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You searched for +publisher:"University of Michigan" +contributor:("Skiniotis, Georgios"). Showing records 1 – 13 of 13 total matches.

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University of Michigan

1. Livingston, Kathryn Elsa. Allosteric Modulation of the Mu Opioid Receptor.

Degree: PhD, Pharmacology, 2016, University of Michigan

 The mu opioid receptor (MOPr), a G protein-coupled receptor (GPCR), is the pharmacological site of action of morphine and related opioid narcotic agonists that bind… (more)

Subjects/Keywords: GPCR; Opioid Pharmacology; Allostery; Efficacy; Science

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APA (6th Edition):

Livingston, K. E. (2016). Allosteric Modulation of the Mu Opioid Receptor. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/120895

Chicago Manual of Style (16th Edition):

Livingston, Kathryn Elsa. “Allosteric Modulation of the Mu Opioid Receptor.” 2016. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/120895.

MLA Handbook (7th Edition):

Livingston, Kathryn Elsa. “Allosteric Modulation of the Mu Opioid Receptor.” 2016. Web. 16 Jun 2019.

Vancouver:

Livingston KE. Allosteric Modulation of the Mu Opioid Receptor. [Internet] [Doctoral dissertation]. University of Michigan; 2016. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/120895.

Council of Science Editors:

Livingston KE. Allosteric Modulation of the Mu Opioid Receptor. [Doctoral Dissertation]. University of Michigan; 2016. Available from: http://hdl.handle.net/2027.42/120895


University of Michigan

2. Mahoney, Jacob Patrick. Allosteric Control of Beta2-adrenergic Receptor Function.

Degree: PhD, Pharmacology, 2016, University of Michigan

 G protein-coupled receptors (GPCRs) are the largest class of transmembrane proteins and allow cells to sense their environment and respond accordingly. The transduction of an… (more)

Subjects/Keywords: GPCR; Nanobody; Allosteric modulator; Pharmacy and Pharmacology; Health Sciences

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APA (6th Edition):

Mahoney, J. P. (2016). Allosteric Control of Beta2-adrenergic Receptor Function. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/133520

Chicago Manual of Style (16th Edition):

Mahoney, Jacob Patrick. “Allosteric Control of Beta2-adrenergic Receptor Function.” 2016. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/133520.

MLA Handbook (7th Edition):

Mahoney, Jacob Patrick. “Allosteric Control of Beta2-adrenergic Receptor Function.” 2016. Web. 16 Jun 2019.

Vancouver:

Mahoney JP. Allosteric Control of Beta2-adrenergic Receptor Function. [Internet] [Doctoral dissertation]. University of Michigan; 2016. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/133520.

Council of Science Editors:

Mahoney JP. Allosteric Control of Beta2-adrenergic Receptor Function. [Doctoral Dissertation]. University of Michigan; 2016. Available from: http://hdl.handle.net/2027.42/133520


University of Michigan

3. Westfield, Gerwin Henri. Molecular Electron Mircroscopy of Signaling Protein Complexes.

Degree: PhD, Biological Chemistry, 2013, University of Michigan

 G protein-coupled receptors (GPCRs) are the primary signal transduction units responsible for the communication between cells and their environment. Thus, GPCRs are involved in every… (more)

Subjects/Keywords: Electron Microscopy; Signaling Protein Complexes; Biochemistry; Biological Chemistry; Science

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APA (6th Edition):

Westfield, G. H. (2013). Molecular Electron Mircroscopy of Signaling Protein Complexes. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/102417

Chicago Manual of Style (16th Edition):

Westfield, Gerwin Henri. “Molecular Electron Mircroscopy of Signaling Protein Complexes.” 2013. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/102417.

MLA Handbook (7th Edition):

Westfield, Gerwin Henri. “Molecular Electron Mircroscopy of Signaling Protein Complexes.” 2013. Web. 16 Jun 2019.

Vancouver:

Westfield GH. Molecular Electron Mircroscopy of Signaling Protein Complexes. [Internet] [Doctoral dissertation]. University of Michigan; 2013. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/102417.

Council of Science Editors:

Westfield GH. Molecular Electron Mircroscopy of Signaling Protein Complexes. [Doctoral Dissertation]. University of Michigan; 2013. Available from: http://hdl.handle.net/2027.42/102417


University of Michigan

4. Loucks, Cherisse Rae. Molecular Architecture of a 40S Ribosomal Subunit Maturation Intermediate.

Degree: PhD, Biological Chemistry, 2011, University of Michigan

 The biogenesis of eukaryotic ribosomes is a highly regulated process and requires approximately 200 assembly factors. The process begins with transcription of ribosomal RNA (rRNA)… (more)

Subjects/Keywords: Electron Microscopy; Ribosome Biogenesis; Structural Biology; Cryo-EM; Ribosome Assembly Factors; 40S; Biological Chemistry; Science

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APA (6th Edition):

Loucks, C. R. (2011). Molecular Architecture of a 40S Ribosomal Subunit Maturation Intermediate. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/86323

Chicago Manual of Style (16th Edition):

Loucks, Cherisse Rae. “Molecular Architecture of a 40S Ribosomal Subunit Maturation Intermediate.” 2011. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/86323.

MLA Handbook (7th Edition):

Loucks, Cherisse Rae. “Molecular Architecture of a 40S Ribosomal Subunit Maturation Intermediate.” 2011. Web. 16 Jun 2019.

Vancouver:

Loucks CR. Molecular Architecture of a 40S Ribosomal Subunit Maturation Intermediate. [Internet] [Doctoral dissertation]. University of Michigan; 2011. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/86323.

Council of Science Editors:

Loucks CR. Molecular Architecture of a 40S Ribosomal Subunit Maturation Intermediate. [Doctoral Dissertation]. University of Michigan; 2011. Available from: http://hdl.handle.net/2027.42/86323


University of Michigan

5. Sikkema, Andrew. Structural and Biochemical Studies of the Initiation Steps in Three Natural Product Biosynthetic Pathways.

Degree: PhD, Biological Chemistry, 2017, University of Michigan

 Natural products are a rich source of diverse chemical compounds, many with pharmaceutical potential. Structural and biochemical investigations into the initiation steps of three natural… (more)

Subjects/Keywords: Natural Products; Olefin Synthase; Apratoxin; Cahuitamycin; Initiation of Natural Product Biosynthesis; 1-nonadecene; Biological Chemistry; Science

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APA (6th Edition):

Sikkema, A. (2017). Structural and Biochemical Studies of the Initiation Steps in Three Natural Product Biosynthetic Pathways. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/137167

Chicago Manual of Style (16th Edition):

Sikkema, Andrew. “Structural and Biochemical Studies of the Initiation Steps in Three Natural Product Biosynthetic Pathways.” 2017. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/137167.

MLA Handbook (7th Edition):

Sikkema, Andrew. “Structural and Biochemical Studies of the Initiation Steps in Three Natural Product Biosynthetic Pathways.” 2017. Web. 16 Jun 2019.

Vancouver:

Sikkema A. Structural and Biochemical Studies of the Initiation Steps in Three Natural Product Biosynthetic Pathways. [Internet] [Doctoral dissertation]. University of Michigan; 2017. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/137167.

Council of Science Editors:

Sikkema A. Structural and Biochemical Studies of the Initiation Steps in Three Natural Product Biosynthetic Pathways. [Doctoral Dissertation]. University of Michigan; 2017. Available from: http://hdl.handle.net/2027.42/137167


University of Michigan

6. Sciore, Aaron. A General, Symmetry-Based Approach for the Assembly of Proteins into Nanoscale Polyhedra.

Degree: PhD, Chemistry, 2016, University of Michigan

 The assembly of individual protein subunits into large-scale symmetrical structures is widespread in Nature and confers unique biological properties which have potential applications in nano-technology… (more)

Subjects/Keywords: protein self-assembly; Chemistry; Science

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APA (6th Edition):

Sciore, A. (2016). A General, Symmetry-Based Approach for the Assembly of Proteins into Nanoscale Polyhedra. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/120840

Chicago Manual of Style (16th Edition):

Sciore, Aaron. “A General, Symmetry-Based Approach for the Assembly of Proteins into Nanoscale Polyhedra.” 2016. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/120840.

MLA Handbook (7th Edition):

Sciore, Aaron. “A General, Symmetry-Based Approach for the Assembly of Proteins into Nanoscale Polyhedra.” 2016. Web. 16 Jun 2019.

Vancouver:

Sciore A. A General, Symmetry-Based Approach for the Assembly of Proteins into Nanoscale Polyhedra. [Internet] [Doctoral dissertation]. University of Michigan; 2016. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/120840.

Council of Science Editors:

Sciore A. A General, Symmetry-Based Approach for the Assembly of Proteins into Nanoscale Polyhedra. [Doctoral Dissertation]. University of Michigan; 2016. Available from: http://hdl.handle.net/2027.42/120840

7. Bornschein, Russell E. Development of Charge Manipulation Nanoelectrospray Ion Mobility-Mass Spectrometry Techniques for Multiprotein Complex Analysis.

Degree: PhD, Chemistry, 2015, University of Michigan

 Macromoleclar protein complexes comprise a critical class of biomolecules unique in both their importance in biology and their relative impenetrability to detailed structural probes. Nanoelectrospray… (more)

Subjects/Keywords: Ion Mobility-Mass Spectrometry; Nanoelectrospray Ionization; Charge Manipulation; Multiprotein Complex Analysis; Collision Induced Dissociation; Chemistry; Science

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APA (6th Edition):

Bornschein, R. E. (2015). Development of Charge Manipulation Nanoelectrospray Ion Mobility-Mass Spectrometry Techniques for Multiprotein Complex Analysis. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/111426

Chicago Manual of Style (16th Edition):

Bornschein, Russell E. “Development of Charge Manipulation Nanoelectrospray Ion Mobility-Mass Spectrometry Techniques for Multiprotein Complex Analysis.” 2015. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/111426.

MLA Handbook (7th Edition):

Bornschein, Russell E. “Development of Charge Manipulation Nanoelectrospray Ion Mobility-Mass Spectrometry Techniques for Multiprotein Complex Analysis.” 2015. Web. 16 Jun 2019.

Vancouver:

Bornschein RE. Development of Charge Manipulation Nanoelectrospray Ion Mobility-Mass Spectrometry Techniques for Multiprotein Complex Analysis. [Internet] [Doctoral dissertation]. University of Michigan; 2015. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/111426.

Council of Science Editors:

Bornschein RE. Development of Charge Manipulation Nanoelectrospray Ion Mobility-Mass Spectrometry Techniques for Multiprotein Complex Analysis. [Doctoral Dissertation]. University of Michigan; 2015. Available from: http://hdl.handle.net/2027.42/111426

8. Bruhn, Brandon Robert. Nanopore-Based Methods for Characterizing Single Proteins.

Degree: PhD, Biomedical Engineering, 2015, University of Michigan

 Proteins represent the most diverse class of biomolecules in both structure and function and are involved in nearly every physiological process; their quantification, identification, and… (more)

Subjects/Keywords: Single protein biophysics; Single molecule sensing; Biotechnology; Biomedical Engineering; Engineering

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APA (6th Edition):

Bruhn, B. R. (2015). Nanopore-Based Methods for Characterizing Single Proteins. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/111522

Chicago Manual of Style (16th Edition):

Bruhn, Brandon Robert. “Nanopore-Based Methods for Characterizing Single Proteins.” 2015. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/111522.

MLA Handbook (7th Edition):

Bruhn, Brandon Robert. “Nanopore-Based Methods for Characterizing Single Proteins.” 2015. Web. 16 Jun 2019.

Vancouver:

Bruhn BR. Nanopore-Based Methods for Characterizing Single Proteins. [Internet] [Doctoral dissertation]. University of Michigan; 2015. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/111522.

Council of Science Editors:

Bruhn BR. Nanopore-Based Methods for Characterizing Single Proteins. [Doctoral Dissertation]. University of Michigan; 2015. Available from: http://hdl.handle.net/2027.42/111522

9. Mancour, Liliya Vasileva. Structural Dynamics of Transmembrane Signaling Complexes by Negative Stain Electron Microscopy.

Degree: PhD, Biological Chemistry, 2013, University of Michigan

 As an integral part of the cell’s communication system, membrane proteins play an essential role in relaying signals between cells and their environment. For example,… (more)

Subjects/Keywords: Using Electron Microscopy for Studying Structures of Membrane Proteins; Biological Chemistry; Science

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APA (6th Edition):

Mancour, L. V. (2013). Structural Dynamics of Transmembrane Signaling Complexes by Negative Stain Electron Microscopy. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/100056

Chicago Manual of Style (16th Edition):

Mancour, Liliya Vasileva. “Structural Dynamics of Transmembrane Signaling Complexes by Negative Stain Electron Microscopy.” 2013. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/100056.

MLA Handbook (7th Edition):

Mancour, Liliya Vasileva. “Structural Dynamics of Transmembrane Signaling Complexes by Negative Stain Electron Microscopy.” 2013. Web. 16 Jun 2019.

Vancouver:

Mancour LV. Structural Dynamics of Transmembrane Signaling Complexes by Negative Stain Electron Microscopy. [Internet] [Doctoral dissertation]. University of Michigan; 2013. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/100056.

Council of Science Editors:

Mancour LV. Structural Dynamics of Transmembrane Signaling Complexes by Negative Stain Electron Microscopy. [Doctoral Dissertation]. University of Michigan; 2013. Available from: http://hdl.handle.net/2027.42/100056

10. Krishnan, Swathi. Structural and Biochemical Insights into Methylation Site and State Specificity of JMJD2 Lysine Demethylases.

Degree: PhD, Biological Chemistry, 2012, University of Michigan

 The human JMJD2/KDM4 family of histone lysine demethylases comprises four homologs: JMJD2A, JMJD2B, JMJD2C and JMJD2D. These enzymes have been implicated in a number of… (more)

Subjects/Keywords: Substrate Specificity of JMJD2 Lysine Demethylases; Biological Chemistry; Chemistry; Health Sciences; Science

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APA (6th Edition):

Krishnan, S. (2012). Structural and Biochemical Insights into Methylation Site and State Specificity of JMJD2 Lysine Demethylases. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/96120

Chicago Manual of Style (16th Edition):

Krishnan, Swathi. “Structural and Biochemical Insights into Methylation Site and State Specificity of JMJD2 Lysine Demethylases.” 2012. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/96120.

MLA Handbook (7th Edition):

Krishnan, Swathi. “Structural and Biochemical Insights into Methylation Site and State Specificity of JMJD2 Lysine Demethylases.” 2012. Web. 16 Jun 2019.

Vancouver:

Krishnan S. Structural and Biochemical Insights into Methylation Site and State Specificity of JMJD2 Lysine Demethylases. [Internet] [Doctoral dissertation]. University of Michigan; 2012. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/96120.

Council of Science Editors:

Krishnan S. Structural and Biochemical Insights into Methylation Site and State Specificity of JMJD2 Lysine Demethylases. [Doctoral Dissertation]. University of Michigan; 2012. Available from: http://hdl.handle.net/2027.42/96120

11. Thompson, Andrea Dooley. The 70-kDa Heat Shock Protein (Hsp70) Chaperone System: Linking ATP Turnover and Complex Formation To Protein Homeostasis.

Degree: PhD, Chemical Biology, 2014, University of Michigan

 The 70-kDa heat shock protein (Hsp70) is a molecular chaperone that binds unfolded proteins and directs them towards a number of divergent pathways, including folding,… (more)

Subjects/Keywords: Chemical Biology; Microtubule Associated Protein Tau (MAPT); Molecular Chaperones; Hsp70; Protein Complexes; Biological Chemistry; Pathology; Science (General); Health Sciences; Science

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APA (6th Edition):

Thompson, A. D. (2014). The 70-kDa Heat Shock Protein (Hsp70) Chaperone System: Linking ATP Turnover and Complex Formation To Protein Homeostasis. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/107047

Chicago Manual of Style (16th Edition):

Thompson, Andrea Dooley. “The 70-kDa Heat Shock Protein (Hsp70) Chaperone System: Linking ATP Turnover and Complex Formation To Protein Homeostasis.” 2014. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/107047.

MLA Handbook (7th Edition):

Thompson, Andrea Dooley. “The 70-kDa Heat Shock Protein (Hsp70) Chaperone System: Linking ATP Turnover and Complex Formation To Protein Homeostasis.” 2014. Web. 16 Jun 2019.

Vancouver:

Thompson AD. The 70-kDa Heat Shock Protein (Hsp70) Chaperone System: Linking ATP Turnover and Complex Formation To Protein Homeostasis. [Internet] [Doctoral dissertation]. University of Michigan; 2014. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/107047.

Council of Science Editors:

Thompson AD. The 70-kDa Heat Shock Protein (Hsp70) Chaperone System: Linking ATP Turnover and Complex Formation To Protein Homeostasis. [Doctoral Dissertation]. University of Michigan; 2014. Available from: http://hdl.handle.net/2027.42/107047

12. Smith, Amber Marie. Structural Analysis of Mechanism and Regulation of Glutamine Amidotransferases.

Degree: PhD, Biological Chemistry, 2014, University of Michigan

 Glutamine amidotransferases (GATs) use glutamine as a nitrogen source for a diverse array of biosynthetic processes. GATs hydrolyze glutamine in a glutaminase domain and transfer… (more)

Subjects/Keywords: glutamine amidotransferases; X-ray crystallography; Biological Chemistry; Science

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APA (6th Edition):

Smith, A. M. (2014). Structural Analysis of Mechanism and Regulation of Glutamine Amidotransferases. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/110353

Chicago Manual of Style (16th Edition):

Smith, Amber Marie. “Structural Analysis of Mechanism and Regulation of Glutamine Amidotransferases.” 2014. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/110353.

MLA Handbook (7th Edition):

Smith, Amber Marie. “Structural Analysis of Mechanism and Regulation of Glutamine Amidotransferases.” 2014. Web. 16 Jun 2019.

Vancouver:

Smith AM. Structural Analysis of Mechanism and Regulation of Glutamine Amidotransferases. [Internet] [Doctoral dissertation]. University of Michigan; 2014. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/110353.

Council of Science Editors:

Smith AM. Structural Analysis of Mechanism and Regulation of Glutamine Amidotransferases. [Doctoral Dissertation]. University of Michigan; 2014. Available from: http://hdl.handle.net/2027.42/110353

13. Raymond, Donald Damian. Structural Studies of RNA Packaging by Phlebovirus Nucleocapsid Proteins and RNA Capping by Flavivirus Methyltransferases.

Degree: PhD, Biological Chemistry, 2012, University of Michigan

 Arboviruses are maintained in nature through a complex life cycle involving blood-sucking insects and susceptible vertebrate hosts. Arboviruses have evolved mechanisms to conceal their RNA… (more)

Subjects/Keywords: RNA-binding Proteins; Rift Valley Fever Virus; Structural Virology; Biological Chemistry; Health Sciences

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APA (6th Edition):

Raymond, D. D. (2012). Structural Studies of RNA Packaging by Phlebovirus Nucleocapsid Proteins and RNA Capping by Flavivirus Methyltransferases. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/95947

Chicago Manual of Style (16th Edition):

Raymond, Donald Damian. “Structural Studies of RNA Packaging by Phlebovirus Nucleocapsid Proteins and RNA Capping by Flavivirus Methyltransferases.” 2012. Doctoral Dissertation, University of Michigan. Accessed June 16, 2019. http://hdl.handle.net/2027.42/95947.

MLA Handbook (7th Edition):

Raymond, Donald Damian. “Structural Studies of RNA Packaging by Phlebovirus Nucleocapsid Proteins and RNA Capping by Flavivirus Methyltransferases.” 2012. Web. 16 Jun 2019.

Vancouver:

Raymond DD. Structural Studies of RNA Packaging by Phlebovirus Nucleocapsid Proteins and RNA Capping by Flavivirus Methyltransferases. [Internet] [Doctoral dissertation]. University of Michigan; 2012. [cited 2019 Jun 16]. Available from: http://hdl.handle.net/2027.42/95947.

Council of Science Editors:

Raymond DD. Structural Studies of RNA Packaging by Phlebovirus Nucleocapsid Proteins and RNA Capping by Flavivirus Methyltransferases. [Doctoral Dissertation]. University of Michigan; 2012. Available from: http://hdl.handle.net/2027.42/95947

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