Abstract

This is a Shannon Award providing partial support for research projects that fall short of the assigned institute's funding range but are in the margin of excellence. The Shannon award is intended to provide support to test the feasibility of the approach; develop further tests and refine research techniques; perform secondary analysis of available data sets; or conduct discrete projects that can demonstrate the PI's research capabilities or lend additional weight to an already meritorious application. Further scientific data for the CRISP System are unavailable at this time.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
James A. Shannon Director's Award (R55)
Project #
1R55GM049928-01
Application #
3509851
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1993-09-01
Project End
1994-04-30
Budget Start
1993-09-01
Budget End
1994-04-30
Support Year
1
Fiscal Year
1993
Total Cost
Indirect Cost

  Institution

Name
University of Minnesota Twin Cities
Department
Type
Other Domestic Higher Education
DUNS #
168559177
City
Minneapolis
State
MN
Country
United States
Zip Code
55455

  Publications

Bartholow, Thomas G; Sanford, Brianne L; Cao, Bach et al. (2014) Strictly conserved lysine of prolyl-tRNA Synthetase editing domain facilitates binding and positioning of misacylated tRNA(Pro.). Biochemistry 53:1059-68
Dewan, Varun; Reader, John; Forsyth, Karin-Musier (2014) Role of aminoacyl-tRNA synthetases in infectious diseases and targets for therapeutic development. Top Curr Chem 344:293-329
Vargas-Rodriguez, Oscar; Musier-Forsyth, Karin (2013) Exclusive use of trans-editing domains prevents proline mistranslation. J Biol Chem 288:14391-9
Kumar, Sandeep; Das, Mom; Hadad, Christopher M et al. (2013) Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK. J Phys Chem B 117:4521-7
Johnson, James M; Sanford, Brianne L; Strom, Alexander M et al. (2013) Multiple pathways promote dynamical coupling between catalytic domains in Escherichia coli prolyl-tRNA synthetase. Biochemistry 52:4399-412
Kumar, Sandeep; Das, Mom; Hadad, Christopher M et al. (2012) Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket. J Biol Chem 287:3175-84
Kumar, Sandeep; Das, Mom; Hadad, Christopher M et al. (2012) Substrate and enzyme functional groups contribute to translational quality control by bacterial prolyl-tRNA synthetase. J Phys Chem B 116:6991-9
Sanford, Brianne; Cao, Bach; Johnson, James M et al. (2012) Role of coupled dynamics in the catalytic activity of prokaryotic-like prolyl-tRNA synthetases. Biochemistry 51:2146-56
So, Byung Ran; An, Songon; Kumar, Sandeep et al. (2011) Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons. J Biol Chem 286:31810-20
Ling, Jiqiang; So, Byung Ran; Yadavalli, Srujana S et al. (2009) Resampling and editing of mischarged tRNA prior to translation elongation. Mol Cell 33:654-60