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
Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine
TL;DR: The experiments demonstrate the capacity of ClpXP and ClpX to perform mechanical work under load, reveal very fast and highly cooperative unfolding of individual substrate domains, suggest a translocation step size of 5-8 amino acids, and support a power-stroke model of denaturation.
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ATP-dependent proteases of bacteria: recognition logic and operating principles.
Tania A. Baker,Robert T. Sauer +1 more
TL;DR: Proteomic approaches have identified numerous substrates for some bacterial enzymes and the sequence motifs responsible for recognition, and recent biochemical dissection of the ATPase cycle and its coupling to protein unfolding has revealed fundamental operating principles.
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Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding.
TL;DR: A tyrosine residue in a pore loop of the hexameric ClpX unfoldase links ATP hydrolysis to mechanical work by gripping substrates during unfolding and translocation, supporting a model in which nucleotide-dependent conformational changes in these pore loops drive substrate translocation and unfolding.
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Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase.
Yong-In Kim,Igor Levchenko,Igor Levchenko,Karolina Fraczkowska,Rachel V. Woodruff,Robert T. Sauer,Tania A. Baker,Tania A. Baker +7 more
TL;DR: A tripeptide 'IGF' in E. coli ClpX that is essential for ClpP recognition is identified and mapping of the IGF loop onto a homolog of known structure suggests a model forClpX–ClpP docking.
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Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.
TL;DR: The structural and mechanistic features of AAA+ proteases and remodelling machines are discussed, focusing on the bacterial ClpXP and ClpX as paradigms, and the potential of these enzymes as antibacterial targets is considered and future challenges for the field are outlined.