| Year |
Citation |
Score |
| 2023 |
Ghanbarpour A, Cohen SE, Fei X, Kinman LF, Bell TA, Zhang JJ, Baker TA, Davis JH, Sauer RT. A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation. Nature Communications. 14: 7281. PMID 37949857 DOI: 10.1038/s41467-023-43145-x |
0.626 |
|
| 2023 |
Ghanbarpour A, Fei X, Baker TA, Davis JH, Sauer RT. 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. PMID 36730206 DOI: 10.1073/pnas.2219044120 |
0.647 |
|
| 2022 |
Kim S, Fei X, Sauer RT, Baker TA. AAA+ protease-adaptor structures reveal altered conformations and ring specialization. Nature Structural & Molecular Biology. 29: 1068-1079. PMID 36329286 DOI: 10.1038/s41594-022-00850-3 |
0.639 |
|
| 2021 |
Sauer RT, Fei X, Bell TA, Baker TA. Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis. Critical Reviews in Biochemistry and Molecular Biology. 1-17. PMID 34923891 DOI: 10.1080/10409238.2021.1979461 |
0.6 |
|
| 2021 |
Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT. Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Reports. 34: 108639. PMID 33472065 DOI: 10.1016/j.celrep.2020.108639 |
0.583 |
|
| 2020 |
Fei X, Bell TA, Barkow SR, Baker TA, Sauer RT. Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. Elife. 9. PMID 33089779 DOI: 10.7554/eLife.61496 |
0.69 |
|
| 2020 |
Fei X, Bell TA, Jenni S, Stinson BM, Baker TA, Harrison SC, Sauer RT. Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate. Elife. 9. PMID 32108573 DOI: 10.7554/Elife.52774 |
0.71 |
|
| 2020 |
Fei X, Bell TA, Jenni S, Stinson BM, Baker TA, Harrison SC, Sauer RT. Author response: Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate Elife. DOI: 10.7554/Elife.52774.Sa2 |
0.613 |
|
| 2018 |
Lorimer GH, Fei X, Ye X. 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. PMID 29735733 DOI: 10.1098/rstb.2017.0179 |
0.588 |
|
| 2017 |
Roh SH, Hryc CF, Jeong HH, Fei X, Jakana J, Lorimer GH, Chiu W. Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM. Proceedings of the National Academy of Sciences of the United States of America. PMID 28710336 DOI: 10.1073/Pnas.1704725114 |
0.619 |
|
| 2016 |
Baytshtok V, Fei X, Grant RA, Baker TA, Sauer RT. A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure (London, England : 1993). PMID 27667691 DOI: 10.1016/J.Str.2016.08.012 |
0.658 |
|
| 2014 |
Fei X, Ye X, LaRonde NA, Lorimer GH. Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form Proceedings of the National Academy of Sciences of the United States of America. 111: 12775-12780. PMID 25136110 DOI: 10.1073/Pnas.1412922111 |
0.626 |
|
| 2013 |
Fei X, Yang D, LaRonde-LeBlanc N, Lorimer GH. Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution Proceedings of the National Academy of Sciences of the United States of America. 110: E2958-E2966. PMID 23861496 DOI: 10.1073/Pnas.1311996110 |
0.687 |
|
| 2009 |
He YX, Huang L, Xue Y, Fei X, Teng YB, Rubin-Pitel SB, Zhao H, Zhou CZ. Crystal structure and computational analyses provide insights into the catalytic mechanism of 2,4-diacetylphloroglucinol hydrolase PhlG from Pseudomonas fluorescens. The Journal of Biological Chemistry. 285: 4603-11. PMID 20018877 DOI: 10.1074/Jbc.M109.044180 |
0.383 |
|
| Show low-probability matches. |