderbilt University; 2011. Available from: http://etd.library.vanderbilt.edu//available/etd-04042011-165321/ ;


Vanderbilt University

2. Duggan, Kelsey Constance. Structural and Functional Analysis of Cyclooxygenase-2 Inhibition by Non-Steroidal Anti-Inflammatory Drugs.

Degree: PhD, Biochemistry, 2011, Vanderbilt University

 The cyclooxygenase enzymes (COX-1 and COX-2) catalyze the conversion arachidonic acid (AA) to prostaglandin H2 (PGH2), which is the precursor to biologically active prostanoids. The… (more)

Subjects/Keywords: naproxen; prostaglandins; cyclooxygenase; non-steroidal anti-inflammatory drugs

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APA (6th Edition):

Duggan, K. C. (2011). Structural and Functional Analysis of Cyclooxygenase-2 Inhibition by Non-Steroidal Anti-Inflammatory Drugs. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-01142011-132702/ ;

Chicago Manual of Style (16th Edition):

Duggan, Kelsey Constance. “Structural and Functional Analysis of Cyclooxygenase-2 Inhibition by Non-Steroidal Anti-Inflammatory Drugs.” 2011. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-01142011-132702/ ;.

MLA Handbook (7th Edition):

Duggan, Kelsey Constance. “Structural and Functional Analysis of Cyclooxygenase-2 Inhibition by Non-Steroidal Anti-Inflammatory Drugs.” 2011. Web. 10 Jul 2020.

Vancouver:

Duggan KC. Structural and Functional Analysis of Cyclooxygenase-2 Inhibition by Non-Steroidal Anti-Inflammatory Drugs. [Internet] [Doctoral dissertation]. Vanderbilt University; 2011. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-01142011-132702/ ;.

Council of Science Editors:

Duggan KC. Structural and Functional Analysis of Cyclooxygenase-2 Inhibition by Non-Steroidal Anti-Inflammatory Drugs. [Doctoral Dissertation]. Vanderbilt University; 2011. Available from: http://etd.library.vanderbilt.edu/available/etd-01142011-132702/ ;


Vanderbilt University

3. Fenn, Larissa Spell. Detection and characterization of glycans and glycoconjugates using ion mobility-mass spectrometry.

Degree: PhD, Chemistry, 2010, Vanderbilt University

 Many of the diseases associated with glycoprotein variation can be more effectively treated with earlier detection substantiating the need for high-throughput methodologies for glycoconjugate characterization.… (more)

Subjects/Keywords: collision cross section; ion mobility; mass spectrometry; glycoproteomics; glycomics; carbohydrate

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APA (6th Edition):

Fenn, L. S. (2010). Detection and characterization of glycans and glycoconjugates using ion mobility-mass spectrometry. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-04122010-131814/ ;

Chicago Manual of Style (16th Edition):

Fenn, Larissa Spell. “Detection and characterization of glycans and glycoconjugates using ion mobility-mass spectrometry.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-04122010-131814/ ;.

MLA Handbook (7th Edition):

Fenn, Larissa Spell. “Detection and characterization of glycans and glycoconjugates using ion mobility-mass spectrometry.” 2010. Web. 10 Jul 2020.

Vancouver:

Fenn LS. Detection and characterization of glycans and glycoconjugates using ion mobility-mass spectrometry. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-04122010-131814/ ;.

Council of Science Editors:

Fenn LS. Detection and characterization of glycans and glycoconjugates using ion mobility-mass spectrometry. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-04122010-131814/ ;


Vanderbilt University

4. Musee, Joel. Determinants of cyclooxygenase-2-mediated oxidative metabolism of the endocannabinoid, 2-arachidonoyl glycerol, in vitro and ex vivo.

Degree: PhD, Biochemistry, 2011, Vanderbilt University

 DETERMINANTS OF CYCLOOXYGENASE-2-MEDIATED OXIDATIVE METABOLISM OF THE ENDOCANNABINOID, 2-ARACHIDONOYL GLYCEROL, IN VITRO AND EX VIVO Joel Musee Dissertation under the direction of Professor Lawrence J.… (more)

Subjects/Keywords: prostaglandins; PGHS; COX; endocannabinoid; 2-arachidonoyl glycerol; analgesia; pain

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APA (6th Edition):

Musee, J. (2011). Determinants of cyclooxygenase-2-mediated oxidative metabolism of the endocannabinoid, 2-arachidonoyl glycerol, in vitro and ex vivo. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-04012011-233806/ ;

Chicago Manual of Style (16th Edition):

Musee, Joel. “Determinants of cyclooxygenase-2-mediated oxidative metabolism of the endocannabinoid, 2-arachidonoyl glycerol, in vitro and ex vivo.” 2011. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-04012011-233806/ ;.

MLA Handbook (7th Edition):

Musee, Joel. “Determinants of cyclooxygenase-2-mediated oxidative metabolism of the endocannabinoid, 2-arachidonoyl glycerol, in vitro and ex vivo.” 2011. Web. 10 Jul 2020.

Vancouver:

Musee J. Determinants of cyclooxygenase-2-mediated oxidative metabolism of the endocannabinoid, 2-arachidonoyl glycerol, in vitro and ex vivo. [Internet] [Doctoral dissertation]. Vanderbilt University; 2011. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-04012011-233806/ ;.

Council of Science Editors:

Musee J. Determinants of cyclooxygenase-2-mediated oxidative metabolism of the endocannabinoid, 2-arachidonoyl glycerol, in vitro and ex vivo. [Doctoral Dissertation]. Vanderbilt University; 2011. Available from: http://etd.library.vanderbilt.edu/available/etd-04012011-233806/ ;


Vanderbilt University

5. Birmingham, William Ross. Bioretrosynthetic Construction of a Non-Natural Nucleoside Analog Biosynthetic Pathway.

Degree: PhD, Biochemistry, 2013, Vanderbilt University

 Engineered biocatalysts have become increasingly sought after as replacements for individual chemical synthetic steps. However, their implementation in multistep sequences as biosynthetic pathways has proven… (more)

Subjects/Keywords: directed evolution; retrograde evolution; bioretrosynthesis; dideoxyinosine; phosphopentomutase; ribokinase

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APA (6th Edition):

Birmingham, W. R. (2013). Bioretrosynthetic Construction of a Non-Natural Nucleoside Analog Biosynthetic Pathway. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-11212013-085213/ ;

Chicago Manual of Style (16th Edition):

Birmingham, William Ross. “Bioretrosynthetic Construction of a Non-Natural Nucleoside Analog Biosynthetic Pathway.” 2013. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-11212013-085213/ ;.

MLA Handbook (7th Edition):

Birmingham, William Ross. “Bioretrosynthetic Construction of a Non-Natural Nucleoside Analog Biosynthetic Pathway.” 2013. Web. 10 Jul 2020.

Vancouver:

Birmingham WR. Bioretrosynthetic Construction of a Non-Natural Nucleoside Analog Biosynthetic Pathway. [Internet] [Doctoral dissertation]. Vanderbilt University; 2013. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-11212013-085213/ ;.

Council of Science Editors:

Birmingham WR. Bioretrosynthetic Construction of a Non-Natural Nucleoside Analog Biosynthetic Pathway. [Doctoral Dissertation]. Vanderbilt University; 2013. Available from: http://etd.library.vanderbilt.edu/available/etd-11212013-085213/ ;


Vanderbilt University

6. Keithly, Mary Elizabeth. Structure, substrate selectivity, and catalytic mechanism of the fosfomycin resistance enzyme, FosB, from Gram-positive pathogens.

Degree: PhD, Chemistry, 2016, Vanderbilt University

 Structure, substrate selectivity, and catalytic mechanism of the fosfomycin resistance enzyme, FosB, from Gram-positive pathogens By: Mary E. Keithly Fosfomycin, a broad spectrum antibiotic, is… (more)

Subjects/Keywords: Microbial antibiotic resistance; fosfomycin; FosB; Gram-positive

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APA (6th Edition):

Keithly, M. E. (2016). Structure, substrate selectivity, and catalytic mechanism of the fosfomycin resistance enzyme, FosB, from Gram-positive pathogens. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-07072016-115310/ ;

Chicago Manual of Style (16th Edition):

Keithly, Mary Elizabeth. “Structure, substrate selectivity, and catalytic mechanism of the fosfomycin resistance enzyme, FosB, from Gram-positive pathogens.” 2016. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-07072016-115310/ ;.

MLA Handbook (7th Edition):

Keithly, Mary Elizabeth. “Structure, substrate selectivity, and catalytic mechanism of the fosfomycin resistance enzyme, FosB, from Gram-positive pathogens.” 2016. Web. 10 Jul 2020.

Vancouver:

Keithly ME. Structure, substrate selectivity, and catalytic mechanism of the fosfomycin resistance enzyme, FosB, from Gram-positive pathogens. [Internet] [Doctoral dissertation]. Vanderbilt University; 2016. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-07072016-115310/ ;.

Council of Science Editors:

Keithly ME. Structure, substrate selectivity, and catalytic mechanism of the fosfomycin resistance enzyme, FosB, from Gram-positive pathogens. [Doctoral Dissertation]. Vanderbilt University; 2016. Available from: http://etd.library.vanderbilt.edu/available/etd-07072016-115310/ ;

7. Prage, Edward B. Structural Studies of Inhibition of the Human Inducible Prostaglandin E Synthase MPGES1.

Degree: PhD, Chemistry, 2012, Vanderbilt University

 The inducible enzyme microsomal prostaglandin E synthase 1 (MPGES1) is a glutathione-dependent prostaglandin H2 isomerase that has been implicated in a variety of inflammatory diseases… (more)

Subjects/Keywords: MAPEG; Eicosanoids; Inflammation; MPGES1; H/D Exchange

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APA (6th Edition):

Prage, E. B. (2012). Structural Studies of Inhibition of the Human Inducible Prostaglandin E Synthase MPGES1. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-02202012-105424/ ;

Chicago Manual of Style (16th Edition):

Prage, Edward B. “Structural Studies of Inhibition of the Human Inducible Prostaglandin E Synthase MPGES1.” 2012. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-02202012-105424/ ;.

MLA Handbook (7th Edition):

Prage, Edward B. “Structural Studies of Inhibition of the Human Inducible Prostaglandin E Synthase MPGES1.” 2012. Web. 10 Jul 2020.

Vancouver:

Prage EB. Structural Studies of Inhibition of the Human Inducible Prostaglandin E Synthase MPGES1. [Internet] [Doctoral dissertation]. Vanderbilt University; 2012. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-02202012-105424/ ;.

Council of Science Editors:

Prage EB. Structural Studies of Inhibition of the Human Inducible Prostaglandin E Synthase MPGES1. [Doctoral Dissertation]. Vanderbilt University; 2012. Available from: http://etd.library.vanderbilt.edu/available/etd-02202012-105424/ ;

8. Hu, Yunfeng. Microbial biosynthesis of benzodiazepines and nitrosugar containing natural products.

Degree: PhD, Chemistry, 2009, Vanderbilt University

 The biosyntheses of benzodiazepines and nitrosugar containing natural products in actinomycetes were investigated. The first biosynthetic gene cluster of a benzodiazepine natural product was identified… (more)

Subjects/Keywords: nitrosugar; benzodiazepines; biosynthesis; natural products

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APA (6th Edition):

Hu, Y. (2009). Microbial biosynthesis of benzodiazepines and nitrosugar containing natural products. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-05192009-102618/ ;

Chicago Manual of Style (16th Edition):

Hu, Yunfeng. “Microbial biosynthesis of benzodiazepines and nitrosugar containing natural products.” 2009. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-05192009-102618/ ;.

MLA Handbook (7th Edition):

Hu, Yunfeng. “Microbial biosynthesis of benzodiazepines and nitrosugar containing natural products.” 2009. Web. 10 Jul 2020.

Vancouver:

Hu Y. Microbial biosynthesis of benzodiazepines and nitrosugar containing natural products. [Internet] [Doctoral dissertation]. Vanderbilt University; 2009. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-05192009-102618/ ;.

Council of Science Editors:

Hu Y. Microbial biosynthesis of benzodiazepines and nitrosugar containing natural products. [Doctoral Dissertation]. Vanderbilt University; 2009. Available from: http://etd.library.vanderbilt.edu/available/etd-05192009-102618/ ;

9. Al-Mestarihi, Ahmad H. Oxidation of deoxyaminosugars by a new flavin-dependent monooxygenase.

Degree: PhD, Chemistry, 2012, Vanderbilt University

 This research work aims to provide biochemical characterization of the enzyme(s) responsible for deoxyaminosugar oxidation in several glycosylated natural products. The enzyme homologues ORF36 and… (more)

Subjects/Keywords: Everninomicin; Baumycin; DnmZ; Monooxygenase; Nitrososynthase; Deoxysugars

…work possible. The graduate school at Vanderbilt University also provided me with financial… …friends at Vanderbilt University, thank you very much for your friendship and support. You made… 

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APA (6th Edition):

Al-Mestarihi, A. H. (2012). Oxidation of deoxyaminosugars by a new flavin-dependent monooxygenase. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-12052012-152927/ ;

Chicago Manual of Style (16th Edition):

Al-Mestarihi, Ahmad H. “Oxidation of deoxyaminosugars by a new flavin-dependent monooxygenase.” 2012. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-12052012-152927/ ;.

MLA Handbook (7th Edition):

Al-Mestarihi, Ahmad H. “Oxidation of deoxyaminosugars by a new flavin-dependent monooxygenase.” 2012. Web. 10 Jul 2020.

Vancouver:

Al-Mestarihi AH. Oxidation of deoxyaminosugars by a new flavin-dependent monooxygenase. [Internet] [Doctoral dissertation]. Vanderbilt University; 2012. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-12052012-152927/ ;.

Council of Science Editors:

Al-Mestarihi AH. Oxidation of deoxyaminosugars by a new flavin-dependent monooxygenase. [Doctoral Dissertation]. Vanderbilt University; 2012. Available from: http://etd.library.vanderbilt.edu/available/etd-12052012-152927/ ;

10. Carter, Melissa Diane. Hemozoin: A Paradigm for Biomineralization in Disease.

Degree: PhD, Chemistry, 2009, Vanderbilt University

 Biomineralization is the formation of organic-inorganic composites by organisms. Originally evolved as a protective mechanism, this complex process has also become a recognized contributor to… (more)

Subjects/Keywords: lipid peroxidation; HTS; HETE; HNE; beta-hematin; hemozoin; malaria; schistosomiasis

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APA (6th Edition):

Carter, M. D. (2009). Hemozoin: A Paradigm for Biomineralization in Disease. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu//available/etd-07152009-140729/ ;

Chicago Manual of Style (16th Edition):

Carter, Melissa Diane. “Hemozoin: A Paradigm for Biomineralization in Disease.” 2009. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu//available/etd-07152009-140729/ ;.

MLA Handbook (7th Edition):

Carter, Melissa Diane. “Hemozoin: A Paradigm for Biomineralization in Disease.” 2009. Web. 10 Jul 2020.

Vancouver:

Carter MD. Hemozoin: A Paradigm for Biomineralization in Disease. [Internet] [Doctoral dissertation]. Vanderbilt University; 2009. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu//available/etd-07152009-140729/ ;.

Council of Science Editors:

Carter MD. Hemozoin: A Paradigm for Biomineralization in Disease. [Doctoral Dissertation]. Vanderbilt University; 2009. Available from: http://etd.library.vanderbilt.edu//available/etd-07152009-140729/ ;

11. Branch, Megan Christine. Exploring New Structural and Functional Space in the Glutathione Transferase Superfamily from Escherichia coli K-12.

Degree: PhD, Biochemistry, 2011, Vanderbilt University

 Genome sequencing projects have revealed that glutathione (GSH) transferases are widely distributed in bacteria but most remain only as annotations in sequenced genomes. The goal… (more)

Subjects/Keywords: yfcg; assignment of enzyme function; escherichia coli; glutathione; glutathione transferase; e. coli; yghu; yqjG

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APA (6th Edition):

Branch, M. C. (2011). Exploring New Structural and Functional Space in the Glutathione Transferase Superfamily from Escherichia coli K-12. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu//available/etd-07012011-143800/ ;

Chicago Manual of Style (16th Edition):

Branch, Megan Christine. “Exploring New Structural and Functional Space in the Glutathione Transferase Superfamily from Escherichia coli K-12.” 2011. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu//available/etd-07012011-143800/ ;.

MLA Handbook (7th Edition):

Branch, Megan Christine. “Exploring New Structural and Functional Space in the Glutathione Transferase Superfamily from Escherichia coli K-12.” 2011. Web. 10 Jul 2020.

Vancouver:

Branch MC. Exploring New Structural and Functional Space in the Glutathione Transferase Superfamily from Escherichia coli K-12. [Internet] [Doctoral dissertation]. Vanderbilt University; 2011. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu//available/etd-07012011-143800/ ;.

Council of Science Editors:

Branch MC. Exploring New Structural and Functional Space in the Glutathione Transferase Superfamily from Escherichia coli K-12. [Doctoral Dissertation]. Vanderbilt University; 2011. Available from: http://etd.library.vanderbilt.edu//available/etd-07012011-143800/ ;

12. Mushrush, Darren J. Mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes.

Degree: PhD, Biochemistry, 2011, Vanderbilt University

 Botulinum neurotoxin (BoNT) belongs to a large class of toxic proteins that act by enzymatically modifying cytosolic substrates within eukaryotic cells. The process by which… (more)

Subjects/Keywords: liposomes; EPR; fluorescence; bacterial toxin; biophysics

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APA (6th Edition):

Mushrush, D. J. (2011). Mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-08252011-124331/ ;

Chicago Manual of Style (16th Edition):

Mushrush, Darren J. “Mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes.” 2011. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-08252011-124331/ ;.

MLA Handbook (7th Edition):

Mushrush, Darren J. “Mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes.” 2011. Web. 10 Jul 2020.

Vancouver:

Mushrush DJ. Mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes. [Internet] [Doctoral dissertation]. Vanderbilt University; 2011. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-08252011-124331/ ;.

Council of Science Editors:

Mushrush DJ. Mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes. [Doctoral Dissertation]. Vanderbilt University; 2011. Available from: http://etd.library.vanderbilt.edu/available/etd-08252011-124331/ ;

13. Brown, Daniel W. The Evolution of Fosfomycin Resistance Enzyme, FosA, from Pseudomonas aeruginosa and the Development of a High-Throughput Screen for the Discovery of Bioactive Inhibitors.

Degree: PhD, Chemistry, 2010, Vanderbilt University

 Fosfomycin is a broad-spectrum antibiotic that has been underused due to the nature of the resistance mounted against it by various microorganisms. The work presented… (more)

Subjects/Keywords: evolution; enzyme; high-throughput; screen; fosfomycin; antibiotic; resistance

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APA (6th Edition):

Brown, D. W. (2010). The Evolution of Fosfomycin Resistance Enzyme, FosA, from Pseudomonas aeruginosa and the Development of a High-Throughput Screen for the Discovery of Bioactive Inhibitors. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-05242010-103718/ ;

Chicago Manual of Style (16th Edition):

Brown, Daniel W. “The Evolution of Fosfomycin Resistance Enzyme, FosA, from Pseudomonas aeruginosa and the Development of a High-Throughput Screen for the Discovery of Bioactive Inhibitors.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-05242010-103718/ ;.

MLA Handbook (7th Edition):

Brown, Daniel W. “The Evolution of Fosfomycin Resistance Enzyme, FosA, from Pseudomonas aeruginosa and the Development of a High-Throughput Screen for the Discovery of Bioactive Inhibitors.” 2010. Web. 10 Jul 2020.

Vancouver:

Brown DW. The Evolution of Fosfomycin Resistance Enzyme, FosA, from Pseudomonas aeruginosa and the Development of a High-Throughput Screen for the Discovery of Bioactive Inhibitors. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-05242010-103718/ ;.

Council of Science Editors:

Brown DW. The Evolution of Fosfomycin Resistance Enzyme, FosA, from Pseudomonas aeruginosa and the Development of a High-Throughput Screen for the Discovery of Bioactive Inhibitors. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-05242010-103718/ ;

14. Loecken, Elisabeth Mary. DNA-Protein Cross-Links Induced by Bis-Electrophiles.

Degree: PhD, Biochemistry, 2010, Vanderbilt University

 Diepoxybutane is a mutagenic and carcinogenic oxidation product of the important industrial chemical and environmental contaminant butadiene. The mutagenic potential of diepoxybutane is thought to… (more)

Subjects/Keywords: carcinogens; bis-electrophiles; DNA damage; DNA-protein cross-links

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APA (6th Edition):

Loecken, E. M. (2010). DNA-Protein Cross-Links Induced by Bis-Electrophiles. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-04102010-225656/ ;

Chicago Manual of Style (16th Edition):

Loecken, Elisabeth Mary. “DNA-Protein Cross-Links Induced by Bis-Electrophiles.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-04102010-225656/ ;.

MLA Handbook (7th Edition):

Loecken, Elisabeth Mary. “DNA-Protein Cross-Links Induced by Bis-Electrophiles.” 2010. Web. 10 Jul 2020.

Vancouver:

Loecken EM. DNA-Protein Cross-Links Induced by Bis-Electrophiles. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-04102010-225656/ ;.

Council of Science Editors:

Loecken EM. DNA-Protein Cross-Links Induced by Bis-Electrophiles. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-04102010-225656/ ;


Vanderbilt University

15. Beihoffer, Lauren Ashley. Mechanistic Insights into Fosfomycin Resistance: Examination of the FosX Class of Fosfomycin Resistance Proteins.

Degree: MS, Biochemistry, 2005, Vanderbilt University

 The objective of this research was to examine the FosX class of metalloenzymes utilized by pathogenic microorganisms for resistance to the antibiotic fosfomycin. Fosfomycin is… (more)

Subjects/Keywords: protein purification; Drug resistance in microorganisms; Fosfomycin; stopped flow spectroscopy; antibiotic resistance; minimum inhibitory concentration of fosfomycin

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APA (6th Edition):

Beihoffer, L. A. (2005). Mechanistic Insights into Fosfomycin Resistance: Examination of the FosX Class of Fosfomycin Resistance Proteins. (Masters Thesis). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-11212005-132421/ ;

Chicago Manual of Style (16th Edition):

Beihoffer, Lauren Ashley. “Mechanistic Insights into Fosfomycin Resistance: Examination of the FosX Class of Fosfomycin Resistance Proteins.” 2005. Masters Thesis, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-11212005-132421/ ;.

MLA Handbook (7th Edition):

Beihoffer, Lauren Ashley. “Mechanistic Insights into Fosfomycin Resistance: Examination of the FosX Class of Fosfomycin Resistance Proteins.” 2005. Web. 10 Jul 2020.

Vancouver:

Beihoffer LA. Mechanistic Insights into Fosfomycin Resistance: Examination of the FosX Class of Fosfomycin Resistance Proteins. [Internet] [Masters thesis]. Vanderbilt University; 2005. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-11212005-132421/ ;.

Council of Science Editors:

Beihoffer LA. Mechanistic Insights into Fosfomycin Resistance: Examination of the FosX Class of Fosfomycin Resistance Proteins. [Masters Thesis]. Vanderbilt University; 2005. Available from: http://etd.library.vanderbilt.edu/available/etd-11212005-132421/ ;


Vanderbilt University

16. Rigsby, Rachel Pharris. Studies of a genomic fosfomycin resistance protein from Pseudomonas aeruginosa.

Degree: PhD, Chemistry, 2005, Vanderbilt University

 CHEMISTRY STUDIES OF A GENOMIC FOSFOMYCIN RESISTANCE PROTEIN FROM PSEUDOMONAS AERUGINOSA RACHEL PHARRIS RIGSBY Dissertation under the direction of Professor Richard N. Armstrong In the… (more)

Subjects/Keywords: antibiotic resistance; fosfomycin resistance

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Rigsby, R. P. (2005). Studies of a genomic fosfomycin resistance protein from Pseudomonas aeruginosa. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-06282005-084134/ ;

Chicago Manual of Style (16th Edition):

Rigsby, Rachel Pharris. “Studies of a genomic fosfomycin resistance protein from Pseudomonas aeruginosa.” 2005. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-06282005-084134/ ;.

MLA Handbook (7th Edition):

Rigsby, Rachel Pharris. “Studies of a genomic fosfomycin resistance protein from Pseudomonas aeruginosa.” 2005. Web. 10 Jul 2020.

Vancouver:

Rigsby RP. Studies of a genomic fosfomycin resistance protein from Pseudomonas aeruginosa. [Internet] [Doctoral dissertation]. Vanderbilt University; 2005. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-06282005-084134/ ;.

Council of Science Editors:

Rigsby RP. Studies of a genomic fosfomycin resistance protein from Pseudomonas aeruginosa. [Doctoral Dissertation]. Vanderbilt University; 2005. Available from: http://etd.library.vanderbilt.edu/available/etd-06282005-084134/ ;


Vanderbilt University

17. Thompson, Lawrence Casper. Dynamic, Structural, and Mechanistic Study of Glutathione Transferases.

Degree: PhD, Biochemistry, 2006, Vanderbilt University

 This project involved the investigation of both the dynamic features of the dimer interface of the Mu class GSH transferase rGSTM1-1, as well as, the… (more)

Subjects/Keywords: hcca isomerase; hydrogen-deuterium exchange mass spectrometry; glutathione cofactor; isomerization; glutathione binding; mechanistic enzymology; transient state kinetics; crystallography; naphthalene metabolism; Xenobiotics  – Metabolism; phase II enzymes; xenobiotic catabolism; kappa glutathione transferases; dimer stability; Glutathione transferase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Thompson, L. C. (2006). Dynamic, Structural, and Mechanistic Study of Glutathione Transferases. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-06232006-122911/ ;

Chicago Manual of Style (16th Edition):

Thompson, Lawrence Casper. “Dynamic, Structural, and Mechanistic Study of Glutathione Transferases.” 2006. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-06232006-122911/ ;.

MLA Handbook (7th Edition):

Thompson, Lawrence Casper. “Dynamic, Structural, and Mechanistic Study of Glutathione Transferases.” 2006. Web. 10 Jul 2020.

Vancouver:

Thompson LC. Dynamic, Structural, and Mechanistic Study of Glutathione Transferases. [Internet] [Doctoral dissertation]. Vanderbilt University; 2006. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-06232006-122911/ ;.

Council of Science Editors:

Thompson LC. Dynamic, Structural, and Mechanistic Study of Glutathione Transferases. [Doctoral Dissertation]. Vanderbilt University; 2006. Available from: http://etd.library.vanderbilt.edu/available/etd-06232006-122911/ ;


Vanderbilt University

18. Weiner, Brian Edward. Biochemical and structural analysis of the p58C and p68N domains of DNA polymerase alpha/primase.

Degree: PhD, Biochemistry, 2008, Vanderbilt University

 The replication of DNA occurs through a complex series of steps involving the coordinated action of many proteins. DNA polymerase alpha/primase (pol-prim) is a critical… (more)

Subjects/Keywords: DNA polymerases  – Structure; T antigen; DNA primase; DNA polymerase alpha; DNA replication; SV40; NMR solution structure

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Weiner, B. E. (2008). Biochemical and structural analysis of the p58C and p68N domains of DNA polymerase alpha/primase. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-07222008-151325/ ;

Chicago Manual of Style (16th Edition):

Weiner, Brian Edward. “Biochemical and structural analysis of the p58C and p68N domains of DNA polymerase alpha/primase.” 2008. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-07222008-151325/ ;.

MLA Handbook (7th Edition):

Weiner, Brian Edward. “Biochemical and structural analysis of the p58C and p68N domains of DNA polymerase alpha/primase.” 2008. Web. 10 Jul 2020.

Vancouver:

Weiner BE. Biochemical and structural analysis of the p58C and p68N domains of DNA polymerase alpha/primase. [Internet] [Doctoral dissertation]. Vanderbilt University; 2008. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-07222008-151325/ ;.

Council of Science Editors:

Weiner BE. Biochemical and structural analysis of the p58C and p68N domains of DNA polymerase alpha/primase. [Doctoral Dissertation]. Vanderbilt University; 2008. Available from: http://etd.library.vanderbilt.edu/available/etd-07222008-151325/ ;

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