Daniel Echelman - Publications
Affiliations: | 2013-2017 | Department of Biological Sc | Columbia University, New York, NY |
Year | Citation | Score | |||
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2021 | Eckels EC, Chaudhuri D, Chakraborty S, Echelman DJ, Haldar S. DsbA is a redox-switchable mechanical chaperone. Chemical Science. 12: 11109-11120. PMID 34522308 DOI: 10.1039/d1sc03048e | 0.743 | |||
2020 | Alonso-Caballero A, Echelman DJ, Tapia-Rojo R, Haldar S, Eckels EC, Fernandez JM. Protein folding modulates the chemical reactivity of a Gram-positive adhesin. Nature Chemistry. PMID 33257887 DOI: 10.1038/s41557-020-00586-x | 0.606 | |||
2017 | Valle Orero J, Rivas-Pardo JA, Tapia-Rojo R, Popa I, Echelman DJ, Haldar S, Fernandez JM. Mechanical deformation accelerates protein ageing. Angewandte Chemie (International Ed. in English). PMID 28470663 DOI: 10.1002/Anie.201703630 | 0.695 | |||
2017 | Echelman DJ, Lee AQ, Fernández JM. Mechanical forces regulate the reactivity of a thioester bond in a bacterial adhesin. The Journal of Biological Chemistry. PMID 28348083 DOI: 10.1074/jbc.M117.777466 | 0.689 | |||
2016 | Popa I, Rivas-Pardo JA, Eckels EC, Echelman D, Valle-Orero J, Fernandez JM. A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics. Journal of the American Chemical Society. PMID 27409974 DOI: 10.1021/Jacs.6B05429 | 0.683 | |||
2016 | Echelman DJ, Alegre-Cebollada J, Badilla CL, Chang C, Ton-That H, Fernández JM. CnaA domains in bacterial pili are efficient dissipaters of large mechanical shocks. Proceedings of the National Academy of Sciences of the United States of America. PMID 26884173 DOI: 10.1073/Pnas.1522946113 | 0.782 | |||
2016 | Echelman D, Fernandez J. Force Spectroscopy of a Bacterial Adhesin with an Internal Thioester Bond Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.2508 | 0.7 | |||
2014 | Echelman D, Alegre-Cebollada J, Squyres G, Fernandez C, Chang C, Ton-That H, Fernandez J. Surviving a Bumpy Ride in the Oropharynx: Bacterial Pili as Nano-Seatbelts that Dissipate Mechanical Energy Biophysical Journal. 106: 578a. DOI: 10.1016/J.Bpj.2013.11.3205 | 0.782 | |||
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