Year |
Citation |
Score |
2022 |
Kolář MH, Nagy G, Kunkel J, Vaiana SM, Bock LV, Grubmüller H. Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel. Nucleic Acids Research. 50: 2258-2269. PMID 35150281 DOI: 10.1093/nar/gkac038 |
0.324 |
|
2017 |
Modi T, Zerze GH, Mittal J, Vaiana SM, Ozkan SB. Intrinsically Disordered Protein Dynamics Uncovered through Dynamic Flexibility Index (DFI) Analysis Biophysical Journal. 112: 208a-209a. DOI: 10.1016/J.Bpj.2016.11.1152 |
0.503 |
|
2016 |
Vaiana SM. Slow Internal Dynamics and Structural Properties of IDPs of the Ct Family: Comparing Amyloid and Non-Amyloid Variants Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.056 |
0.497 |
|
2015 |
Sizemore SM, Cope SM, Roy A, Ghirlanda G, Vaiana SM. Slow Internal Dynamics and Charge Expansion in the Disordered Protein CGRP: A Comparison with Amylin. Biophysical Journal. 109: 1038-48. PMID 26331261 DOI: 10.1016/J.Bpj.2015.07.023 |
0.779 |
|
2015 |
Sizemore SM, Zerze GH, Cope SM, Mittal J, Vaiana SM. Comparing Solution Structures of Amylin and CGRP by Nanosecond Laser-Pump Spectroscopy and Atomistic Simulations Biophysical Journal. 108: 388a-389a. DOI: 10.1016/J.Bpj.2014.11.2129 |
0.786 |
|
2015 |
Sizemore S, Cope S, Soranno A, Vaiana S. Charge Patterning, Salt Screening and Denaturant Expansion in the CGRP Neuropeptide Biophysical Journal. 108: 229a-230a. DOI: 10.1016/J.Bpj.2014.11.1268 |
0.759 |
|
2015 |
Sizemore SM, Cope SM, Vaiana SM. Evidence for Internal Friction in IDPs of the Calcitonin Peptide Family Biophysical Journal. 108: 194a. DOI: 10.1016/J.Bpj.2014.11.1074 |
0.733 |
|
2014 |
Cope SM, Sizemore SM, Roy A, Ghirlanda G, Vaiana SM. Structure and Internal Dynamics of Calcitonin Family Peptides: Implications for Amyloid Formation Biophysical Journal. 106: 687a. DOI: 10.1016/J.Bpj.2013.11.3802 |
0.788 |
|
2014 |
Sizemore SM, Cope SM, Roy A, Ghirlanda G, Vaiana SM. Solvent Effects on the Structure and Internal Dynamics of Calcitonin Gene-Related Peptide Biophysical Journal. 106: 271a. DOI: 10.1016/J.Bpj.2013.11.1588 |
0.783 |
|
2013 |
Cope SM, Shinde S, Best RB, Ghirlanda G, Vaiana SM. Cyclic N-terminal loop of amylin forms non amyloid fibers. Biophysical Journal. 105: 1661-9. PMID 24094407 DOI: 10.1016/J.Bpj.2013.08.026 |
0.731 |
|
2013 |
Cope SM, Sizemore SM, Roy A, Ghirlanda G, Vaiana SM. Effect of Prolines on the Intrinsic Stiffness of Islet Amyloid Polypeptide Variants Biophysical Journal. 104: 57a. DOI: 10.1016/J.Bpj.2012.11.352 |
0.763 |
|
2013 |
Sizemore SM, Cope SM, Roy A, Ghirlanda G, Vaiana SM. Electrostatic Interactions Modulate the Structure and Dynamics of Calcitonin Gene-Related Peptide Biophysical Journal. 104: 54a-55a. DOI: 10.1016/J.Bpj.2012.11.342 |
0.791 |
|
2013 |
Cope SM, Shinde S, Best RB, Giovanna G, Vaiana SM. Cyclic N Terminal Fragment of Amylin Forms Non Amyloid Fibers: Implications for Intra- and Inter-Molecular Interactions in Amylin Biophysical Journal. 104: 389a-390a. DOI: 10.1016/J.Bpj.2012.11.2171 |
0.757 |
|
2012 |
Kaur P, Plochberger B, Costa P, Cope SM, Vaiana SM, Lindsay S. Hydrophobicity of methylated DNA as a possible mechanism for gene silencing. Physical Biology. 9: 065001. PMID 23196865 DOI: 10.1088/1478-3975/9/6/065001 |
0.666 |
|
2012 |
Murphy RD, Conlon J, Mansoor T, Luca S, Vaiana SM, Buchete NV. Conformational dynamics of human IAPP monomers. Biophysical Chemistry. 167: 1-7. PMID 22609945 DOI: 10.1016/J.Bpc.2012.03.010 |
0.438 |
|
2012 |
Cope SM, Shinde S, Ghirlanda G, Vaiana SM. Effect of a Single-Point Mutation on the Conformation and Dynamics of Islet Amyloid Polypeptide from Nanosecond-Resolved Intramolecular Contact Formation Biophysical Journal. 102: 632a. DOI: 10.1016/J.Bpj.2011.11.3440 |
0.775 |
|
2012 |
Sizemore SM, Cope SM, Shinde S, Ghirlanda G, Vaiana SM. Transient Tertiary Contact Formation in the CGRP Neuropeptide Revealed by Nanosecond Laser Spectroscopy Biophysical Journal. 102: 10a. DOI: 10.1016/J.Bpj.2011.11.077 |
0.792 |
|
2011 |
Tsen KT, Tsen SW, Fu Q, Lindsay SM, Li Z, Cope S, Vaiana S, Kiang JG. Studies of inactivation of encephalomyocarditis virus, M13 bacteriophage, and Salmonella typhimurium by using a visible femtosecond laser: insight into the possible inactivation mechanisms. Journal of Biomedical Optics. 16: 078003. PMID 21806295 DOI: 10.1117/1.3600771 |
0.689 |
|
2010 |
Tsen KT, Tsen SWD, Fu Q, Lindsay SM, Kibler K, Jacobs B, Wu TC, Li Z, Yan H, Cope S, Vaiana S, Kiang JG. Photonic approach to the selective inactivation of viruses with a near-infrared ultrashort pulsed laser Progress in Biomedical Optics and Imaging - Proceedings of Spie. 7561. DOI: 10.1117/12.841316 |
0.673 |
|
2009 |
Vaiana SM, Best RB, Yau WM, Eaton WA, Hofrichter J. Evidence for a partially structured state of the amylin monomer Biophysical Journal. 97: 2948-2957. PMID 19948124 DOI: 10.1016/J.Bpj.2009.08.041 |
0.521 |
|
2009 |
Vaiana SM, Best RB, Yau W, Eaton WA, Hofrichter J. Collapse Of Rat And Human Amylin From Nanosecond-resolved Intramolecular Contact Formation Biophysical Journal. 96: 319a. DOI: 10.1016/J.Bpj.2008.12.1601 |
0.557 |
|
2008 |
Vaiana SM, Ghirlando R, Yau WM, Eaton WA, Hofrichter J. Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers Biophysical Journal. 94: L45-L47. PMID 18223003 DOI: 10.1529/Biophysj.107.125146 |
0.397 |
|
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