Abstract

Principal Investigator/Program Director (Last, first, middle): Valentine, Joan S. - Core A ?WhiteleQQe. Julian P. DESCRIPTION: The role of analytical Core A is to provide a comprehensive range of services for the physical, chemical and proteomic characterization of SOD-containing and other aggregates derived from both in vivo transgenic ALS mouse models and in vitro from SOD1 mutants treated with potential pro-oxidants. Importantly, our analyses are based on a discovery-based approach that does not rely upon preconceptions as to what we may be lookingfor.
Specific Aim 1. Proteomic analysis of aggregates Specific Aim 2. Metal analysis of aggregates and SOD1 protein preparations.
Specific Aim 3. Aggregate heterogeneity and molecular weight.
Specific Aim 4. Protein mass profiling and covalent modification sites.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Program Projects (P01)
Project #
5P01NS049134-04
Application #
7631370
Study Section
National Institute of Neurological Disorders and Stroke Initial Review Group (NSD)
Project Start
Project End
Budget Start
2008-05-31
Budget End
2009-05-30
Support Year
4
Fiscal Year
2008
Total Cost
$189,545
Indirect Cost

  Institution

Name
University of California Los Angeles
Department
Type
DUNS #
092530369
City
Los Angeles
State
CA
Country
United States
Zip Code
90095

  Publications

Sheng, Yuewei; Capri, Joseph; Waring, Alan et al. (2018) Exposure of Solvent-Inaccessible Regions in the Amyloidogenic Protein Human SOD1 Determined by Hydroxyl Radical Footprinting. J Am Soc Mass Spectrom :
Ayers, Jacob I; McMahon, Benjamin; Gill, Sabrina et al. (2017) Relationship between mutant Cu/Zn superoxide dismutase 1 maturation and inclusion formation in cell models. J Neurochem 140:140-150
Xu, Guilian; Fromholt, Susan; Ayers, Jacob I et al. (2015) Substantially elevating the levels of ?B-crystallin in spinal motor neurons of mutant SOD1 mice does not significantly delay paralysis or attenuate mutant protein aggregation. J Neurochem 133:452-64
Saelices, Lorena; Johnson, Lisa M; Liang, Wilson Y et al. (2015) Uncovering the Mechanism of Aggregation of Human Transthyretin. J Biol Chem 290:28932-43
Gelfand, Paul; Smith, Randy J; Stavitski, Eli et al. (2015) Characterization of Protein Structural Changes in Living Cells Using Time-Lapsed FTIR Imaging. Anal Chem 87:6025-31
Chattopadhyay, Madhuri; Nwadibia, Ekeoma; Strong, Cynthia D et al. (2015) The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation. J Biol Chem 290:30624-36
Xu, Guilian; Ayers, Jacob I; Roberts, Brittany L et al. (2015) Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice. Hum Mol Genet 24:1019-35
Sheng, Yuewei; Abreu, Isabel A; Cabelli, Diane E et al. (2014) Superoxide dismutases and superoxide reductases. Chem Rev 114:3854-918
Brown, Hilda H; Borchelt, David R (2014) Analysis of mutant SOD1 electrophoretic mobility by Blue Native gel electrophoresis; evidence for soluble multimeric assemblies. PLoS One 9:e104583
Ayers, Jacob I; Xu, Guilian; Pletnikova, Olga et al. (2014) Conformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases. Acta Neuropathol Commun 2:55

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