Advanced search options

Advanced Search Options 🞨

Browse by author name (“Author name starts with…”).

Find ETDs with:

in
/  
in
/  
in
/  
in

Written in Published in Earliest date Latest date

Sorted by

Results per page:

Sorted by: relevance · author · university · dateNew search

You searched for +publisher:"Vanderbilt University" +contributor:("F. Peter Guengerich"). Showing records 1 – 14 of 14 total matches.

Search Limiters

Last 2 Years | English Only

No search limiters apply to these results.

▼ Search Limiters


Vanderbilt University

1. Sohl, Christal Dyane. Kinetic Analysis of the Multi-Step Cytochrome P450 1A2 and 19A1 Enzymes.

Degree: PhD, Biochemistry, 2010, Vanderbilt University

 The kinetic characterization of cytochrome P450s that catalyze multi-step, sequential reactions is the focus of this work. Two novel substrates were identified for P450 1A2,… (more)

Subjects/Keywords: global fitting; cooperativity; aromatase; enzymes; pre-steady-state kinetics; kinetics; P450s

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Sohl, C. D. (2010). Kinetic Analysis of the Multi-Step Cytochrome P450 1A2 and 19A1 Enzymes. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-06152010-090554/ ;

Chicago Manual of Style (16th Edition):

Sohl, Christal Dyane. “Kinetic Analysis of the Multi-Step Cytochrome P450 1A2 and 19A1 Enzymes.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-06152010-090554/ ;.

MLA Handbook (7th Edition):

Sohl, Christal Dyane. “Kinetic Analysis of the Multi-Step Cytochrome P450 1A2 and 19A1 Enzymes.” 2010. Web. 10 Jul 2020.

Vancouver:

Sohl CD. Kinetic Analysis of the Multi-Step Cytochrome P450 1A2 and 19A1 Enzymes. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-06152010-090554/ ;.

Council of Science Editors:

Sohl CD. Kinetic Analysis of the Multi-Step Cytochrome P450 1A2 and 19A1 Enzymes. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-06152010-090554/ ;


Vanderbilt University

2. 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

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

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

3. Xiao, Yi. Functional annotation of orphan human P450 enzymes: heterologous expression and substrate searches by metabolomic approaches.

Degree: PhD, Biochemistry, 2014, Vanderbilt University

 Cytochrome P450s are versatile biocatalysts that play crucial roles in many important biological processes. Functional annotation of orphan P450 enzymes is the focus of this… (more)

Subjects/Keywords: functional annotation; substrate searches; orphan human P450 enzyme; metabolomic approaches

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Xiao, Y. (2014). Functional annotation of orphan human P450 enzymes: heterologous expression and substrate searches by metabolomic approaches. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-09152014-151801/ ;

Chicago Manual of Style (16th Edition):

Xiao, Yi. “Functional annotation of orphan human P450 enzymes: heterologous expression and substrate searches by metabolomic approaches.” 2014. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-09152014-151801/ ;.

MLA Handbook (7th Edition):

Xiao, Yi. “Functional annotation of orphan human P450 enzymes: heterologous expression and substrate searches by metabolomic approaches.” 2014. Web. 10 Jul 2020.

Vancouver:

Xiao Y. Functional annotation of orphan human P450 enzymes: heterologous expression and substrate searches by metabolomic approaches. [Internet] [Doctoral dissertation]. Vanderbilt University; 2014. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-09152014-151801/ ;.

Council of Science Editors:

Xiao Y. Functional annotation of orphan human P450 enzymes: heterologous expression and substrate searches by metabolomic approaches. [Doctoral Dissertation]. Vanderbilt University; 2014. Available from: http://etd.library.vanderbilt.edu/available/etd-09152014-151801/ ;


Vanderbilt University

4. Albertolle, Matthew Edward. SULFENYLATION OF CYTOCHROMES P450 IN RESPONSE TO REDOX ALTERATION.

Degree: PhD, Biochemistry, 2019, Vanderbilt University

 Mammalian cytochrome P450 (P450) enzymes catalyze complex reactions involved in the biosynthesis of endogenous metabolites such as steroids, vitamins, and hormones. Additionally, several enzymes in… (more)

Subjects/Keywords: Cytochrome P450; Redox; Enzymology; Proteomics; Sulfenic Acid

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Albertolle, M. E. (2019). SULFENYLATION OF CYTOCHROMES P450 IN RESPONSE TO REDOX ALTERATION. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-01182019-000143/ ;

Chicago Manual of Style (16th Edition):

Albertolle, Matthew Edward. “SULFENYLATION OF CYTOCHROMES P450 IN RESPONSE TO REDOX ALTERATION.” 2019. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-01182019-000143/ ;.

MLA Handbook (7th Edition):

Albertolle, Matthew Edward. “SULFENYLATION OF CYTOCHROMES P450 IN RESPONSE TO REDOX ALTERATION.” 2019. Web. 10 Jul 2020.

Vancouver:

Albertolle ME. SULFENYLATION OF CYTOCHROMES P450 IN RESPONSE TO REDOX ALTERATION. [Internet] [Doctoral dissertation]. Vanderbilt University; 2019. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-01182019-000143/ ;.

Council of Science Editors:

Albertolle ME. SULFENYLATION OF CYTOCHROMES P450 IN RESPONSE TO REDOX ALTERATION. [Doctoral Dissertation]. Vanderbilt University; 2019. Available from: http://etd.library.vanderbilt.edu/available/etd-01182019-000143/ ;


Vanderbilt University

5. Zheng, Yuxiang. The mechanism and physiological function of epidermal lipoxygenase-3.

Degree: PhD, Pharmacology, 2010, Vanderbilt University

 The goal of my thesis research is to elucidate the catalytic mechanism and physiological function of the atypical mammalian lipoxygenase, epidermal lipoxygenase-3. Although named as… (more)

Subjects/Keywords: hydroperoxide; epoxyalcohol; skin; lipoxygenase; essential fatty acid

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Zheng, Y. (2010). The mechanism and physiological function of epidermal lipoxygenase-3. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu//available/etd-12032010-001429/ ;

Chicago Manual of Style (16th Edition):

Zheng, Yuxiang. “The mechanism and physiological function of epidermal lipoxygenase-3.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu//available/etd-12032010-001429/ ;.

MLA Handbook (7th Edition):

Zheng, Yuxiang. “The mechanism and physiological function of epidermal lipoxygenase-3.” 2010. Web. 10 Jul 2020.

Vancouver:

Zheng Y. The mechanism and physiological function of epidermal lipoxygenase-3. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu//available/etd-12032010-001429/ ;.

Council of Science Editors:

Zheng Y. The mechanism and physiological function of epidermal lipoxygenase-3. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu//available/etd-12032010-001429/ ;


Vanderbilt University

6. 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

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

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/ ;

7. Garmendia, Craig Alexander. In vitro replication studies of oligonucleotides containing site-specific DNA adducts in frameshift-prone sequences.

Degree: MS, Chemistry, 2008, Vanderbilt University

 Exposure to endogenous and exogenous chemicals can lead to modification of DNA and potentially lead to cancer. Frameshift mutations may be a consequence of these… (more)

Subjects/Keywords: Oligonucleotides  – Synthesis; Tandem Mass Spectrometry; Frameshift; DNA Adducts; Acrolein; Crotonaldehyde; Chemical carcinogenesis

…spectrometry was performed at the Vanderbilt University Mass Spectrometry Resource Center. 3… …and pol II¯ were obtained from the lab of Dr. Guengerich (Vanderbilt University)… 

Page 1 Page 2 Page 3 Page 4 Page 5

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Garmendia, C. A. (2008). In vitro replication studies of oligonucleotides containing site-specific DNA adducts in frameshift-prone sequences. (Masters Thesis). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-12042008-144306/ ;

Chicago Manual of Style (16th Edition):

Garmendia, Craig Alexander. “In vitro replication studies of oligonucleotides containing site-specific DNA adducts in frameshift-prone sequences.” 2008. Masters Thesis, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-12042008-144306/ ;.

MLA Handbook (7th Edition):

Garmendia, Craig Alexander. “In vitro replication studies of oligonucleotides containing site-specific DNA adducts in frameshift-prone sequences.” 2008. Web. 10 Jul 2020.

Vancouver:

Garmendia CA. In vitro replication studies of oligonucleotides containing site-specific DNA adducts in frameshift-prone sequences. [Internet] [Masters thesis]. Vanderbilt University; 2008. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-12042008-144306/ ;.

Council of Science Editors:

Garmendia CA. In vitro replication studies of oligonucleotides containing site-specific DNA adducts in frameshift-prone sequences. [Masters Thesis]. Vanderbilt University; 2008. Available from: http://etd.library.vanderbilt.edu/available/etd-12042008-144306/ ;

8. 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

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

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/ ;

9. 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

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

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/ ;

10. 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

Page 1 Page 2 Page 3 Page 4 Page 5 Page 6 Page 7

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

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/ ;

11. Gonzalez, Eric. The Kinetic and Chemical Mechanisms of Human Cytochrome P450 17A1.

Degree: PhD, Biochemistry, 2017, Vanderbilt University

 Human cytochrome P450 (P450) 17A1 is an essential enzyme in the steroid biosynthesis pathway that mediates a critical branch point which leads to either glucocorticoid… (more)

Subjects/Keywords: enzyme kinetics; prostate cancer; P450 17A1; cytochrome P450

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Gonzalez, E. (2017). The Kinetic and Chemical Mechanisms of Human Cytochrome P450 17A1. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-04102017-150657/ ;

Chicago Manual of Style (16th Edition):

Gonzalez, Eric. “The Kinetic and Chemical Mechanisms of Human Cytochrome P450 17A1.” 2017. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-04102017-150657/ ;.

MLA Handbook (7th Edition):

Gonzalez, Eric. “The Kinetic and Chemical Mechanisms of Human Cytochrome P450 17A1.” 2017. Web. 10 Jul 2020.

Vancouver:

Gonzalez E. The Kinetic and Chemical Mechanisms of Human Cytochrome P450 17A1. [Internet] [Doctoral dissertation]. Vanderbilt University; 2017. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-04102017-150657/ ;.

Council of Science Editors:

Gonzalez E. The Kinetic and Chemical Mechanisms of Human Cytochrome P450 17A1. [Doctoral Dissertation]. Vanderbilt University; 2017. Available from: http://etd.library.vanderbilt.edu/available/etd-04102017-150657/ ;

12. Sedgeman, Carl Andrew. Formation, Degradation, and Bypass of DNA-Protein Crosslinks.

Degree: PhD, Biochemistry, 2018, Vanderbilt University

 The preservation of DNA replication is requisite for cellular integrity and prevention of tumor formation and cell death. The Y-family DNA polymerases (Pol eta, kappa,… (more)

Subjects/Keywords: carcinogens; enzymology; DNA damage

Vanderbilt University, Nashville, TN). Oligonucleotides containing a 6chloropurine were… 

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Sedgeman, C. A. (2018). Formation, Degradation, and Bypass of DNA-Protein Crosslinks. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-09172018-134411/ ;

Chicago Manual of Style (16th Edition):

Sedgeman, Carl Andrew. “Formation, Degradation, and Bypass of DNA-Protein Crosslinks.” 2018. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-09172018-134411/ ;.

MLA Handbook (7th Edition):

Sedgeman, Carl Andrew. “Formation, Degradation, and Bypass of DNA-Protein Crosslinks.” 2018. Web. 10 Jul 2020.

Vancouver:

Sedgeman CA. Formation, Degradation, and Bypass of DNA-Protein Crosslinks. [Internet] [Doctoral dissertation]. Vanderbilt University; 2018. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-09172018-134411/ ;.

Council of Science Editors:

Sedgeman CA. Formation, Degradation, and Bypass of DNA-Protein Crosslinks. [Doctoral Dissertation]. Vanderbilt University; 2018. Available from: http://etd.library.vanderbilt.edu/available/etd-09172018-134411/ ;


Vanderbilt University

13. Schavolt, Kristy Lynn. Identification and regulation of p53 target genes in primary human epidermal keratinocytes.

Degree: PhD, Biochemistry, 2006, Vanderbilt University

 BIOCHEMISTRY IDENTIFICATION AND REGULATION OF P53 TARGET GENES IN PRIMARY HUMAN EPIDERMAL KERATINOCYTES KRISTY L. SCHAVOLT Dissertation under the direction of Professor Jennifer A. Pietenpol… (more)

Subjects/Keywords: repressor; crosslink; Affymetrix; real-time PCR; p21; 14-3-3sigma; p48; p53R2; Noxa; Fas/APO1; serine-15; phosphorylation; MDM2; DNA damage; adriamycin; ultraviolet radiation; adenovirus; PARP; PCR; transcription factor; Keratinocytes; p53 antioncogene; Cellular control mechanisms

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Schavolt, K. L. (2006). Identification and regulation of p53 target genes in primary human epidermal keratinocytes. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-12012006-002106/ ;

Chicago Manual of Style (16th Edition):

Schavolt, Kristy Lynn. “Identification and regulation of p53 target genes in primary human epidermal keratinocytes.” 2006. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-12012006-002106/ ;.

MLA Handbook (7th Edition):

Schavolt, Kristy Lynn. “Identification and regulation of p53 target genes in primary human epidermal keratinocytes.” 2006. Web. 10 Jul 2020.

Vancouver:

Schavolt KL. Identification and regulation of p53 target genes in primary human epidermal keratinocytes. [Internet] [Doctoral dissertation]. Vanderbilt University; 2006. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-12012006-002106/ ;.

Council of Science Editors:

Schavolt KL. Identification and regulation of p53 target genes in primary human epidermal keratinocytes. [Doctoral Dissertation]. Vanderbilt University; 2006. Available from: http://etd.library.vanderbilt.edu/available/etd-12012006-002106/ ;


Vanderbilt University

14. Brown, Kyle Lamar. Structural Studies of Fluxional Lesions in Deoxyribonucleic Acid.

Degree: PhD, Chemistry, 2008, Vanderbilt University

 This dissertation involves the structural and equilibrium studies of three DNA lesions: aflatoxin B1 formamidopyrimidine, methyl formamidopyrimidine, and thymine glycol. Studies of the methyl formamidopyrimidine… (more)

Subjects/Keywords: DNA damage; NMR; Formamidopyrimidine; Aflatoxin B1; Thymine Glycol; DNA  – Structure

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Brown, K. L. (2008). Structural Studies of Fluxional Lesions in Deoxyribonucleic Acid. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-06032008-181621/ ;

Chicago Manual of Style (16th Edition):

Brown, Kyle Lamar. “Structural Studies of Fluxional Lesions in Deoxyribonucleic Acid.” 2008. Doctoral Dissertation, Vanderbilt University. Accessed July 10, 2020. http://etd.library.vanderbilt.edu/available/etd-06032008-181621/ ;.

MLA Handbook (7th Edition):

Brown, Kyle Lamar. “Structural Studies of Fluxional Lesions in Deoxyribonucleic Acid.” 2008. Web. 10 Jul 2020.

Vancouver:

Brown KL. Structural Studies of Fluxional Lesions in Deoxyribonucleic Acid. [Internet] [Doctoral dissertation]. Vanderbilt University; 2008. [cited 2020 Jul 10]. Available from: http://etd.library.vanderbilt.edu/available/etd-06032008-181621/ ;.

Council of Science Editors:

Brown KL. Structural Studies of Fluxional Lesions in Deoxyribonucleic Acid. [Doctoral Dissertation]. Vanderbilt University; 2008. Available from: http://etd.library.vanderbilt.edu/available/etd-06032008-181621/ ;

.