James Arndt
Affiliations: | Chemistry | West Virginia University, Morgantown, WV, United States |
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| Arndt JR, Chaibva M, Beasley M, et al. (2019) Nucleation inhibition of Huntingtin protein (htt) by polyproline PPII helices: a potential interaction with the N-terminal α-helical region of htt. Biochemistry |
| Chaibva M, Jawahery S, Pilkington AW, et al. (2016) Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding. Biophysical Journal. 111: 349-62 |
| Legleiter J, Arndt JR, Chaibva M, et al. (2016) Factors Modulating the Interaction of Huntingtin with Lipid Membranes: Implications for Huntington's Disease Biophysical Journal. 110: 358a-359a |
| Arndt JR, Kondalaji SG, Maurer MM, et al. (2015) Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues. Biochemistry. 54: 4285-96 |
| Arndt JR, Chaibva M, Legleiter J. (2015) The emerging role of the first 17 amino acids of huntingtin in Huntington's disease. Biomolecular Concepts. 6: 33-46 |
| Arndt JR, Brown RJ, Burke KA, et al. (2015) Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation. Journal of Mass Spectrometry : Jms. 50: 117-26 |
| Arndt JR, Chaibva M, Legleiter J. (2015) The emerging role of the first 17 amino acids of huntingtin in Huntington's disease Biomolecular Concepts. 6: 33-46 |
| Arndt JR, Kondalaji SG, Maurer MM, et al. (2015) Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues Biochemistry. 54: 4285-4296 |
| Arndt JR, Kondalaji SG, Sarver O, et al. (2015) Gas-Phase Conformations of a Huntingtin N-Terminal Peptide Reveal Condensed-Phase Heterogeneity with and without the Presence of a PPII Helix Biophysical Journal. 108: 385a |
| Chaibva M, Arndt JR, Valentine SJ, et al. (2015) Acetylation Regulates the Interaction of Huntingtin with Lipid Membranes: Implications for Huntington Disease Biophysical Journal. 108: 254a |