This core is designed to provide an analytical underpinning to the quantitative efforts of all the projects. The ultimate goal is to distal the vast amount of raw biophysical and biochemical data generated by the individual projects into a single unifying model of several highly complementary models that will enhance our understanding of both FHC and the molecular structure function relationships for the various contractile proteins. To achieve this goal, state-of-the-art data analysis, complex computer-based modeling, and effective communication of the results will be required. Each project depends upon computational activities. In some, computers are fundamental to the gathering and processing of raw data, in others they support the visualization of molecular structures, storage and manipulation of genetic codes, etc. Although the development and maintenance of computer-oriented applications is now part of each laboratory's individual efforts, that current paradigm also causes significant duplication of effort. Since the members of the core must, by the nature of their work, maintain an advanced working knowledge of hardware and software applications, his expertise can be efficiently shared with all the projects as part of the core. The proposed design of the core would provide substantive effort in developing: 1) models and simulations related to individual projects; 2) a quantitative basis for translating data between various project- specific models; 3) new methods for data analysis and visualization;

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Program Projects (P01)
Project #
5P01HL059408-04
Application #
6692775
Study Section
Heart, Lung, and Blood Program Project Review Committee (HLBP)
Project Start
2002-02-01
Project End
2004-01-31
Budget Start
Budget End
Support Year
4
Fiscal Year
2002
Total Cost
Indirect Cost
Name
University of Vermont & St Agric College
Department
Type
DUNS #
066811191
City
Burlington
State
VT
Country
United States
Zip Code
05405
Singh, Sonia R; Robbins, Jeffrey (2018) Desmin and Cardiac Disease: An Unfolding Story. Circ Res 122:1324-1326
Lin, Brian Leei; Li, Amy; Mun, Ji Young et al. (2018) Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner. Sci Rep 8:2604
Kensler, Robert W; Craig, Roger; Moss, Richard L (2017) Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments. Proc Natl Acad Sci U S A 114:E1355-E1364
McLendon, Patrick M; Davis, Gregory; Gulick, James et al. (2017) An Unbiased High-Throughput Screen to Identify Novel Effectors That Impact on Cardiomyocyte Aggregate Levels. Circ Res 121:604-616
Bhuiyan, Md Shenuarin; McLendon, Patrick; James, Jeanne et al. (2016) In vivo definition of cardiac myosin-binding protein C's critical interactions with myosin. Pflugers Arch 468:1685-95
Gupta, Manish K; McLendon, Patrick M; Gulick, James et al. (2016) UBC9-Mediated Sumoylation Favorably Impacts Cardiac Function in Compromised Hearts. Circ Res 118:1894-905
Warshaw, David M (2016) HEART DISEASE. Throttling back the heart's molecular motor. Science 351:556-7
James, Jeanne; Robbins, Jeffrey (2016) Healing a Heart Through Genetic Intervention. Circ Res 118:920-2
Mun, Ji Young; Kensler, Robert W; Harris, Samantha P et al. (2016) The cMyBP-C HCM variant L348P enhances thin filament activation through an increased shift in tropomyosin position. J Mol Cell Cardiol 91:141-7
Previs, Michael J; Mun, Ji Young; Michalek, Arthur J et al. (2016) Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function. Proc Natl Acad Sci U S A 113:3239-44

Showing the most recent 10 out of 168 publications