Xue Fei
Affiliations: | Massachusetts Institute of Technology, Cambridge, MA, United States |
Area:
chaperones, protein folding, AAA+ proteaseGoogle:
"Xue Fei"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| George H. Lorimer | grad student | 2009-2014 | NIH & University of Maryland College Park |
| Robert T. Sauer | post-doc |
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Publications
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| Ghanbarpour A, Cohen SE, Fei X, et al. (2023) A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation. Nature Communications. 14: 7281 |
| Ghanbarpour A, Fei X, Baker TA, et al. (2023) The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery. Proceedings of the National Academy of Sciences of the United States of America. 120: e2219044120 |
| Kim S, Fei X, Sauer RT, et al. (2022) AAA+ protease-adaptor structures reveal altered conformations and ring specialization. Nature Structural & Molecular Biology. 29: 1068-1079 |
| Sauer RT, Fei X, Bell TA, et al. (2021) Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis. Critical Reviews in Biochemistry and Molecular Biology. 1-17 |
| Baytshtok V, Fei X, Shih TT, et al. (2021) Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Reports. 34: 108639 |
| Fei X, Bell TA, Barkow SR, et al. (2020) Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. Elife. 9 |
| Fei X, Bell TA, Jenni S, et al. (2020) Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate. Elife. 9 |
| Fei X, Bell TA, Jenni S, et al. (2020) Author response: Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate Elife |
| Lorimer GH, Fei X, Ye X. (2018) The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 373 |
| Roh SH, Hryc CF, Jeong HH, et al. (2017) Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM. Proceedings of the National Academy of Sciences of the United States of America |