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Focal loss of the glutamate transporter EAAT2 in a transgenic rat model of SOD1 mutant-mediated amyotrophic lateral sclerosis (ALS).
Howland DS, Liu J, She Y, Goad B, Maragakis NJ, Kim B, Erickson J, Kulik J, DeVito L, Psaltis G, DeGennaro LJ, Cleveland DW, Rothstein JD. Howland DS, et al. Among authors: liu j. Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1604-9. doi: 10.1073/pnas.032539299. Epub 2002 Jan 29. Proc Natl Acad Sci U S A. 2002. PMID: 11818550 Free PMC article.
Toxicity of ALS-linked SOD1 mutants.
Williamson TL, Corson LB, Huang L, Burlingame A, Liu J, Bruijn LI, Cleveland DW. Williamson TL, et al. Among authors: liu j. Science. 2000 Apr 21;288(5465):399. doi: 10.1126/science.288.5465.399a. Science. 2000. PMID: 10798964 No abstract available.
Formation of advanced glycation end-product-modified superoxide dismutase-1 (SOD1) is one of the mechanisms responsible for inclusions common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutation, and transgenic mice expressing human SOD1 gene mutation.
Kato S, Nakashima K, Horiuchi S, Nagai R, Cleveland DW, Liu J, Hirano A, Takikawa M, Kato M, Nakano I, Sakoda S, Asayama K, Ohama E. Kato S, et al. Among authors: liu j. Neuropathology. 2001 Mar;21(1):67-81. doi: 10.1046/j.1440-1789.2001.00359.x. Neuropathology. 2001. PMID: 11304045 Review.
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