Smita P. Soni, Ph.D.
Affiliations: | 2010 | Physics | Purdue University, West Lafayette, IN, United States |
Area:
General BiophysicsGoogle:
"Smita Soni"Mean distance: (not calculated yet)
Parents
Sign in to add mentorStephen R. Wassall | grad student | 2010 | Purdue | |
(The effect of acyl chain unsaturation on phospholipid bilayer.) | ||||
Robert V. Stahelin | post-doc | 2010-2015 | Indiana University School of Medicine-South Bend (Chemistry Tree) |
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Publications
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Adu-Gyamfi E, Johnson KA, Fraser ME, et al. (2015) Host Cell Plasma Membrane Phosphatidylserine Regulates the Assembly and Budding of Ebola Virus. Journal of Virology. 89: 9440-53 |
Adu-Gyamfi E, Soni SP, Jee CS, et al. (2014) A loop region in the N-terminal domain of Ebola virus VP40 is important in viral assembly, budding, and egress. Viruses. 6: 3837-54 |
Soni SP, Stahelin RV. (2014) The Ebola virus matrix protein VP40 selectively induces vesiculation from phosphatidylserine-enriched membranes. The Journal of Biological Chemistry. 289: 33590-7 |
Soni SP, Stahelin RV. (2014) The Ebola Virus Matrix Protein Bends Biological Membranes Biophysical Journal. 106: 513a |
Soni SP, Adu-Gyamfi E, Yong SS, et al. (2013) The Ebola virus matrix protein deeply penetrates the plasma membrane: an important step in viral egress. Biophysical Journal. 104: 1940-9 |
Adu-Gyamfi E, Soni SP, Xue Y, et al. (2013) The Ebola virus matrix protein penetrates into the plasma membrane: a key step in viral protein 40 (VP40) oligomerization and viral egress. The Journal of Biological Chemistry. 288: 5779-89 |
Soni SP, Adu-Gyamfi E, Stahelin RV, et al. (2013) Membrane Penetrating Ability of Ebola Matrix Protein, VP40 Biophysical Journal. 104: 595a |
Adu-Gyamfi E, Soni SP, Stahelin RV. (2013) Elucidating the Mechanism of Ebola Virus Assembly and Budding Biophysical Journal. 104: 416a |
Soni SP, Ward JA, Sen SE, et al. (2009) Effect of trans unsaturation on molecular organization in a phospholipid membrane. Biochemistry. 48: 11097-107 |
Shaikh SR, Locascio DS, Soni SP, et al. (2009) Oleic- and docosahexaenoic acid-containing phosphatidylethanolamines differentially phase separate from sphingomyelin. Biochimica Et Biophysica Acta. 1788: 2421-6 |