Daniel A. Kraut, Ph.D.
Affiliations: | 2006 | Stanford University, Palo Alto, CA |
Area:
ribozymesGoogle:
"Daniel Kraut"Mean distance: 8.67 | S | N | B | C | P |
Parents
Sign in to add mentor| Daniel Herschlag | grad student | 2006 | Stanford | |
| (Testing the role of transition state complementarity and the enzyme environment in ketosteroid isomerase.) | ||||
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Publications
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| Bragança CE, Kraut DA. (2020) Mode of Targeting to the Proteasome Determines GFP Fate. Journal of Biological Chemistry |
| Cundiff MD, Hurley CM, Wong JD, et al. (2019) Ubiquitin receptors are required for substrate-mediated activation of the proteasome's unfolding ability. Scientific Reports. 9: 14506 |
| Reichard EL, Chirico GG, Dewey WJ, et al. (2016) Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome. The Journal of Biological Chemistry |
| Nassif ND, Cambray SE, Kraut DA. (2014) Slipping up: partial substrate degradation by ATP-dependent proteases. Iubmb Life. 66: 309-17 |
| Kraut DA. (2013) Slippery substrates impair ATP-dependent protease function by slowing unfolding. The Journal of Biological Chemistry. 288: 34729-35 |
| Kraut DA, Israeli E, Schrader EK, et al. (2012) Sequence- and species-dependence of proteasomal processivity. Acs Chemical Biology. 7: 1444-53 |
| Kraut DA, Matouschek A. (2011) Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization. Acs Chemical Biology. 6: 1087-95 |
| Kraut DA, Sigala PA, Fenn TD, et al. (2010) Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole. Proceedings of the National Academy of Sciences of the United States of America. 107: 1960-5 |
| Schwans JP, Kraut DA, Herschlag D. (2009) Determining the catalytic role of remote substrate binding interactions in ketosteroid isomerase. Proceedings of the National Academy of Sciences of the United States of America. 106: 14271-5 |
| Koodathingal P, Jaffe NE, Kraut DA, et al. (2009) ATP-dependent proteases differ substantially in their ability to unfold globular proteins. The Journal of Biological Chemistry. 284: 18674-84 |