Jason R. Greenwald, Ph.D.
Affiliations: | 2000 | University of California, San Diego, La Jolla, CA |
Area:
Structure, function, dynamics and thermodynamics of protein-protein interactions: NMR, mass spectrometry and kineticsGoogle:
"Jason Greenwald"Mean distance: 8.6 | S | N | B | C | P |
Parents
Sign in to add mentorElizabeth A. Komives | grad student | 2000 | UCSD | |
(Crystallographic analyses as a means to study the structure, stability and function of proteins.) |
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Publications
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Bomba R, Rout SK, Bütikofer M, et al. (2019) Carbonyl Sulfide as a Prebiotic Activation Agent for Stereo- and Sequence-Selective, Amyloid-Templated Peptide Elongation. Origins of Life and Evolution of the Biosphere : the Journal of the International Society For the Study of the Origin of Life. 49: 213-224 |
Bomba R, Kwiatkowski W, Sánchez-Ferrer A, et al. (2018) Cooperative Induction of Ordered Peptide and Fatty Acid Aggregates. Biophysical Journal. 115: 2336-2347 |
Greenwald J, Kwiatkowski W, Riek R. (2018) Peptide Amyloids in the Origin of Life. Journal of Molecular Biology. 430: 3735-3750 |
Rout SK, Friedmann MP, Riek R, et al. (2018) A prebiotic template-directed peptide synthesis based on amyloids. Nature Communications. 9: 234 |
Greenwald J, Friedmann MP, Riek R. (2016) Amyloid Aggregates Arise from Amino Acid Condensations under Prebiotic Conditions. Angewandte Chemie (International Ed. in English) |
Friedmann MP, Torbeev V, Zelenay V, et al. (2015) Towards Prebiotic Catalytic Amyloids Using High Throughput Screening. Plos One. 10: e0143948 |
Seuring C, Greenwald J, Wasmer C, et al. (2012) The mechanism of toxicity in HET-S/HET-s prion incompatibility. Plos Biology. 10: e1001451 |
Greenwald J, Riek R. (2012) On the possible amyloid origin of protein folds. Journal of Molecular Biology. 421: 417-26 |
Greenwald J, Riek R. (2010) Biology of amyloid: structure, function, and regulation. Structure (London, England : 1993). 18: 1244-60 |
Greenwald J, Buhtz C, Ritter C, et al. (2010) The mechanism of prion inhibition by HET-S. Molecular Cell. 38: 889-99 |