Amy M. Ruschak, Ph.D.

Affiliations: 
Yale University, New Haven, CT 
Area:
Protein Folding and Dynamics, Structural Biology
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"Amy Ruschak"
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Andrew D. Miranker grad student 2008 Yale
 (Mechanism of amyloid fiber formation in a peptide model system.)
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Publications

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Witten J, Ruschak A, Poterba T, et al. (2015) Mapping Protein Conformational Landscapes under Strongly Native Conditions with Hydrogen Exchange Mass Spectrometry. The Journal of Physical Chemistry. B. 119: 10016-24
Ruschak AM, Rose JD, Coughlin MP, et al. (2013) Engineered solubility tag for solution NMR of proteins. Protein Science : a Publication of the Protein Society. 22: 1646-54
Ruschak AM, Kay LE. (2012) Proteasome allostery as a population shift between interchanging conformers. Proceedings of the National Academy of Sciences of the United States of America. 109: E3454-62
Velyvis A, Ruschak AM, Kay LE. (2012) An economical method for production of (2)H, (13)CH3-threonine for solution NMR studies of large protein complexes: application to the 670 kDa proteasome. Plos One. 7: e43725
Ruschak AM, Slassi M, Kay LE, et al. (2011) Novel proteasome inhibitors to overcome bortezomib resistance. Journal of the National Cancer Institute. 103: 1007-17
Religa TL, Ruschak AM, Rosenzweig R, et al. (2011) Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease. Journal of the American Chemical Society. 133: 9063-8
Ruschak AM, Velyvis A, Kay LE. (2010) A simple strategy for ¹³C, ¹H labeling at the Ile-γ2 methyl position in highly deuterated proteins. Journal of Biomolecular Nmr. 48: 129-35
Ruschak AM, Religa TL, Breuer S, et al. (2010) The proteasome antechamber maintains substrates in an unfolded state. Nature. 467: 868-71
Ruschak AM, Kay LE. (2010) Methyl groups as probes of supra-molecular structure, dynamics and function. Journal of Biomolecular Nmr. 46: 75-87
Ruschak AM, Miranker AD. (2009) The role of prefibrillar structures in the assembly of a peptide amyloid. Journal of Molecular Biology. 393: 214-26
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