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Lee Freiburger

Researcher at Technische Universität München

Publications -  15
Citations -  644

Lee Freiburger is an academic researcher from Technische Universität München. The author has contributed to research in topics: Isothermal titration calorimetry & Cooperativity. The author has an hindex of 12, co-authored 15 publications receiving 518 citations. Previous affiliations of Lee Freiburger include McGill University & Center for Integrated Protein Science Munich.

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Journal ArticleDOI

Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein

TL;DR: Hsp90 cochaperones differentially affect formation of the Hsp90-GR complex, serving as control elements for cycle progression and revealing an intricate interplay of client and co chaperones as molecular modulators of the hsp90 machine.
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A C-terminal HSP90 inhibitor restores glucocorticoid sensitivity and relieves a mouse allograft model of Cushing disease

TL;DR: It is shown that corticotroph adenomas overexpress HSP90 compared to the normal pituitary, which suggests that the pathogenesis of Cushing disease caused by overexpression of heat shock proteins and consequently misregulated GR sensitivity may be overcome pharmacologically with an appropriate H SP90 inhibitor.
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Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme

TL;DR: An approach combining isothermal titration calorimetry, circular dichroism and nuclear magnetic resonance spectroscopy to quantify allostery in terms of protein thermodynamics, structure and dynamics was applied to study the interaction between aminoglycoside N-(6′)-acetyltransferase-Ii and one of its substrates, acetyl coenzyme A.
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Efficient segmental isotope labeling of multi-domain proteins using Sortase A

TL;DR: This work presents an optimized strategy for segmental labeling of multi-domain proteins using the S. aureus transpeptidase Sortase A to enable routine production of milligram amounts of purified segmentally labeled protein for NMR and other biophysical studies.
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Elucidating protein binding mechanisms by variable-c ITC.

TL;DR: A simple approach for discriminating between different binding mechanisms is reported, based on a global analysis of ITC data obtained over a range of sample concentrations, to the interaction between the enzyme aminoglycoside N-(6′)-acetyltransferase-Ii (AAC( 6′)-Ii) and one of its substrates, AcCoA.