Peter Schuck
Affiliations: | NIBIB | National Institutes of Health, Bethesda, MD |
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| Harkness RW, Toyama Y, Ripstein ZA, et al. (2021) Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP. Proceedings of the National Academy of Sciences of the United States of America. 118 |
| Parupudi A, Chaturvedi SK, Adão R, et al. (2021) Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations. Scientific Reports. 11: 5741 |
| Schuck P. (2021) Analytical Ultracentrifugation as a Tool for Studying Protein Interactions. Biophysical Reviews. 5: 159-171 |
| Chaturvedi SK, Parupudi A, Juul-Madsen K, et al. (2020) Measuring aggregates, self-association, and weak interactions in concentrated therapeutic antibody solutions. Mabs. 12: 1810488 |
| Zhao H, Li W, Chu W, et al. (2020) Quantitative Analysis of Protein Self-Association by Sedimentation Velocity. Current Protocols in Protein Science. 101: e109 |
| Zhao H, Datta SAK, Kim SH, et al. (2019) Nucleic acid-induced dimerization of HIV-1 Gag protein. The Journal of Biological Chemistry |
| Montecinos-Franjola F, Chaturvedi SK, Schuck P, et al. (2019) All tubulins are not alike: Heterodimer dissociation differs among different biological sources. The Journal of Biological Chemistry. 294: 10315-10324 |
| Chaturvedi SK, Schuck P. (2019) A Reappraisal of Sedimentation Nonideality Coefficients for the Analysis of Weak Interactions of Therapeutic Proteins. The Aaps Journal. 21: 35 |
| Chaturvedi SK, Sagar V, Zhao H, et al. (2019) Measuring Ultra-Weak Protein Self-Association by Non-ideal Sedimentation Velocity. Journal of the American Chemical Society. 141: 2990-2996 |
| Chaturvedi SK, Ma J, Zhao H, et al. (2017) Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions. Nature Protocols. 12: 1777-1791 |