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You searched for +publisher:"Vanderbilt University" +contributor:("Brian E. Wadzinski"). Showing records 1 – 7 of 7 total matches.

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Vanderbilt University

1. Lu, Lucy Xiangxi. Phosphoregulation of the Cdc25 phosphatase and its effects on Schizosaccharomyces pombe mitotic entrance and exit.

Degree: PhD, Cell and Developmental Biology, 2012, Vanderbilt University

 Cdk1 kinase dephosphorylation and activation by Cdc25 phosphatase is essential for mitotic entry. Activated Cdk1 phosphorylates Cdc25 and other substrates, further activating Cdc25 to form… (more)

Subjects/Keywords: Cdk1; phosphatases; kinases; mitosis; bistability; ultrasensitivity; schizosaccharomyces pombe; Cdc14; Clp1; Cdc25; Cdc2

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

APA (6th Edition):

Lu, L. X. (2012). Phosphoregulation of the Cdc25 phosphatase and its effects on Schizosaccharomyces pombe mitotic entrance and exit. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/13924

Chicago Manual of Style (16th Edition):

Lu, Lucy Xiangxi. “Phosphoregulation of the Cdc25 phosphatase and its effects on Schizosaccharomyces pombe mitotic entrance and exit.” 2012. Doctoral Dissertation, Vanderbilt University. Accessed January 19, 2021. http://hdl.handle.net/1803/13924.

MLA Handbook (7th Edition):

Lu, Lucy Xiangxi. “Phosphoregulation of the Cdc25 phosphatase and its effects on Schizosaccharomyces pombe mitotic entrance and exit.” 2012. Web. 19 Jan 2021.

Vancouver:

Lu LX. Phosphoregulation of the Cdc25 phosphatase and its effects on Schizosaccharomyces pombe mitotic entrance and exit. [Internet] [Doctoral dissertation]. Vanderbilt University; 2012. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1803/13924.

Council of Science Editors:

Lu LX. Phosphoregulation of the Cdc25 phosphatase and its effects on Schizosaccharomyces pombe mitotic entrance and exit. [Doctoral Dissertation]. Vanderbilt University; 2012. Available from: http://hdl.handle.net/1803/13924


Vanderbilt University

2. Coffa, Sergio. Non-visual arrestins bind mitogen activated protein kinases and regulate their signaling.

Degree: PhD, Pharmacology, 2011, Vanderbilt University

 Arrestins are multifunctional signaling proteins, important for the regulation of signal transduction and the trafficking of G protein-coupled receptors (GPCRs). Recently, GPCR-arrestin interactions have been… (more)

Subjects/Keywords: arrestin

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APA (6th Edition):

Coffa, S. (2011). Non-visual arrestins bind mitogen activated protein kinases and regulate their signaling. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/13814

Chicago Manual of Style (16th Edition):

Coffa, Sergio. “Non-visual arrestins bind mitogen activated protein kinases and regulate their signaling.” 2011. Doctoral Dissertation, Vanderbilt University. Accessed January 19, 2021. http://hdl.handle.net/1803/13814.

MLA Handbook (7th Edition):

Coffa, Sergio. “Non-visual arrestins bind mitogen activated protein kinases and regulate their signaling.” 2011. Web. 19 Jan 2021.

Vancouver:

Coffa S. Non-visual arrestins bind mitogen activated protein kinases and regulate their signaling. [Internet] [Doctoral dissertation]. Vanderbilt University; 2011. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1803/13814.

Council of Science Editors:

Coffa S. Non-visual arrestins bind mitogen activated protein kinases and regulate their signaling. [Doctoral Dissertation]. Vanderbilt University; 2011. Available from: http://hdl.handle.net/1803/13814


Vanderbilt University

3. Bruntz, Ronald Chase. Insights into the Molecular Mechanisms of Phospholipase D-Mediated Cancer Cell Survival.

Degree: PhD, Pharmacology, 2014, Vanderbilt University

 The production of bioactive lipids by phospholipases has long been appreciated as an important mode of cellular communication. Phospholipase D (PLD) enzymes hydrolyze phosphatidylcholine to… (more)

Subjects/Keywords: phospholipase D; phosphatidic acid; cancer; Akt; cell signaling; autophagy

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APA (6th Edition):

Bruntz, R. C. (2014). Insights into the Molecular Mechanisms of Phospholipase D-Mediated Cancer Cell Survival. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/10427

Chicago Manual of Style (16th Edition):

Bruntz, Ronald Chase. “Insights into the Molecular Mechanisms of Phospholipase D-Mediated Cancer Cell Survival.” 2014. Doctoral Dissertation, Vanderbilt University. Accessed January 19, 2021. http://hdl.handle.net/1803/10427.

MLA Handbook (7th Edition):

Bruntz, Ronald Chase. “Insights into the Molecular Mechanisms of Phospholipase D-Mediated Cancer Cell Survival.” 2014. Web. 19 Jan 2021.

Vancouver:

Bruntz RC. Insights into the Molecular Mechanisms of Phospholipase D-Mediated Cancer Cell Survival. [Internet] [Doctoral dissertation]. Vanderbilt University; 2014. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1803/10427.

Council of Science Editors:

Bruntz RC. Insights into the Molecular Mechanisms of Phospholipase D-Mediated Cancer Cell Survival. [Doctoral Dissertation]. Vanderbilt University; 2014. Available from: http://hdl.handle.net/1803/10427


Vanderbilt University

4. Cleghorn, Whitney Marie. Arrestins regulate cell spreading and motility via focal adhesion dynamics.

Degree: PhD, Pharmacology, 2012, Vanderbilt University

 Arrestins bind G protein-coupled receptors and more than 100 non-receptor partners, regulating various signaling pathways and cellular functions. The interactions of many proteins (e.g., Src,… (more)

Subjects/Keywords: structural biology; pharmacology; morphology; cell biology; GPCR; arrestin

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APA (6th Edition):

Cleghorn, W. M. (2012). Arrestins regulate cell spreading and motility via focal adhesion dynamics. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/12660

Chicago Manual of Style (16th Edition):

Cleghorn, Whitney Marie. “Arrestins regulate cell spreading and motility via focal adhesion dynamics.” 2012. Doctoral Dissertation, Vanderbilt University. Accessed January 19, 2021. http://hdl.handle.net/1803/12660.

MLA Handbook (7th Edition):

Cleghorn, Whitney Marie. “Arrestins regulate cell spreading and motility via focal adhesion dynamics.” 2012. Web. 19 Jan 2021.

Vancouver:

Cleghorn WM. Arrestins regulate cell spreading and motility via focal adhesion dynamics. [Internet] [Doctoral dissertation]. Vanderbilt University; 2012. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1803/12660.

Council of Science Editors:

Cleghorn WM. Arrestins regulate cell spreading and motility via focal adhesion dynamics. [Doctoral Dissertation]. Vanderbilt University; 2012. Available from: http://hdl.handle.net/1803/12660


Vanderbilt University

5. Bartlett, Christina Swan. Role of the prostaglandin E2 receptor EP1 in hypertensive end-organ damage.

Degree: PhD, Pharmacology, 2012, Vanderbilt University

 Hypertension is a prevalent disease affecting one in three adults in the United States. Approximately 25 % of the adult population is either not receiving… (more)

Subjects/Keywords: Prostaglandin; Receptor; Hypertension; Diabetes

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APA (6th Edition):

Bartlett, C. S. (2012). Role of the prostaglandin E2 receptor EP1 in hypertensive end-organ damage. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/14916

Chicago Manual of Style (16th Edition):

Bartlett, Christina Swan. “Role of the prostaglandin E2 receptor EP1 in hypertensive end-organ damage.” 2012. Doctoral Dissertation, Vanderbilt University. Accessed January 19, 2021. http://hdl.handle.net/1803/14916.

MLA Handbook (7th Edition):

Bartlett, Christina Swan. “Role of the prostaglandin E2 receptor EP1 in hypertensive end-organ damage.” 2012. Web. 19 Jan 2021.

Vancouver:

Bartlett CS. Role of the prostaglandin E2 receptor EP1 in hypertensive end-organ damage. [Internet] [Doctoral dissertation]. Vanderbilt University; 2012. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1803/14916.

Council of Science Editors:

Bartlett CS. Role of the prostaglandin E2 receptor EP1 in hypertensive end-organ damage. [Doctoral Dissertation]. Vanderbilt University; 2012. Available from: http://hdl.handle.net/1803/14916


Vanderbilt University

6. Strayhorn, William David. Expression of Dub-1 and Dub-2 and analysis of a role for deubiquitination in the regulation of nuclear factor-kappa B.

Degree: PhD, Cell and Developmental Biology, 2004, Vanderbilt University

 The ubiquitin-proteasome pathway (UPP) is the principal mechanism for the selective degradation of short-lived proteins. The proximal signal for UPP-mediated proteolysis is the covalent modification… (more)

Subjects/Keywords: I kappa B alpha; nuclear factor-kappa B; UBP; deubiquitination; DUB; ubiquitin

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APA (6th Edition):

Strayhorn, W. D. (2004). Expression of Dub-1 and Dub-2 and analysis of a role for deubiquitination in the regulation of nuclear factor-kappa B. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/11876

Chicago Manual of Style (16th Edition):

Strayhorn, William David. “Expression of Dub-1 and Dub-2 and analysis of a role for deubiquitination in the regulation of nuclear factor-kappa B.” 2004. Doctoral Dissertation, Vanderbilt University. Accessed January 19, 2021. http://hdl.handle.net/1803/11876.

MLA Handbook (7th Edition):

Strayhorn, William David. “Expression of Dub-1 and Dub-2 and analysis of a role for deubiquitination in the regulation of nuclear factor-kappa B.” 2004. Web. 19 Jan 2021.

Vancouver:

Strayhorn WD. Expression of Dub-1 and Dub-2 and analysis of a role for deubiquitination in the regulation of nuclear factor-kappa B. [Internet] [Doctoral dissertation]. Vanderbilt University; 2004. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1803/11876.

Council of Science Editors:

Strayhorn WD. Expression of Dub-1 and Dub-2 and analysis of a role for deubiquitination in the regulation of nuclear factor-kappa B. [Doctoral Dissertation]. Vanderbilt University; 2004. Available from: http://hdl.handle.net/1803/11876


Vanderbilt University

7. Li, Chunsheng. MyD88: central relay station of Interleukin 1 signaling pathway.

Degree: PhD, Microbiology and Immunology, 2005, Vanderbilt University

 As inflammation is a major mechanism of disease, we investigated the signal transduction processes induced by the key inflammatory cytokine Interleukin (IL) 1 beta as… (more)

Subjects/Keywords: IL-1beta signaling pathway; MyD88; gene expression profiling; inflammation; nuclear import; IL-1 receptor accessary protein; Interleukin-1; Cellular signal transduction

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

APA (6th Edition):

Li, C. (2005). MyD88: central relay station of Interleukin 1 signaling pathway. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/15268

Chicago Manual of Style (16th Edition):

Li, Chunsheng. “MyD88: central relay station of Interleukin 1 signaling pathway.” 2005. Doctoral Dissertation, Vanderbilt University. Accessed January 19, 2021. http://hdl.handle.net/1803/15268.

MLA Handbook (7th Edition):

Li, Chunsheng. “MyD88: central relay station of Interleukin 1 signaling pathway.” 2005. Web. 19 Jan 2021.

Vancouver:

Li C. MyD88: central relay station of Interleukin 1 signaling pathway. [Internet] [Doctoral dissertation]. Vanderbilt University; 2005. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1803/15268.

Council of Science Editors:

Li C. MyD88: central relay station of Interleukin 1 signaling pathway. [Doctoral Dissertation]. Vanderbilt University; 2005. Available from: http://hdl.handle.net/1803/15268

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