J
Johannes Buchner
Researcher at Technische Universität München
Publications - 393
Citations - 38541
Johannes Buchner is an academic researcher from Technische Universität München. The author has contributed to research in topics: Chaperone (protein) & Protein folding. The author has an hindex of 99, co-authored 360 publications receiving 34381 citations. Previous affiliations of Johannes Buchner include University of Regensburg & University of Freiburg.
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The Heat Shock Response: Life on the Verge of Death
TL;DR: This Review summarizes the concepts of the protective Hsp network, and the most conserved Hsps are molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures.
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Small heat shock proteins are molecular chaperones
TL;DR: It is shown that all sHsps investigated act as molecular chaperones in these folding reactions and at stoichiometric amounts they maximally prevent the aggregation of citrate synthase and alpha-glucosidase under heat shock conditions and stabilize the proteins.
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X-ray spectral modelling of the AGN obscuring region in the CDFS: Bayesian model selection and catalogue
Johannes Buchner,Antonis Georgakakis,Kirpal Nandra,Li-Ting Hsu,Cyprian Rangel,Murray Brightman,Andrea Merloni,Mara Salvato,Jennifer L. Donley,Dale D. Kocevski +9 more
TL;DR: In this article, a Bayesian framework was developed for model comparison and parameter estimation of X-ray spectra of active galactic nuclei (AGN) in the 4 Ms Chandra Deep Field South.
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The HSP90 chaperone machinery
TL;DR: Owing to the importance of HSP90 in the regulation of many cellular proteins, it has become a promising drug target for the treatment of several diseases, which include cancer and diseases associated with protein misfolding.
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Some like it hot: the structure and function of small heat-shock proteins
TL;DR: Small heat-shock proteins are a widespread and diverse class of molecular chaperones that maintain protein homeostasis by binding proteins in non-native conformations, thereby preventing substrate aggregation.