T
Tania A. Baker
Researcher at Massachusetts Institute of Technology
Publications - 211
Citations - 18438
Tania A. Baker is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Protein degradation & ATP hydrolysis. The author has an hindex of 71, co-authored 205 publications receiving 17125 citations. Previous affiliations of Tania A. Baker include Stanford University & Howard Hughes Medical Institute.
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Journal ArticleDOI
A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli.
Mitchell Singer,Tania A. Baker,G Schnitzler,S M Deischel,M Goel,W Dove,K J Jaacks,Alan D. Grossman,James W. Erickson,Carol A. Gross +9 more
TL;DR: A collection of 182 isogenic strains containing genetically linked antibiotic resistance elements located at approximately 1-min intervals around the Escherichia coli chromosome, designed to be used in a rapid two-step mapping system in E. coli.
Journal ArticleDOI
AAA+ proteases: ATP-fueled machines of protein destruction.
Robert T. Sauer,Tania A. Baker +1 more
TL;DR: The current understanding of the molecular mechanisms of substrate recognition, adaptor function, and ATP-fueled unfolding and translocation are reviewed.
Journal ArticleDOI
Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals.
TL;DR: These results represent a description of general rules governing substrate recognition by a AAA+ family ATPase and suggest strategies for regulation of protein degradation.
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Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
Robert T. Sauer,Daniel N. Bolon,Briana M. Burton,Randall E. Burton,Julia M. Flynn,Robert A. Grant,Greg L. Hersch,Shilpa A. Joshi,Jon A. Kenniston,Igor Levchenko,Saskia B. Neher,Elizabeth S.C. Oakes,Samia M. Siddiqui,David A. Wah,Tania A. Baker +14 more
TL;DR: Exciting progress has been made in understanding how AAA(+) machines recognize specific proteins as targets and then carry out ATP-dependent dismantling of the tertiary and/or quaternary structure of these molecules during the processes of protein degradation and the disassembly of macromolecular complexes.
Journal ArticleDOI
Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines
TL;DR: It is shown that diverse geometric arrangements can support the enzymatic unfolding of protein substrates and translocation of the denatured polypeptide into the ClpP peptidase for degradation by covalently linking active and inactive subunits of the ATPase ClpX to form hexamers.