P
Peter M. Tessier
Researcher at University of Michigan
Publications - 89
Citations - 5184
Peter M. Tessier is an academic researcher from University of Michigan. The author has contributed to research in topics: Monoclonal antibody & Protein aggregation. The author has an hindex of 37, co-authored 89 publications receiving 4422 citations. Previous affiliations of Peter M. Tessier include Massachusetts Institute of Technology & Rensselaer Polytechnic Institute.
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A class of porous metallic nanostructures
TL;DR: In this article, a new class of metallic materials with long-range nano-scale ordering and hierarchical porosity was synthesized by using colloidal crystals as templates, and they were used to fabricate structures from inorganic oxides, polymers, diamond and glassy carbon.
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Assembly of Gold Nanostructured Films Templated by Colloidal Crystals and Use in Surface-Enhanced Raman Spectroscopy
Peter M. Tessier,Orlin D. Velev,Anand T. Kalambur,John F. Rabolt,A. M. Lenhoff,Eric W. Kaler +5 more
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Resveratrol Selectively Remodels Soluble Oligomers and Fibrils of Amyloid Aβ into Off-pathway Conformers
Ali Reza A. Ladiwala,Jason C. Lin,Shyam Sundhar Bale,Anna Marie Marcelino-Cruz,Moumita Bhattacharya,Jonathan S. Dordick,Peter M. Tessier +6 more
TL;DR: Surprisingly, resveratrol does not remodel non-toxic oligomers or accelerate Aβ monomer aggregation despite that both conformers possess random coil secondary structures indistinguishable from soluble oligomers and significantly different from their β-sheet rich, fibrillar counterparts.
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Rapid Measurement of Protein Osmotic Second Virial Coefficients by Self-Interaction Chromatography
TL;DR: This work has measured protein interactions using self-interaction chromatography, in which protein is immobilized on chromatographic particles and the retention of the same protein is measured in isocratic elution, and obtains quantitative agreement between virial coefficients measured by self- INTERACTION chromatography and traditional characterization methods over a wide range of pH and ionic strengths.
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Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity
Ali Reza A. Ladiwala,Jeffrey Litt,Ravi S. Kane,Darryl Aucoin,Steven O. Smith,Swarnim Ranjan,Judianne Davis,William E. Van Nostrand,Peter M. Tessier +8 more
TL;DR: The results suggest that the ability of non-fibrillar Aβ oligomers to interact with and disrupt cellular membranes is linked to the degree of solvent exposure of their central and C-terminal hydrophobic peptide segments.