Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM028222-17
Application #
2175137
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1980-01-01
Project End
1997-12-31
Budget Start
1996-01-01
Budget End
1996-12-31
Support Year
17
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of California Los Angeles
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
119132785
City
Los Angeles
State
CA
Country
United States
Zip Code
90095

  Publications

Sea, Kevin; Sohn, Se Hui; Durazo, Armando et al. (2015) Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase. J Biol Chem 290:2405-18
Sheng, Yuewei; Abreu, Isabel A; Cabelli, Diane E et al. (2014) Superoxide dismutases and superoxide reductases. Chem Rev 114:3854-918
Ming, Li-June; Valentine, Joan Selverstone (2014) Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases. J Biol Inorg Chem 19:647-57
Durazo, Armando; Shaw, Bryan F; Chattopadhyay, Madhuri et al. (2009) Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature. J Biol Chem 284:34382-9
Oztug Durer, Zeynep A; Cohlberg, Jeffrey A; Dinh, Phong et al. (2009) Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase. PLoS One 4:e5004
Cao, Xiaohang; Antonyuk, Svetlana V; Seetharaman, Sai V et al. (2008) Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. J Biol Chem 283:16169-77
Potter, Soshanna Zittin; Zhu, Haining; Shaw, Bryan Francis et al. (2007) Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein. J Am Chem Soc 129:4575-83
Shaw, Bryan Francis; Durazo, Armando; Nersissian, Aram M et al. (2006) Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry. J Biol Chem 281:18167-76
Ferri, Alberto; Cozzolino, Mauro; Crosio, Claudia et al. (2006) Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials. Proc Natl Acad Sci U S A 103:13860-5
Strange, Richard W; Antonyuk, Svetlana V; Hough, Michael A et al. (2006) Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. J Mol Biol 356:1152-62

Showing the most recent 10 out of 56 publications