+publisher:"University of Missouri – Columbia" +contributor:("Van Doren, Steven")

1. Marcink, Tara. Membrane interactions with membrane type 1 matrix metalloproteinase.

Degree: 2018, University of Missouri – Columbia

► Membrane type 1 matrix metalloproteinase (MT1-MMP) is essential to a myriad of extracellular activities including tumor cell migration and angiogenesis. At the cell surface, MT1-MMP… (more)

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APA (6^th Edition):

Marcink, T. (2018). Membrane interactions with membrane type 1 matrix metalloproteinase. (Thesis). University of Missouri – Columbia. Retrieved from http://hdl.handle.net/10355/68915

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Marcink, Tara. “Membrane interactions with membrane type 1 matrix metalloproteinase.” 2018. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. http://hdl.handle.net/10355/68915.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Marcink, Tara. “Membrane interactions with membrane type 1 matrix metalloproteinase.” 2018. Web. 15 Apr 2021.

Vancouver:

Marcink T. Membrane interactions with membrane type 1 matrix metalloproteinase. [Internet] [Thesis]. University of Missouri – Columbia; 2018. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10355/68915.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Marcink T. Membrane interactions with membrane type 1 matrix metalloproteinase. [Thesis]. University of Missouri – Columbia; 2018. Available from: http://hdl.handle.net/10355/68915

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Missouri – Columbia

2. Xu, Jia (Research scientist). Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis.

Degree: 2016, University of Missouri – Columbia

URL: https://doi.org/10.32469/10355/59793

► Phosphomannomutase/phosphoglucomutase (PMM/PGM) contributes to the infectivity of an opportunistic human pathogen Pseudomonas aeruginosa by participating in carbohydrate biosynthesis. As a phospho-transfer enzyme, PMM/PGM catalyzes reversible… (more)

▼ Phosphomannomutase/phosphoglucomutase (PMM/PGM) contributes to the infectivity of an opportunistic human pathogen Pseudomonas aeruginosa by participating in carbohydrate biosynthesis. As a phospho-transfer enzyme, PMM/PGM catalyzes reversible conversion between 1- and 6- phosphosugars via a bisphosphorylated hexose intermediate rotating 180[degree symbol] in the catalytic cleft. Although PMM/PGM is well studied both structurally and kinetically, the mechanisms of its intramolecular and intermolecular communication are less well understood, especially in solution. Multiple solution NMR techniques are used in this dissertation's work to reveal information on PMM/PGM interactions at the atomic level. NMR-detected hydrogen exchange in combination with molecular dynamics and electrostatic calculations found phosphorylation of active Ser108 residue stabilizes PMM/PGM by attracting domains together. Responses of PMM/PGM to various phosphosugars were characterized by NMR-detected titrations. The large set of assigned peaks were analyzed by various types of principal component analysis (PCA) to derive binding isotherms, over-arching relationships among phosphosugar ligand binding reactions, and equilibrium shifts of PMM/PGM during its catalytic cycle. PCA was also found to be able to extract binding isotherms directly from non-interpreted 2D NMR spectra of complexes forming in solution. Procedures were identified that are reliable for obtaining the binding isotherms, regardless of the spectral peaks being in the fast, slow, or intermediate exchange regimes, or mixtures thereof. Applying PCA to time-domain NMR data also yields binding isotherms from titrations in fast or slow exchange. The algorithm readily extracts from an MRI movie its time courses, such as breathing and heart rate in chest imaging. To enable the community to exploit these new capabilities, we have developed the multi-platform software named TREND to track equilibrium and non-equilibrium population shifts among 2D data frames. The principal components obtained represent the main changes among the data frames. Besides binding isotherms and time courses, the main changes extracted by TREND can be any variety of population shifts. TREND can reconstruct the series of measurements from selected principal components. TREND supports multiple data formats, including raw NMR data, images, movies, lists, and spreadsheet files. The software can also be used for data clustering or noise filtering. Advisors/Committee Members: Van Doren, Steven R., 1963- (advisor), Beamer, Lesa J. (Lesa Jean) (advisor).

Subjects/Keywords: Pseudomonas aeruginosa infections; Nuclear magnetic resonance spectroscopy

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

APA (6^th Edition):

Xu, J. (. s. (2016). Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis. (Thesis). University of Missouri – Columbia. Retrieved from https://doi.org/10.32469/10355/59793

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Xu, Jia (Research scientist). “Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis.” 2016. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. https://doi.org/10.32469/10355/59793.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Xu, Jia (Research scientist). “Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis.” 2016. Web. 15 Apr 2021.

Vancouver:

Xu J(s. Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis. [Internet] [Thesis]. University of Missouri – Columbia; 2016. [cited 2021 Apr 15]. Available from: https://doi.org/10.32469/10355/59793.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Xu J(s. Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis. [Thesis]. University of Missouri – Columbia; 2016. Available from: https://doi.org/10.32469/10355/59793

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Missouri – Columbia

3. Zhao, Yingchu. Transient collagen triple-helix binding to membrane type 1 matrix metalloproteinase : interaction studies and NMR-guided structural docking.

Degree: 2015, University of Missouri – Columbia

URL: http://hdl.handle.net/10355/49038

► [ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] MT1-MMP (MMP-14) as pericellular collagenase is critically involved in cancer cell invasion through collagen… (more)

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

APA (6^th Edition):

Zhao, Y. (2015). Transient collagen triple-helix binding to membrane type 1 matrix metalloproteinase : interaction studies and NMR-guided structural docking. (Thesis). University of Missouri – Columbia. Retrieved from http://hdl.handle.net/10355/49038

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Zhao, Yingchu. “Transient collagen triple-helix binding to membrane type 1 matrix metalloproteinase : interaction studies and NMR-guided structural docking.” 2015. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. http://hdl.handle.net/10355/49038.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Zhao, Yingchu. “Transient collagen triple-helix binding to membrane type 1 matrix metalloproteinase : interaction studies and NMR-guided structural docking.” 2015. Web. 15 Apr 2021.

Vancouver:

Zhao Y. Transient collagen triple-helix binding to membrane type 1 matrix metalloproteinase : interaction studies and NMR-guided structural docking. [Internet] [Thesis]. University of Missouri – Columbia; 2015. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10355/49038.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Zhao Y. Transient collagen triple-helix binding to membrane type 1 matrix metalloproteinase : interaction studies and NMR-guided structural docking. [Thesis]. University of Missouri – Columbia; 2015. Available from: http://hdl.handle.net/10355/49038

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Missouri – Columbia

4. Byrne, Todd S. Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea.

Degree: 2012, University of Missouri – Columbia

URL: http://hdl.handle.net/10355/33129

► Matrix metalloproteinase (MMP-12) is associated with many costly, life-threatening diseases, such as atherosclerosis, pulmonary emphysema, asthma, and multiple sclerosis. Therefore, macrophage secreted MMP-12 is likely… (more)

▼ Matrix metalloproteinase (MMP-12) is associated with many costly, life-threatening diseases, such as atherosclerosis, pulmonary emphysema, asthma, and multiple sclerosis. Therefore, macrophage secreted MMP-12 is likely found in many parts of the body likely interacting with extracellular components as have been shown and previously investigated by in vitro studies. MMP-12 is capable of cleaving elastin and may biologically cleave other extracellular components, such as collagen. This article seeks to investigate interactions of MMP-12 with a collagen-mimicking triple helical peptide (THP). The methods employed for this study involved paramagnetic relaxation enhancement (PRE). A THP paramagnetically labeled with the artificial amino acid TOAC was used to investigate the interaction between MMP-12 and a THP. This study aims to answer the question of how a THP binds to MMP-12. Preliminary structures of the complex presented here have converged. The THP binds to MMP-12 in a specific manner in one type of angle of inclination. Whereby, the orientations of the THP appear to have the N-terminus along the unprimed side of MMP-12. These results may also further hint at an exosite near the C2 calcium binding site on MMP-12. The inhibition of MMP-12 by a natural polyphenol, (-)-Epigallocatechin gallate (EGCG) was investigated. Also, structural information concerning the binding sites of EGCG to MMP-12 was obtained. The methods employed involve paramagnetic relaxation enhancement, inhibition of enzyme activity, and stability by urea denaturation. A paramagnetic ECG, an analog of EGCG, was generated by incubating briefly in the presence of peroxide and horse radish peroxidase. The radical was used in an attempt to characterize the interaction between EGCG and MMP-12. The initial NMR investigations involving paramagnetic relaxation enhancement (PRE) or/and NOE experiments with EGCG suggest two to three binding sites on MMP-12, including one near a calcium binding site. Inhibition of enzyme kinetics and denaturation melts were also carried out with MMP-12 in the presence of EGCG to better ascertain the most significant binding site of EGCG to MMP-12. The kinetic experiments indicate that inhibition appears to be non-competitive, and there is a calcium dependence for the EGCG inhibition of MMP-12. The calcium dependent inhibition suggests that the calcium site (C2 site or Ca 403) indicated in the PRE and NOE experiments could be the key site of allosteric inhibition of MMP-12 by EGCG. This study investigates the interaction of MMP-12 with dodecyl phosphatidylcholine (DPC) micelles and 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) micelles. The composition of the micelles has been varied. For example, DPC/CHAPS micelles and DPC/CHAPS doped with cholesterol sulfate micelles have been investigated. Chemical shift perturbations and line broadening analysis has been conducted, and the initial results suggest a KD of physiological importance. Cross -correlation rates and the extent of chemical shift perturbation between the DPC/CHAPS… Advisors/Committee Members: Van Doren, Steven (advisor).

Subjects/Keywords: matrix metalloproteinase; extracellular components; binding site

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

APA (6^th Edition):

Byrne, T. S. (2012). Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea. (Thesis). University of Missouri – Columbia. Retrieved from http://hdl.handle.net/10355/33129

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Byrne, Todd S. “Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea.” 2012. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. http://hdl.handle.net/10355/33129.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Byrne, Todd S. “Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea.” 2012. Web. 15 Apr 2021.

Vancouver:

Byrne TS. Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea. [Internet] [Thesis]. University of Missouri – Columbia; 2012. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10355/33129.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Byrne TS. Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea. [Thesis]. University of Missouri – Columbia; 2012. Available from: http://hdl.handle.net/10355/33129

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Missouri – Columbia

5. Palmier, Mark O., 1951-. Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions.

Degree: 2008, University of Missouri – Columbia

URL: https://doi.org/10.32469/10355/9192

► [ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] What determines MMP-12 elastase activity? We have found that the fibrillar substrate specificity of… (more)

Subjects/Keywords: Metalloproteinases; Antigenic determinants; Mutagenesis; Emphysema, Pulmonary; Aortic aneurysms

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

APA (6^th Edition):

Palmier, Mark O., 1. (2008). Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions. (Thesis). University of Missouri – Columbia. Retrieved from https://doi.org/10.32469/10355/9192

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Palmier, Mark O., 1951-. “Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions.” 2008. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. https://doi.org/10.32469/10355/9192.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Palmier, Mark O., 1951-. “Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions.” 2008. Web. 15 Apr 2021.

Vancouver:

Palmier, Mark O. 1. Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions. [Internet] [Thesis]. University of Missouri – Columbia; 2008. [cited 2021 Apr 15]. Available from: https://doi.org/10.32469/10355/9192.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Palmier, Mark O. 1. Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions. [Thesis]. University of Missouri – Columbia; 2008. Available from: https://doi.org/10.32469/10355/9192

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Missouri – Columbia

6. Palmier, Mark O., 1951-. Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions.

Degree: 2008, University of Missouri – Columbia

URL: http://hdl.handle.net/10355/9192

► [ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] What determines MMP-12 elastase activity? We have found that the fibrillar substrate specificity of… (more)

Subjects/Keywords: Metalloproteinases; Antigenic determinants; Mutagenesis; Emphysema, Pulmonary; Aortic aneurysms

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

APA (6^th Edition):

Palmier, Mark O., 1. (2008). Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions. (Thesis). University of Missouri – Columbia. Retrieved from http://hdl.handle.net/10355/9192

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Palmier, Mark O., 1951-. “Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions.” 2008. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. http://hdl.handle.net/10355/9192.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Palmier, Mark O., 1951-. “Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions.” 2008. Web. 15 Apr 2021.

Vancouver:

Palmier, Mark O. 1. Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions. [Internet] [Thesis]. University of Missouri – Columbia; 2008. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10355/9192.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Palmier, Mark O. 1. Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions. [Thesis]. University of Missouri – Columbia; 2008. Available from: http://hdl.handle.net/10355/9192

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Missouri – Columbia

7. Ding, Zhaofeng, 1978-. Kinase-interacting FHA domain of kinase associated protein phosphatase : phosphopeptide interactions and NMR-detected dynamics.

Degree: PhD, 2007, University of Missouri – Columbia

URL: http://hdl.handle.net/10355/4729

► FHA domains are phosphoThr recognition modules found in diverse signaling proteins. Kinase-associated protein phosphatase (KAPP) from Arabidopsis employs its FHA domain in its negative regulation… (more)

Subjects/Keywords: Forkhead-associated domain.; Forkhead-associated domain; Plants – Development; Phosphoprotein phosphatases; Protein kinases; Nuclear magnetic resonance; Cellular signal transduction; Mutagenesis

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

APA (6^th Edition):

Ding, Zhaofeng, 1. (2007). Kinase-interacting FHA domain of kinase associated protein phosphatase : phosphopeptide interactions and NMR-detected dynamics. (Doctoral Dissertation). University of Missouri – Columbia. Retrieved from http://hdl.handle.net/10355/4729

Chicago Manual of Style (16^th Edition):

Ding, Zhaofeng, 1978-. “Kinase-interacting FHA domain of kinase associated protein phosphatase : phosphopeptide interactions and NMR-detected dynamics.” 2007. Doctoral Dissertation, University of Missouri – Columbia. Accessed April 15, 2021. http://hdl.handle.net/10355/4729.

MLA Handbook (7^th Edition):

Ding, Zhaofeng, 1978-. “Kinase-interacting FHA domain of kinase associated protein phosphatase : phosphopeptide interactions and NMR-detected dynamics.” 2007. Web. 15 Apr 2021.

Vancouver:

Ding, Zhaofeng 1. Kinase-interacting FHA domain of kinase associated protein phosphatase : phosphopeptide interactions and NMR-detected dynamics. [Internet] [Doctoral dissertation]. University of Missouri – Columbia; 2007. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10355/4729.

Council of Science Editors:

Ding, Zhaofeng 1. Kinase-interacting FHA domain of kinase associated protein phosphatase : phosphopeptide interactions and NMR-detected dynamics. [Doctoral Dissertation]. University of Missouri – Columbia; 2007. Available from: http://hdl.handle.net/10355/4729

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