Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI054467-02
Application #
6799213
Study Section
Physiological Chemistry Study Section (PC)
Program Officer
Kirkham, Perry M
Project Start
2003-09-15
Project End
2007-12-31
Budget Start
2004-01-01
Budget End
2004-12-31
Support Year
2
Fiscal Year
2004
Total Cost
$235,450
Indirect Cost

  Institution

Name
University of Oklahoma Health Sciences Center
Department
Biochemistry
Type
Schools of Medicine
DUNS #
878648294
City
Oklahoma City
State
OK
Country
United States
Zip Code
73117

  Publications

Matveev, Alexander V; Fitzgerald, J Browning; Xu, Jianhua et al. (2010) The disease-causing mutations in the carboxyl terminus of the cone cyclic nucleotide-gated channel CNGA3 subunit alter the local secondary structure and interfere with the channel active conformational change. Biochemistry 49:1628-39
Zhao, Shuying; Gwyn, Lori M; De, Pallabi et al. (2009) A non-sequence-specific DNA binding mode of RAG1 is inhibited by RAG2. J Mol Biol 387:744-58
Gwyn, Lori M; Peak, Mandy M; De, Pallabi et al. (2009) A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity. J Mol Biol 390:863-78
De, Pallabi; Zhao, Shuying; Gwyn, Lori M et al. (2008) Thermal dependency of RAG1 self-association properties. BMC Biochem 9:5
De, Pallabi; Rodgers, Karla K (2004) Putting the pieces together: identification and characterization of structural domains in the V(D)J recombination protein RAG1. Immunol Rev 200:70-82
De, Pallabi; Peak, Mandy M; Rodgers, Karla K (2004) DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated. Mol Cell Biol 24:6850-60