Tania A. Baker
Affiliations: | Biology | Massachusetts Institute of Technology, Cambridge, MA, United States |
Area:
macromolecular machinesWebsite:
https://biology.mit.edu/people/tania_bakerGoogle:
"Tania A. Baker"Bio:
http://www.nasonline.org/member-directory/members/20014916.html
http://web.mit.edu/bakerlab/
http://searchworks.stanford.edu/view/5574118
Cross-listing: Chemistry Tree
Parents
Sign in to add mentor| Arthur Kornberg | grad student | 1988 | Stanford | |
| (Early events during initiation of DNA replication from the E. coli chromosomal origin) | ||||
| Kiyoshi Mizuuchi | post-doc | NIH | ||
Children
Sign in to add trainee| Briana Burton | grad student | MIT | |
| Hema Chandra Kotamarthi | post-doc | 2014-2020 | MIT (Chemistry Tree) |
BETA: Related publications
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Publications
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| 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 |
| Zuromski KL, Kim S, Sauer RT, et al. (2021) Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease. The Journal of Biological Chemistry. 101407 |
| 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 |
| Kim S, Zuromski KL, Bell TA, et al. (2020) ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP. Elife. 9 |
| Mawla GD, Hall BM, Cárcamo-Oyarce G, et al. (2020) ClpP1P2 peptidase activity promotes biofilm formation in P. aeruginosa. Molecular Microbiology |
| Saunders RA, Stinson BM, Baker TA, et al. (2020) Multistep substrate binding and engagement by the AAA+ ClpXP protease. Proceedings of the National Academy of Sciences of the United States of America |
| Fei X, Bell TA, Barkow SR, et al. (2020) Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. Elife. 9 |
| Zuromski KL, Sauer RT, Baker TA. (2020) Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease. Proceedings of the National Academy of Sciences of the United States of America |
| Torres-Delgado A, Kotamarthi HC, Sauer RT, et al. (2020) The intrinsically disordered N-terminal extension of the ClpS adaptor reprograms its partner AAA+ ClpAP protease. Journal of Molecular Biology |
| Fei X, Bell TA, Jenni S, et al. (2020) Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate. Elife. 9 |