People

Summer Sivas

Tel: 805-893-2673

E-mail: ssivas@chem.ucsb.edu

Curriculum vita (2009)

Publications

• Amyloid-β Protein Oligomerization and the Importance of Tetramers and Dodecamers in the Aetiology of Alzheimer's Disease
  Summer L. Bernstein, Nicholas F. Dupuis, Noel D. Lazo, Thomas Wyttenbach, Margaret M. Condron, Gal Bitan, David B. Teplow, Joan-Emma Shea, Brandon T. Ruotolo, Carol V. Robinson, and Michael T. Bowers
  Nat. Chem. 2009, 1, 326-331
• Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization
  Megan M. Murray, Summer L. Bernstein, Vy Nyugen, Margaret M. Condron, David B. Teplow, and Michael T. Bowers
  J. Am. Chem. Soc 2009, 131, 6316-6317
• Amyloid β-Protein: Experiment and Theory on the 21-30 Fragment
  Megan M. Murray, Mary Griffin Krone, Summer L. Bernstein, Andrij Baumketner, Margaret M. Condron, Noel D. Lazo, David B. Teplow, Thomas Wyttenbach, Joan-Emma Shea, and Michael T. Bowers
  J. Phys. Chem. B 2009, 113, 6041-6046
• The Structure of Aβ42 C-Terminal Fragments Probed by a Combined Experimental and Theoretical Study
  Chun Wu, Megan M. Murray, Summer L. Bernstein, Margaret M. Condron, Gal Bitan, Joan-Emma Shea, and Michael T. Bowers
  J. Mol. Biol. 2009, 387, 492-501
• Noncovalent Protein Interactions
  Summer L. Bernstein and Michael T. Bowers
  In Protein Mass Spectrometry; Whitelegge, J. P.; Ed.; Comprehensive Analytical Chemistry
  Elsevier: Amsterdam, 2009; Vol. 52, pp 63-82
• Spermine Binding to Parkinson's Protein α-Synuclein and Its Disease-Related A30P and A53T Mutants
  Megan Grabenauer, Summer L. Bernstein, Jennifer C. Lee, Thomas Wyttenbach, Nicholas F. Dupuis, Harry B. Gray, Jay R. Winkler, and Michael T. Bowers
  J. Phys. Chem. B 2008, 112, 11147-11154
• Effects of Familial Alzheimer's Disease Mutations on the Folding Nucleation of the Amyloid β-Protein
  Mary Griffin Krone, Andrij Baumketner, Summer L. Bernstein, Thomas Wyttenbach, Noel D. Lazo, David B. Teplow, Michael T. Bowers, and Joan-Emma Shea
  J. Mol. Biol. 2008, 381, 221-228
• Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach
  D. B. Teplow, N. D. Lazo, G. Bitan, S. Bernstein, T. Wyttenbach, M. T. Bowers, A. Baumketner, J.-E. Shea, B. Urbanc, L. Cruz, J. Borreguero, and H. E. Stanley
  Acc. Chem. Res. 2006, 39, 635-645
• Towards inhibition of amyloid β-protein oligomerization
  S. M. Spring, S. L. Bernstein, N. D. Lazo, B. Urbanc, H. E. Stanley, M. T. Bowers, D. B. Teplow, and G. Bitan
  In Understanding Biology Using Peptides: Proceedings of the 19th American Peptide Symposium, San Diego, California, USA, August 5-9, 2006; S. E. Blondelle, Ed.; American Peptide Symposia
  Springer Publishing Group: Secaucus, NJ, 2006; Vol. 9, pp 515-516
• G-quadruplexes in telomeric repeats are conserved in a solvent-free environment
  E. S. Baker, S. L. Bernstein, V. Gabelica, E. De Pauw, and M. T. Bowers
  Int. J. Mass Spectrom. 2006, 253, 225-237
• Characterisation of DEFB107 by mass spectrometry: Lessons from an anti-antimicrobial defensin
  B. J. McCullough, H. Eastwood, D. J. Clark, N. C. Polfer, D. J. Campopiano, J. A Dorin, A. Maxwell, R. J. Langley, J. R.W. Govan, S. L. Bernstein, M. T. Bowers, and P. E. Barran
  Int. J. Mass Spectrom. 2006, 252, 180-188
• Structure of the 21-30 fragment of amyloid β-protein
  A. Baumketner, S. L. Bernstein, T. Wyttenbach, N. D. Lazo, D. B. Teplow, M. T. Bowers, and J.-E. Shea
  Protein Sci. 2006, 15, 1239-1247
• Amyloid β-protein monomer structure: A computational and experimental study
  A. Baumketner, S. L. Bernstein, T. Wyttenbach, G. Bitan, D. B. Teplow, M. T. Bowers, and J.-E. Shea
  Protein Sci. 2006, 15, 420-428
• Site-specific dimensions across a highly denatured protein; a single molecule study
  E. R. McCarney, J. H. Werner, S. L. Bernstein, I. Ruczinski, D. E. Makarov, P. M. Goodwin, and K. W. Plaxco
  J. Mol. Biol. 2005, 352, 672-682
• Structural characterization of G-quadruplexes in deoxyguanosine clusters using ion mobility mass spectrometry
  E. S. Baker, S. L. Bernstein, and M. T. Bowers
  J. Am. Soc. Mass Spectrom. 2005, 16, 989-997
• Amyloid β-protein: Monomer structure and early aggregation states of Aβ42 and its Pro¹⁹ alloform
  S. L. Bernstein, T. Wyttenbach, A. Baumketner, J.-E. Shea, G. Bitan, D. B. Teplow, and M. T. Bowers
  J. Am. Chem. Soc. 2005, 127, 2075-2084
• α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation
  S. L. Bernstein, D. Liu, T. Wyttenbach, M. T. Bowers, J. C. Lee, H. B. Gray, and J. R. Winkler
  J. Am. Soc. Mass Spectrom. 2004, 15, 1435-1443
• The ion mobility mass spectrometry method and its application to duplex formation of oligonucleotides and aggregation of proteins
  T. Wyttenbach, E. S. Baker, S. L. Bernstein, A. Ferzoco, J. Gidden, D. Liu, and M. T. Bowers
  In Advances in Mass Spectrometry: Proceedings of the 16th International Mass Spectrometry Conference, Edinburgh, Scotland, UK, August 31-September 5, 2003; A. E. Ashcroft, G. Brenton, and J. J. Monaghan, Eds.; Elsevier B. V.: Amsterdam, The Netherlands, 2004; Vol. 16, pp 189-200
• Origin of bonding interactions in Cu₂⁺(H₂)_n clusters: An experimental and theoretical investigation
  M. J. Manard, J. E. Bushnell, S. L. Bernstein, and M. T. Bowers
  J. Phys. Chem. A 2002, 106, 10027-10032