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You searched for +publisher:"University of Cincinnati" +contributor:("Stan, George"). Showing records 1 – 5 of 5 total matches.

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University of Cincinnati

1. Kravats, Andrea N. Coarse grained molecular dynamics simulations of the coupling between the allosteric mechanism of the ClpY nanomachine and threading of a substrate protein.

Degree: PhD, Arts and Sciences: Chemistry, 2013, University of Cincinnati

 Protein quality control is critical in maintaining cell viability. Recognitionand degradation of aberrant proteins in the cellular environment is essential,as many neurodegenerative diseases are linked… (more)

Subjects/Keywords: Physical Chemistry; ATPase; protein unfolding; protein translocation; coarse grained simulations

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APA (6th Edition):

Kravats, A. N. (2013). Coarse grained molecular dynamics simulations of the coupling between the allosteric mechanism of the ClpY nanomachine and threading of a substrate protein. (Doctoral Dissertation). University of Cincinnati. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384849649

Chicago Manual of Style (16th Edition):

Kravats, Andrea N. “Coarse grained molecular dynamics simulations of the coupling between the allosteric mechanism of the ClpY nanomachine and threading of a substrate protein.” 2013. Doctoral Dissertation, University of Cincinnati. Accessed June 20, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384849649.

MLA Handbook (7th Edition):

Kravats, Andrea N. “Coarse grained molecular dynamics simulations of the coupling between the allosteric mechanism of the ClpY nanomachine and threading of a substrate protein.” 2013. Web. 20 Jun 2019.

Vancouver:

Kravats AN. Coarse grained molecular dynamics simulations of the coupling between the allosteric mechanism of the ClpY nanomachine and threading of a substrate protein. [Internet] [Doctoral dissertation]. University of Cincinnati; 2013. [cited 2019 Jun 20]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384849649.

Council of Science Editors:

Kravats AN. Coarse grained molecular dynamics simulations of the coupling between the allosteric mechanism of the ClpY nanomachine and threading of a substrate protein. [Doctoral Dissertation]. University of Cincinnati; 2013. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384849649


University of Cincinnati

2. Tonddast-Navaei, Sam, M.S. Mechanism of Substrate Protein Remodeling by Allosteric Motions of AAA+ Nanomachines.

Degree: PhD, Arts and Sciences: Chemistry, 2014, University of Cincinnati

 Proteins are large complex molecules that play important roles in cellular activities such as DNA replication, molecular transport, cell immunity, and regulatory activities. Based on… (more)

Subjects/Keywords: Physical Chemistry; Protein unfolding; Protein translocation; Protein degradation; ATPase; p97; Molecular Dynamics

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APA (6th Edition):

Tonddast-Navaei, Sam, M. S. (2014). Mechanism of Substrate Protein Remodeling by Allosteric Motions of AAA+ Nanomachines. (Doctoral Dissertation). University of Cincinnati. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384869946

Chicago Manual of Style (16th Edition):

Tonddast-Navaei, Sam, M S. “Mechanism of Substrate Protein Remodeling by Allosteric Motions of AAA+ Nanomachines.” 2014. Doctoral Dissertation, University of Cincinnati. Accessed June 20, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384869946.

MLA Handbook (7th Edition):

Tonddast-Navaei, Sam, M S. “Mechanism of Substrate Protein Remodeling by Allosteric Motions of AAA+ Nanomachines.” 2014. Web. 20 Jun 2019.

Vancouver:

Tonddast-Navaei, Sam MS. Mechanism of Substrate Protein Remodeling by Allosteric Motions of AAA+ Nanomachines. [Internet] [Doctoral dissertation]. University of Cincinnati; 2014. [cited 2019 Jun 20]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384869946.

Council of Science Editors:

Tonddast-Navaei, Sam MS. Mechanism of Substrate Protein Remodeling by Allosteric Motions of AAA+ Nanomachines. [Doctoral Dissertation]. University of Cincinnati; 2014. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1384869946


University of Cincinnati

3. Smith, Nathan B. Computational Studies of Protein Folding Assistance and Conformational Pathways of Biological Nanomachines.

Degree: PhD, Arts and Sciences: Chemistry, 2015, University of Cincinnati

 Protein homeostasis is crucial for a cell's viability and therefore an organism's survival. Proteins, upon translation, must reach a three-dimensional structure known as their native… (more)

Subjects/Keywords: Physical Chemistry; allostery; p97; GroEL; biological nanomachine; protein folding; protein unfolding

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

APA (6th Edition):

Smith, N. B. (2015). Computational Studies of Protein Folding Assistance and Conformational Pathways of Biological Nanomachines. (Doctoral Dissertation). University of Cincinnati. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=ucin1448037580

Chicago Manual of Style (16th Edition):

Smith, Nathan B. “Computational Studies of Protein Folding Assistance and Conformational Pathways of Biological Nanomachines.” 2015. Doctoral Dissertation, University of Cincinnati. Accessed June 20, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1448037580.

MLA Handbook (7th Edition):

Smith, Nathan B. “Computational Studies of Protein Folding Assistance and Conformational Pathways of Biological Nanomachines.” 2015. Web. 20 Jun 2019.

Vancouver:

Smith NB. Computational Studies of Protein Folding Assistance and Conformational Pathways of Biological Nanomachines. [Internet] [Doctoral dissertation]. University of Cincinnati; 2015. [cited 2019 Jun 20]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1448037580.

Council of Science Editors:

Smith NB. Computational Studies of Protein Folding Assistance and Conformational Pathways of Biological Nanomachines. [Doctoral Dissertation]. University of Cincinnati; 2015. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1448037580

4. Wang, Huan, Ph.D. Elucidating Allosteric Mechanisms of the AAA+ ClpATPases Using Molecular Dynamics Simulations.

Degree: PhD, Arts and Sciences: Chemistry, 2015, University of Cincinnati

 AAA+ unfolding chaperones play vital function in cells as to maintain its proteasome balance.Misfolded or aggregated proteins could be unfolded and degraded by AAA+ unfolding… (more)

Subjects/Keywords: Physical Chemistry; protein quality control; AAA unfolding chaperone; protein folding; molecular dynamics

University of Cincinnati, P&G and National Science Foundations for their generous funding. And I… 

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

APA (6th Edition):

Wang, Huan, P. D. (2015). Elucidating Allosteric Mechanisms of the AAA+ ClpATPases Using Molecular Dynamics Simulations. (Doctoral Dissertation). University of Cincinnati. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=ucin1439296238

Chicago Manual of Style (16th Edition):

Wang, Huan, Ph D. “Elucidating Allosteric Mechanisms of the AAA+ ClpATPases Using Molecular Dynamics Simulations.” 2015. Doctoral Dissertation, University of Cincinnati. Accessed June 20, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1439296238.

MLA Handbook (7th Edition):

Wang, Huan, Ph D. “Elucidating Allosteric Mechanisms of the AAA+ ClpATPases Using Molecular Dynamics Simulations.” 2015. Web. 20 Jun 2019.

Vancouver:

Wang, Huan PD. Elucidating Allosteric Mechanisms of the AAA+ ClpATPases Using Molecular Dynamics Simulations. [Internet] [Doctoral dissertation]. University of Cincinnati; 2015. [cited 2019 Jun 20]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1439296238.

Council of Science Editors:

Wang, Huan PD. Elucidating Allosteric Mechanisms of the AAA+ ClpATPases Using Molecular Dynamics Simulations. [Doctoral Dissertation]. University of Cincinnati; 2015. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1439296238

5. Shrestha, Pooja. Mechanism of substrate protein remodeling by molecular chaperones.

Degree: PhD, Arts and Sciences: Physics, 2013, University of Cincinnati

 Protein quality control regulates the natural load of proteins by providing folding assistance or degradation mechanism to prevent misfolding or aggregation. It is maintained by… (more)

Subjects/Keywords: Biophysics; Protein quality control; Normal mode analysis; Multi-domain protein; Effect of confinement; Group II chaperonin; ClpP

…discussions. I would like to thanks to all my professors at University of Cincinnati, my professors… 

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

APA (6th Edition):

Shrestha, P. (2013). Mechanism of substrate protein remodeling by molecular chaperones. (Doctoral Dissertation). University of Cincinnati. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=ucin1378113185

Chicago Manual of Style (16th Edition):

Shrestha, Pooja. “Mechanism of substrate protein remodeling by molecular chaperones.” 2013. Doctoral Dissertation, University of Cincinnati. Accessed June 20, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1378113185.

MLA Handbook (7th Edition):

Shrestha, Pooja. “Mechanism of substrate protein remodeling by molecular chaperones.” 2013. Web. 20 Jun 2019.

Vancouver:

Shrestha P. Mechanism of substrate protein remodeling by molecular chaperones. [Internet] [Doctoral dissertation]. University of Cincinnati; 2013. [cited 2019 Jun 20]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1378113185.

Council of Science Editors:

Shrestha P. Mechanism of substrate protein remodeling by molecular chaperones. [Doctoral Dissertation]. University of Cincinnati; 2013. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=ucin1378113185

.