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:("Walter J. Chazin"). Showing records 1 – 19 of 19 total matches.

Search Limiters

Last 2 Years | English Only

No search limiters apply to these results.

▼ Search Limiters


Vanderbilt University

1. Starling, Michael Paul. Evaluation of Autodock Vina for use in fragment-based drug discovery.

Degree: MS, Chemistry, 2013, Vanderbilt University

 The most common approaches to treatment of cancer are chemo- and radiation-therapies that cause DNA damage. The efficiency of these treatments is reduced over time… (more)

Subjects/Keywords: fragment-based; FBDD; drug discovery; cancer; RPA

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Starling, M. P. (2013). Evaluation of Autodock Vina for use in fragment-based drug discovery. (Masters Thesis). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-02252013-131225/ ;

Chicago Manual of Style (16th Edition):

Starling, Michael Paul. “Evaluation of Autodock Vina for use in fragment-based drug discovery.” 2013. Masters Thesis, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-02252013-131225/ ;.

MLA Handbook (7th Edition):

Starling, Michael Paul. “Evaluation of Autodock Vina for use in fragment-based drug discovery.” 2013. Web. 09 Aug 2020.

Vancouver:

Starling MP. Evaluation of Autodock Vina for use in fragment-based drug discovery. [Internet] [Masters thesis]. Vanderbilt University; 2013. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-02252013-131225/ ;.

Council of Science Editors:

Starling MP. Evaluation of Autodock Vina for use in fragment-based drug discovery. [Masters Thesis]. Vanderbilt University; 2013. Available from: http://etd.library.vanderbilt.edu/available/etd-02252013-131225/ ;


Vanderbilt University

2. Alers Rivera, Ileana. NMR analysis of the RPA dimer core RPA32D/14.

Degree: MS, Chemical and Physical Biology, 2011, Vanderbilt University

 CHEMICAL AND PHYSICAL BIOLOGY NMR STUDIES OF THE RPA DIMER CORE RPA32D/14 ILEANA ALERS RIVERA Thesis under the direction of Professor Walter J. Chazin Replication… (more)

Subjects/Keywords: telomeres; Replication Protein A; G-quadruplex

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Alers Rivera, I. (2011). NMR analysis of the RPA dimer core RPA32D/14. (Masters Thesis). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-07162011-113100/ ;

Chicago Manual of Style (16th Edition):

Alers Rivera, Ileana. “NMR analysis of the RPA dimer core RPA32D/14.” 2011. Masters Thesis, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-07162011-113100/ ;.

MLA Handbook (7th Edition):

Alers Rivera, Ileana. “NMR analysis of the RPA dimer core RPA32D/14.” 2011. Web. 09 Aug 2020.

Vancouver:

Alers Rivera I. NMR analysis of the RPA dimer core RPA32D/14. [Internet] [Masters thesis]. Vanderbilt University; 2011. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-07162011-113100/ ;.

Council of Science Editors:

Alers Rivera I. NMR analysis of the RPA dimer core RPA32D/14. [Masters Thesis]. Vanderbilt University; 2011. Available from: http://etd.library.vanderbilt.edu/available/etd-07162011-113100/ ;


Vanderbilt University

3. LaFrance, Michelle Ellen. Identification of Host Factors, Including an Epithelial Cell Receptor, Responsible for Clostridium difficile TcdB-Mediated Cytotoxicity.

Degree: PhD, Biochemistry, 2016, Vanderbilt University

 Clostridium difficile is the leading cause of hospital-acquired diarrhea in the United States. The two main virulence factors of C. difficile are the large toxins,… (more)

Subjects/Keywords: Clostridium difficile; PVRL3; nectin; receptor; toxin; TcdB

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

LaFrance, M. E. (2016). Identification of Host Factors, Including an Epithelial Cell Receptor, Responsible for Clostridium difficile TcdB-Mediated Cytotoxicity. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-03282016-124039/ ;

Chicago Manual of Style (16th Edition):

LaFrance, Michelle Ellen. “Identification of Host Factors, Including an Epithelial Cell Receptor, Responsible for Clostridium difficile TcdB-Mediated Cytotoxicity.” 2016. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-03282016-124039/ ;.

MLA Handbook (7th Edition):

LaFrance, Michelle Ellen. “Identification of Host Factors, Including an Epithelial Cell Receptor, Responsible for Clostridium difficile TcdB-Mediated Cytotoxicity.” 2016. Web. 09 Aug 2020.

Vancouver:

LaFrance ME. Identification of Host Factors, Including an Epithelial Cell Receptor, Responsible for Clostridium difficile TcdB-Mediated Cytotoxicity. [Internet] [Doctoral dissertation]. Vanderbilt University; 2016. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-03282016-124039/ ;.

Council of Science Editors:

LaFrance ME. Identification of Host Factors, Including an Epithelial Cell Receptor, Responsible for Clostridium difficile TcdB-Mediated Cytotoxicity. [Doctoral Dissertation]. Vanderbilt University; 2016. Available from: http://etd.library.vanderbilt.edu/available/etd-03282016-124039/ ;


Vanderbilt University

4. Nguyen, Elizabeth Dong. Structural Studies of the Interaction between mGlu5 and Allosteric Modulators.

Degree: PhD, Chemical and Physical Biology, 2013, Vanderbilt University

 The metabotropic glutamate receptor subtype 5 (mGlu5), a class C G-protein coupled receptor (GPCR), is involved in cognitive function through diverse signaling pathways that modulate… (more)

Subjects/Keywords: ligand docking; GPCR; schizophrenia; computational structural biology; protein structure prediction

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Nguyen, E. D. (2013). Structural Studies of the Interaction between mGlu5 and Allosteric Modulators. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-07172013-164828/ ;

Chicago Manual of Style (16th Edition):

Nguyen, Elizabeth Dong. “Structural Studies of the Interaction between mGlu5 and Allosteric Modulators.” 2013. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-07172013-164828/ ;.

MLA Handbook (7th Edition):

Nguyen, Elizabeth Dong. “Structural Studies of the Interaction between mGlu5 and Allosteric Modulators.” 2013. Web. 09 Aug 2020.

Vancouver:

Nguyen ED. Structural Studies of the Interaction between mGlu5 and Allosteric Modulators. [Internet] [Doctoral dissertation]. Vanderbilt University; 2013. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-07172013-164828/ ;.

Council of Science Editors:

Nguyen ED. Structural Studies of the Interaction between mGlu5 and Allosteric Modulators. [Doctoral Dissertation]. Vanderbilt University; 2013. Available from: http://etd.library.vanderbilt.edu/available/etd-07172013-164828/ ;


Vanderbilt University

5. Guler, Gulfem Dilek. Human DNA helicase B in replication fork surveillance and replication stress recovery.

Degree: PhD, Biological Sciences, 2012, Vanderbilt University

 Correct and faithful genome duplication is crucial for preserving genomic integrity. Genome duplication is, therefore, highly regulated through a complex network of proteins that accomplish… (more)

Subjects/Keywords: Replication protein A; RPA; DNA helicase; DNA replication; DNA repair; replication stress; HelB; HDHB

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Guler, G. D. (2012). Human DNA helicase B in replication fork surveillance and replication stress recovery. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu//available/etd-12292011-192757/ ;

Chicago Manual of Style (16th Edition):

Guler, Gulfem Dilek. “Human DNA helicase B in replication fork surveillance and replication stress recovery.” 2012. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu//available/etd-12292011-192757/ ;.

MLA Handbook (7th Edition):

Guler, Gulfem Dilek. “Human DNA helicase B in replication fork surveillance and replication stress recovery.” 2012. Web. 09 Aug 2020.

Vancouver:

Guler GD. Human DNA helicase B in replication fork surveillance and replication stress recovery. [Internet] [Doctoral dissertation]. Vanderbilt University; 2012. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu//available/etd-12292011-192757/ ;.

Council of Science Editors:

Guler GD. Human DNA helicase B in replication fork surveillance and replication stress recovery. [Doctoral Dissertation]. Vanderbilt University; 2012. Available from: http://etd.library.vanderbilt.edu//available/etd-12292011-192757/ ;


Vanderbilt University

6. Law, Cheryl Lynn. NMR Resonance Assignments and Secondary Structure of a Mutant Form of the Human KCNE1 Channel Accessory Protein that Exhibits KCNE3-like Function.

Degree: PhD, Biochemistry, 2019, Vanderbilt University

 KCNQ1 (Q1), a voltage-gated potassium channel, is modulated by members of the KCNE family, the best-characterized being KCNE1 (E1) and KCNE3 (E3). The Q1/E1 complex… (more)

Subjects/Keywords: KCNE1; NMR; structural biology; membrane proteins; potassium channels; KCNQ1; KCNE3

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Law, C. L. (2019). NMR Resonance Assignments and Secondary Structure of a Mutant Form of the Human KCNE1 Channel Accessory Protein that Exhibits KCNE3-like Function. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-03252019-234212/ ;

Chicago Manual of Style (16th Edition):

Law, Cheryl Lynn. “NMR Resonance Assignments and Secondary Structure of a Mutant Form of the Human KCNE1 Channel Accessory Protein that Exhibits KCNE3-like Function.” 2019. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-03252019-234212/ ;.

MLA Handbook (7th Edition):

Law, Cheryl Lynn. “NMR Resonance Assignments and Secondary Structure of a Mutant Form of the Human KCNE1 Channel Accessory Protein that Exhibits KCNE3-like Function.” 2019. Web. 09 Aug 2020.

Vancouver:

Law CL. NMR Resonance Assignments and Secondary Structure of a Mutant Form of the Human KCNE1 Channel Accessory Protein that Exhibits KCNE3-like Function. [Internet] [Doctoral dissertation]. Vanderbilt University; 2019. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-03252019-234212/ ;.

Council of Science Editors:

Law CL. NMR Resonance Assignments and Secondary Structure of a Mutant Form of the Human KCNE1 Channel Accessory Protein that Exhibits KCNE3-like Function. [Doctoral Dissertation]. Vanderbilt University; 2019. Available from: http://etd.library.vanderbilt.edu/available/etd-03252019-234212/ ;


Vanderbilt University

7. Sugitani, Norie. Structural and Biophysical Characterization of the Nucleotide Excision Repair Factor XPA.

Degree: PhD, Chemistry, 2017, Vanderbilt University

 Maintaining the integrity of the genome is critical for the survival of all organisms. Genome maintenance must be efficient because we are constantly under exposure… (more)

Subjects/Keywords: NER; XPA; DNA repair; RPA

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Sugitani, N. (2017). Structural and Biophysical Characterization of the Nucleotide Excision Repair Factor XPA. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu//available/etd-03212017-135434/ ;

Chicago Manual of Style (16th Edition):

Sugitani, Norie. “Structural and Biophysical Characterization of the Nucleotide Excision Repair Factor XPA.” 2017. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu//available/etd-03212017-135434/ ;.

MLA Handbook (7th Edition):

Sugitani, Norie. “Structural and Biophysical Characterization of the Nucleotide Excision Repair Factor XPA.” 2017. Web. 09 Aug 2020.

Vancouver:

Sugitani N. Structural and Biophysical Characterization of the Nucleotide Excision Repair Factor XPA. [Internet] [Doctoral dissertation]. Vanderbilt University; 2017. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu//available/etd-03212017-135434/ ;.

Council of Science Editors:

Sugitani N. Structural and Biophysical Characterization of the Nucleotide Excision Repair Factor XPA. [Doctoral Dissertation]. Vanderbilt University; 2017. Available from: http://etd.library.vanderbilt.edu//available/etd-03212017-135434/ ;


Vanderbilt University

8. 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

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

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 August 09, 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. 09 Aug 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 Aug 09]. 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/ ;

9. Mitchener, Michelle Marie. A. Competition and allostery govern substrate selectivity of cyclooxygenase-2 B. Enzymatic oxidation of M1dG in the genome.

Degree: PhD, Chemistry, 2017, Vanderbilt University

 Part A: Cyclooxygenase-2 (COX-2) oxygenates arachidonic acid (AA) and its ester analog, 2-arachidonoylglycerol (2-AG), to prostaglandins (PGs) and prostaglandin glyceryl esters (PG-Gs), respectively. Although the… (more)

Subjects/Keywords: M1dG; chemical kinetics; endocannabinoids; cyclooxygenase-2; DNA adducts

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Mitchener, M. M. (2017). A. Competition and allostery govern substrate selectivity of cyclooxygenase-2 B. Enzymatic oxidation of M1dG in the genome. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-12042017-111654/ ;

Chicago Manual of Style (16th Edition):

Mitchener, Michelle Marie. “A. Competition and allostery govern substrate selectivity of cyclooxygenase-2 B. Enzymatic oxidation of M1dG in the genome.” 2017. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-12042017-111654/ ;.

MLA Handbook (7th Edition):

Mitchener, Michelle Marie. “A. Competition and allostery govern substrate selectivity of cyclooxygenase-2 B. Enzymatic oxidation of M1dG in the genome.” 2017. Web. 09 Aug 2020.

Vancouver:

Mitchener MM. A. Competition and allostery govern substrate selectivity of cyclooxygenase-2 B. Enzymatic oxidation of M1dG in the genome. [Internet] [Doctoral dissertation]. Vanderbilt University; 2017. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-12042017-111654/ ;.

Council of Science Editors:

Mitchener MM. A. Competition and allostery govern substrate selectivity of cyclooxygenase-2 B. Enzymatic oxidation of M1dG in the genome. [Doctoral Dissertation]. Vanderbilt University; 2017. Available from: http://etd.library.vanderbilt.edu/available/etd-12042017-111654/ ;

10. Pretto Garcia, Dalyir Imelda. Domain-based structural studies of Replication Protein A: analysis of an RPA32N phospho-mimic mutant and the role of RPA70N in binding ssDNA.

Degree: PhD, Biochemistry, 2010, Vanderbilt University

 Replication Protein A (RPA) is the primary eukaryotic ssDNA binding protein utilized in preventing secondary structure formation and re-annealing of unwound DNA strands, thereby controlling… (more)

Subjects/Keywords: RPA; RPA phosphorylation; SAXS; RPA ssDNA binding

…x28;Sivaraja Vaithiyalingham, Erick Warren, Brandt Eichman and Walter J. Chazin, unpublished… 

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Pretto Garcia, D. I. (2010). Domain-based structural studies of Replication Protein A: analysis of an RPA32N phospho-mimic mutant and the role of RPA70N in binding ssDNA. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-07122010-152656/ ;

Chicago Manual of Style (16th Edition):

Pretto Garcia, Dalyir Imelda. “Domain-based structural studies of Replication Protein A: analysis of an RPA32N phospho-mimic mutant and the role of RPA70N in binding ssDNA.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-07122010-152656/ ;.

MLA Handbook (7th Edition):

Pretto Garcia, Dalyir Imelda. “Domain-based structural studies of Replication Protein A: analysis of an RPA32N phospho-mimic mutant and the role of RPA70N in binding ssDNA.” 2010. Web. 09 Aug 2020.

Vancouver:

Pretto Garcia DI. Domain-based structural studies of Replication Protein A: analysis of an RPA32N phospho-mimic mutant and the role of RPA70N in binding ssDNA. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-07122010-152656/ ;.

Council of Science Editors:

Pretto Garcia DI. Domain-based structural studies of Replication Protein A: analysis of an RPA32N phospho-mimic mutant and the role of RPA70N in binding ssDNA. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-07122010-152656/ ;

11. Huang, Hao. Docking of the p68 subunit of DNA polymerase ¦á-primase on the SV40 helicase is required for the viral primosome activity.

Degree: PhD, Biological Sciences, 2010, Vanderbilt University

 DNA polymerase ¦Ã-primase (pol-prim) plays a central role in eukaryotic DNA replication, initiating synthesis on both the leading and lagging strand DNA templates. Pol-prim consists… (more)

Subjects/Keywords: DNA polymerase alpha-primase; DNA helicase; p68; SV40 primosome

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Huang, H. (2010). Docking of the p68 subunit of DNA polymerase ¦á-primase on the SV40 helicase is required for the viral primosome activity. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-11042010-114906/ ;

Chicago Manual of Style (16th Edition):

Huang, Hao. “Docking of the p68 subunit of DNA polymerase ¦á-primase on the SV40 helicase is required for the viral primosome activity.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-11042010-114906/ ;.

MLA Handbook (7th Edition):

Huang, Hao. “Docking of the p68 subunit of DNA polymerase ¦á-primase on the SV40 helicase is required for the viral primosome activity.” 2010. Web. 09 Aug 2020.

Vancouver:

Huang H. Docking of the p68 subunit of DNA polymerase ¦á-primase on the SV40 helicase is required for the viral primosome activity. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-11042010-114906/ ;.

Council of Science Editors:

Huang H. Docking of the p68 subunit of DNA polymerase ¦á-primase on the SV40 helicase is required for the viral primosome activity. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-11042010-114906/ ;

12. Robertson, Patrick David. Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10.

Degree: PhD, Biological Sciences, 2010, Vanderbilt University

 Eukaryotic DNA replication is tightly regulated during the initiation phase to ensure that the genome is copied only once and at the proper time during… (more)

Subjects/Keywords: DNA Replication; DNA Binding; Zinc Motif; Mcm10; NMR; C-Terminal Domain

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Robertson, P. D. (2010). Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-06032010-145223/ ;

Chicago Manual of Style (16th Edition):

Robertson, Patrick David. “Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-06032010-145223/ ;.

MLA Handbook (7th Edition):

Robertson, Patrick David. “Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10.” 2010. Web. 09 Aug 2020.

Vancouver:

Robertson PD. Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-06032010-145223/ ;.

Council of Science Editors:

Robertson PD. Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-06032010-145223/ ;

13. Brosey, Chris Arlen. Investigating the architectural basis of RPA quaternary remodeling upon binding ssDNA.

Degree: PhD, Biochemistry, 2011, Vanderbilt University

 The integrity and propagation of the genome depends upon the fidelity of DNA processing events such as replication, damage recognition, and repair. Requisite to the… (more)

Subjects/Keywords: NMR spectroscopy; NMR 15N relaxation; small-angle x-ray scattering; Replication Protein A; small-angle neutron scattering; protein modularity; ssDNA binding protein; DNA processing

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):

Brosey, C. A. (2011). Investigating the architectural basis of RPA quaternary remodeling upon binding ssDNA. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-10282011-155051/ ;

Chicago Manual of Style (16th Edition):

Brosey, Chris Arlen. “Investigating the architectural basis of RPA quaternary remodeling upon binding ssDNA.” 2011. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-10282011-155051/ ;.

MLA Handbook (7th Edition):

Brosey, Chris Arlen. “Investigating the architectural basis of RPA quaternary remodeling upon binding ssDNA.” 2011. Web. 09 Aug 2020.

Vancouver:

Brosey CA. Investigating the architectural basis of RPA quaternary remodeling upon binding ssDNA. [Internet] [Doctoral dissertation]. Vanderbilt University; 2011. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-10282011-155051/ ;.

Council of Science Editors:

Brosey CA. Investigating the architectural basis of RPA quaternary remodeling upon binding ssDNA. [Doctoral Dissertation]. Vanderbilt University; 2011. Available from: http://etd.library.vanderbilt.edu/available/etd-10282011-155051/ ;

14. 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 August 09, 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. 09 Aug 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 Aug 09]. 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/ ;


Vanderbilt University

15. Velez-Cruz, Renier. DNA Lesions as Cellular Poisons of Topoisomerase II-alpha.

Degree: PhD, Biochemistry, 2005, Vanderbilt University

 Topoisomerase II is an essential enzyme that controls DNA topology. This enzyme generates a protein-linked DNA break as a catalytic intermediate. This intermediate, known as… (more)

Subjects/Keywords: DNA adducts; topoisomerases; DNA; DNA damage; DNA repair

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Velez-Cruz, R. (2005). DNA Lesions as Cellular Poisons of Topoisomerase II-alpha. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-10112005-183529/ ;

Chicago Manual of Style (16th Edition):

Velez-Cruz, Renier. “DNA Lesions as Cellular Poisons of Topoisomerase II-alpha.” 2005. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-10112005-183529/ ;.

MLA Handbook (7th Edition):

Velez-Cruz, Renier. “DNA Lesions as Cellular Poisons of Topoisomerase II-alpha.” 2005. Web. 09 Aug 2020.

Vancouver:

Velez-Cruz R. DNA Lesions as Cellular Poisons of Topoisomerase II-alpha. [Internet] [Doctoral dissertation]. Vanderbilt University; 2005. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-10112005-183529/ ;.

Council of Science Editors:

Velez-Cruz R. DNA Lesions as Cellular Poisons of Topoisomerase II-alpha. [Doctoral Dissertation]. Vanderbilt University; 2005. Available from: http://etd.library.vanderbilt.edu/available/etd-10112005-183529/ ;


Vanderbilt University

16. Dattilo, Brian Matthew. Structural characterization of the receptor for advanced glycation end products reveals a two domain modular architecture.

Degree: PhD, Biochemistry, 2007, Vanderbilt University

 The Receptor for Advanced Glycation End Products (RAGE) contains a single transmembrane helix, a small cytosolic domain, and an extracellular region (sRAGE) composed of three… (more)

Subjects/Keywords: Structural Biology; RAGE; Receptor for Advanced Glycation End Products; Soluble RAGE; Receptor Signaling; S100 Proteins; Ligands (Biochemistry)

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Dattilo, B. M. (2007). Structural characterization of the receptor for advanced glycation end products reveals a two domain modular architecture. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-05302007-114804/ ;

Chicago Manual of Style (16th Edition):

Dattilo, Brian Matthew. “Structural characterization of the receptor for advanced glycation end products reveals a two domain modular architecture.” 2007. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-05302007-114804/ ;.

MLA Handbook (7th Edition):

Dattilo, Brian Matthew. “Structural characterization of the receptor for advanced glycation end products reveals a two domain modular architecture.” 2007. Web. 09 Aug 2020.

Vancouver:

Dattilo BM. Structural characterization of the receptor for advanced glycation end products reveals a two domain modular architecture. [Internet] [Doctoral dissertation]. Vanderbilt University; 2007. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-05302007-114804/ ;.

Council of Science Editors:

Dattilo BM. Structural characterization of the receptor for advanced glycation end products reveals a two domain modular architecture. [Doctoral Dissertation]. Vanderbilt University; 2007. Available from: http://etd.library.vanderbilt.edu/available/etd-05302007-114804/ ;


Vanderbilt University

17. Kussrow, Amanda Kathryn. Interrogation of Biomolecular Interactions Utilizing Backscattering Interferometry.

Degree: PhD, Chemistry, 2009, Vanderbilt University

 Backscattering interferometry (BSI) is a relatively new technique used to study molecular interactions in a label-free format and is proving to be a versatile biosensing… (more)

Subjects/Keywords: backscattering interferometry; biosensor; molecular interaction; binding affinity

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Kussrow, A. K. (2009). Interrogation of Biomolecular Interactions Utilizing Backscattering Interferometry. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu//available/etd-12042009-092927/ ;

Chicago Manual of Style (16th Edition):

Kussrow, Amanda Kathryn. “Interrogation of Biomolecular Interactions Utilizing Backscattering Interferometry.” 2009. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu//available/etd-12042009-092927/ ;.

MLA Handbook (7th Edition):

Kussrow, Amanda Kathryn. “Interrogation of Biomolecular Interactions Utilizing Backscattering Interferometry.” 2009. Web. 09 Aug 2020.

Vancouver:

Kussrow AK. Interrogation of Biomolecular Interactions Utilizing Backscattering Interferometry. [Internet] [Doctoral dissertation]. Vanderbilt University; 2009. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu//available/etd-12042009-092927/ ;.

Council of Science Editors:

Kussrow AK. Interrogation of Biomolecular Interactions Utilizing Backscattering Interferometry. [Doctoral Dissertation]. Vanderbilt University; 2009. Available from: http://etd.library.vanderbilt.edu//available/etd-12042009-092927/ ;


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

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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 August 09, 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. 09 Aug 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 Aug 09]. 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/ ;


Vanderbilt University

19. Dimitrova, Yoana Nantcheva. Biochemical and structural analyses of TBL1: insights into the function of a transcriptional regulator.

Degree: PhD, Biochemistry, 2010, Vanderbilt University

 The mechanism controlling the switch between gene activation and repression is critically important for understanding the process of transcriptional regulation. Gene expression is highly controlled… (more)

Subjects/Keywords: transcriptional regulation; ubiquitination; beta-catenin; TBL1

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Dimitrova, Y. N. (2010). Biochemical and structural analyses of TBL1: insights into the function of a transcriptional regulator. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://etd.library.vanderbilt.edu/available/etd-10282010-173834/ ;

Chicago Manual of Style (16th Edition):

Dimitrova, Yoana Nantcheva. “Biochemical and structural analyses of TBL1: insights into the function of a transcriptional regulator.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed August 09, 2020. http://etd.library.vanderbilt.edu/available/etd-10282010-173834/ ;.

MLA Handbook (7th Edition):

Dimitrova, Yoana Nantcheva. “Biochemical and structural analyses of TBL1: insights into the function of a transcriptional regulator.” 2010. Web. 09 Aug 2020.

Vancouver:

Dimitrova YN. Biochemical and structural analyses of TBL1: insights into the function of a transcriptional regulator. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2020 Aug 09]. Available from: http://etd.library.vanderbilt.edu/available/etd-10282010-173834/ ;.

Council of Science Editors:

Dimitrova YN. Biochemical and structural analyses of TBL1: insights into the function of a transcriptional regulator. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://etd.library.vanderbilt.edu/available/etd-10282010-173834/ ;

.