Tania A. Baker

Affiliations: 
Biology Massachusetts Institute of Technology, Cambridge, MA, United States 
Area:
macromolecular machines
Website:
https://biology.mit.edu/people/tania_baker
Google:
"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

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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

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Briana Burton grad student MIT
Hema Chandra Kotamarthi post-doc 2014-2020 MIT (Chemistry Tree)
BETA: Related publications

Publications

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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
Bilyk B, Kim S, Fazal A, et al. (2020) Regulation of Antimycin Biosynthesis Is Controlled by the ClpXP Protease. Msphere. 5
Fei X, Bell TA, Jenni S, et al. (2020) Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate. Elife. 9
Kotamarthi HC, Sauer RT, Baker TA. (2020) The Non-dominant AAA+ Ring in the ClpAP Protease Functions as an Anti-stalling Motor to Accelerate Protein Unfolding and Translocation. Cell Reports. 30: 2644-2654.e3
Kardon JR, Moroco JA, Engen JR, et al. (2020) Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding. Elife. 9
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