Mary Elizabeth Huff

Affiliations: 
2003 Scripps Research Institute, La Jolla, La Jolla, CA, United States 
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Jeffery W. Kelly grad student 2003 Scripps Institute
 (The biochemical basis of gelsolin amyloid disease.)
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Publications

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Page LJ, Suk JY, Huff ME, et al. (2005) Metalloendoprotease cleavage triggers gelsolin amyloidogenesis. The Embo Journal. 24: 4124-32
Page LJ, Huff ME, Kelly JW, et al. (2004) Ca2+ binding protects against gelsolin amyloidosis. Biochemical and Biophysical Research Communications. 322: 1105-10
Zhang Q, Powers ET, Nieva J, et al. (2004) Metabolite-initiated protein misfolding may trigger Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America. 101: 4752-7
Huff ME, Balch WE, Kelly JW. (2003) Pathological and functional amyloid formation orchestrated by the secretory pathway. Current Opinion in Structural Biology. 13: 674-82
Huff ME, Page LJ, Balch WE, et al. (2003) Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of finnish type. Journal of Molecular Biology. 334: 119-27
DiDonato M, Craig L, Huff ME, et al. (2003) ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization. Journal of Molecular Biology. 332: 601-15
DiDonato M, Craig L, Huff ME, et al. (2003) Erratum to “ALS Mutants of Human Superoxide Dismutase form Fibrous Aggregates via Framework Destabilization” [J. Mol. Biol. 332 (2003) 601–615] Journal of Molecular Biology. 334: 175
Chen CD, Huff ME, Matteson J, et al. (2001) Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilization. The Embo Journal. 20: 6277-87
Ratnaswamy G, Huff ME, Su AI, et al. (2001) Destabilization of Ca2+-free gelsolin may not be responsible for proteolysis in Familial Amyloidosis of Finnish Type. Proceedings of the National Academy of Sciences of the United States of America. 98: 2334-9
Koepf EK, Petrassi HM, Ratnaswamy G, et al. (1999) Characterization of the structure and function of W --> F WW domain variants: identification of a natively unfolded protein that folds upon ligand binding. Biochemistry. 38: 14338-51
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