Her primary areas of study are Biochemistry, Endopeptidase Clp, Protease, Proteases and Cell biology. Her Biochemistry study frequently draws connections between adjacent fields such as Biophysics. Her Endopeptidase Clp research incorporates elements of Proteolysis, Denaturation, Adenosine triphosphate and Protein folding.
The Protease study combines topics in areas such as Overproduction, DNA damage, Ribosome and Intracellular. She has included themes like Protein subcellular localization prediction, Systems biology and Escherichia coli in her Proteases study. Her Cell biology research is multidisciplinary, incorporating elements of SeqA protein domain, DNA, DNA replication, DnaA and dnaB helicase.
The scientist’s investigation covers issues in Biochemistry, Biophysics, Protease, Cell biology and Endopeptidase Clp. Her is doing research in Proteolysis, Proteases, ATPase, Peptide sequence and Plasma protein binding, both of which are found in Biochemistry. Her study in Biophysics is interdisciplinary in nature, drawing from both Protein degradation, ATP hydrolysis, Substrate, Random hexamer and Unfolded protein response.
Tania A. Baker works mostly in the field of Protease, limiting it down to topics relating to Signal transducing adaptor protein and, in certain cases, Peptide. Tetramer, Stereochemistry, Molecular biology and Recombination is closely connected to Transposase in her research, which is encompassed under the umbrella topic of Cell biology. Her Endopeptidase Clp research is multidisciplinary, relying on both Protein subunit, Adenosine triphosphate, Protein folding, AAA proteins and Binding site.
Her main research concerns Biophysics, Protease, Proteases, Cell biology and Proteolysis. The study incorporates disciplines such as Protein degradation, Function, Substrate, Random hexamer and Unfolded protein response in addition to Biophysics. Her Protease study combines topics in areas such as Translocase and Escherichia coli.
Her Proteases study integrates concerns from other disciplines, such as ATP hydrolysis and Structural biology. In her study, which falls under the umbrella issue of Cell biology, Mitochondrion, In vivo, Pseudomonas aeruginosa and Bacteria is strongly linked to Active site. Her biological study focuses on Protein subunit.
Tania A. Baker focuses on Biophysics, Unfolded protein response, Protease, Random hexamer and Protein degradation. Her studies deal with areas such as Cooperativity, ATP hydrolysis, Proteases, Enzyme and Structural biology as well as Unfolded protein response. ATP hydrolysis is a subfield of Biochemistry that she tackles.
Her work deals with themes such as Function and Escherichia coli, which intersect with Protease. Her Random hexamer research integrates issues from Protein structure, Proteostasis and Protein subunit. Her Protein degradation research incorporates themes from Association dissociation, Docking, Substrate and Proteolysis.
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A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli.
M Singer;T A Baker;G Schnitzler;S M Deischel.
Microbiological Research (1989)
AAA+ proteases: ATP-fueled machines of protein destruction.
Robert T. Sauer;Tania A. Baker.
Annual Review of Biochemistry (2011)
Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals.
Julia M Flynn;Saskia B Neher;Yong In Kim;Robert T Sauer.
Molecular Cell (2003)
Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
Robert T. Sauer;Daniel N. Bolon;Briana M. Burton;Randall E. Burton.
Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines
Andreas Martin;Tania A. Baker;Robert T. Sauer.
Polymerases and the Replisome: Machines within Machines
Tania A Baker;Stephen P Bell.
ClpXP, an ATP-powered unfolding and protein-degradation machine
Tania A. Baker;Robert T. Sauer.
Biochimica et Biophysica Acta (2012)
Dynamics of Substrate Denaturation and Translocation by the ClpXP Degradation Machine
Yong-In Kim;Randall E. Burton;Briana M. Burton;Robert T. Sauer.
Molecular Cell (2000)
A specificity-enhancing factor for the ClpXP degradation machine.
Igor Levchenko;Meredith Seidel;Robert T. Sauer;Tania A. Baker.
Disassembly of the Mu transposase tetramer by the ClpX chaperone.
I. Levchenko;Li Luo;T. A. Baker.
Genes & Development (1995)
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