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035 a| (Sirsi) o1105587109;

035 a| (OCoLC)1105587109;

049 a| EREE;

100 1 a| Johnson, Dylan James ,e| author.?| UNAUTHORIZED;

245 14 a| The C-terminus of troponin T modulates calcium regulation of actin-myosin interactions /c| by Dylan James Johnson.;

264 1 a| [Greenville, N.C.] :b| [East Carolina University],c| 2019.;

300 a| 204 pages :b| illustrations.;

336 a| textb| txt2| rdacontent;

337 a| computerb| c2| rdamedia;

338 a| online resourceb| cr2| rdacarrier;

347 a| text fileb| PDFc| 4.928 MB2| rda;

490 1 a| ECU Brody School of Medicine dissertation;

538 a| System requirements: Adobe Reader.;

538 a| Mode of access: World Wide Web.;

502 b| Ph.D.c| East Carolina Universityd| 2019.;

500 a| Presented to the faculty of the Department of Biochemistry;

500 a| Advisor: Joseph Chalovich;

500 a| Title from PDF t.p. (viewed October 3, 2019).;

520 3 a| The highly conserved terminal fourteen C-terminal residues of troponin T play a novel role in the regulation of striated muscle contraction. Elimination of the terminal fourteen residues of the C-terminal region of troponin T stabilizes the functional active state and destabilizes one of two inactive states, the blocked state. We've used a series of functional assays to assess the magnitude of disruption to the actin state distribution by different mutations within that C-terminus. In doing so, we have identified the characteristics of the C-terminus required for its function. To probe the structural mechanism of the C-terminus of troponin T, we used a series of FRET pairs to measure the interactions of the C-terminus of troponin T and how those interactions are disrupted by C-terminal mutation. Though mutation in the C-terminus of troponin T is associated with a specific cardiovascular disease, hypertrophic cardiomyopathy, the findings from our lab indicate this region's function has broader implications on our fundamental understanding of striated muscle regulation and treatment of cardiovascular disease. Our incomplete understanding of this cycle's regulation has led to the generation of a variety of hypothesis to explain the gaps in our knowledge. We have taken steps to characterize the functional and structural consequence of mutation within the C-terminus of troponin T and now believe we have closed some of the gaps in our knowledge of this regulated cycle.;

504 a| Includes bibliographical references.;

650 2 a| Troponin T.=| ^A1337338;

650 2 a| Actins.=| ^A926433;

650 2 a| Calcium.=| ^A1058002;

650 2 a| Myosins.=| ^A939365;

650 2 a| Calcium, Dietary.=| ^A951242;

653 a| mutation;

653 a| cardiomyopathy;

653 a| tropomyosin;

653 a| striated;

653 a| cardiac;

653 a| C-terminus;

653 a| TnT;

700 1 a| Chalovich, Joseph,e| degree supervisor.?| UNAUTHORIZED;

710 2 a| East Carolina University.b| Department of Biochemistry and Molecular Biology.?| UNAUTHORIZED;

830 0 a| ECU Brody School of Medicine dissertation.?| UNAUTHORIZED;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/7238;

949 o| wjh;

994 a| C0b| ERE;

096 a| WE 500;

596 a| 1 4;

998 a| 5111087;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5111087-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 6/24/2019x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5111087-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 6/24/2019x| ETDz| HERESOURCE;

The C-terminus of troponin T modulates calcium regulation of actin-myosin interactions / by Dylan James Johnson.

Author/creator	Johnson, Dylan James author.
Other author	Chalovich, Joseph, degree supervisor.
Other author	East Carolina University. Department of Biochemistry and Molecular Biology.
Format	Theses and dissertations
Publication	[Greenville, N.C.] : [East Carolina University], 2019.
Description	204 pages : illustrations.
Supplemental Content	Access via ScholarShip
Subjects	Troponin T. Actins. Calcium. Myosins. Calcium, Dietary.

Series	ECU Brody School of Medicine dissertation ECU Brody School of Medicine dissertation. UNAUTHORIZED
Summary	The highly conserved terminal fourteen C-terminal residues of troponin T play a novel role in the regulation of striated muscle contraction. Elimination of the terminal fourteen residues of the C-terminal region of troponin T stabilizes the functional active state and destabilizes one of two inactive states, the blocked state. We've used a series of functional assays to assess the magnitude of disruption to the actin state distribution by different mutations within that C-terminus. In doing so, we have identified the characteristics of the C-terminus required for its function. To probe the structural mechanism of the C-terminus of troponin T, we used a series of FRET pairs to measure the interactions of the C-terminus of troponin T and how those interactions are disrupted by C-terminal mutation. Though mutation in the C-terminus of troponin T is associated with a specific cardiovascular disease, hypertrophic cardiomyopathy, the findings from our lab indicate this region's function has broader implications on our fundamental understanding of striated muscle regulation and treatment of cardiovascular disease. Our incomplete understanding of this cycle's regulation has led to the generation of a variety of hypothesis to explain the gaps in our knowledge. We have taken steps to characterize the functional and structural consequence of mutation within the C-terminus of troponin T and now believe we have closed some of the gaps in our knowledge of this regulated cycle.
General note	Presented to the faculty of the Department of Biochemistry
General note	Advisor: Joseph Chalovich
General note	Title from PDF t.p. (viewed October 3, 2019).
Dissertation note	Ph.D. East Carolina University 2019.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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The C-terminus of troponin T modulates calcium regulation of actin-myosin interactions / by Dylan James Johnson.

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