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Stefan Walter
Researcher at Technische Universität München
Publications - 24
Citations - 2331
Stefan Walter 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 18, co-authored 22 publications receiving 2232 citations. Previous affiliations of Stefan Walter include University of Michigan.
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Journal ArticleDOI
Protein-modified nanocrystalline diamond thin films for biosensor applications
Andreas Härtl,Evelyn Schmich,Jose A. Garrido,Jorge Hernando,Silvia Catharino,Stefan Walter,Peter Feulner,Alexander Kromka,Doris Steinmüller,Martin Stutzmann +9 more
TL;DR: It is shown that proteins can be attached covalently to nanocrystalline diamond thin films, and, although the biomolecules are immobilized at the surface, they are still fully functional and active.
Journal ArticleDOI
Molecular chaperones--cellular machines for protein folding.
Stefan Walter,Johannes Buchner +1 more
TL;DR: This review discusses the principal features of this peculiar class of proteins, their structure-function relationships, and the underlying molecular mechanisms that allow the functional state of proteins to be maintained under conditions in which they would normally unfold and aggregate.
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Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104.
TL;DR: It is shown that recovery of proteins from aggregates in the cell requires the chaperones to work together with defined but overlapping functions, and the results are consistent with a model of several interrelated defense lines against protein aggregation.
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The molecular chaperone Hsp104--a molecular machine for protein disaggregation.
TL;DR: Hsp104 is an ATP dependent molecular machine that-in cooperation with Hsp70 and Hsp40-extracts polypeptide chains from protein aggregates and facilitates their refolding, although the molecular details of this process are still poorly understood.
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The Co-chaperone Sba1 Connects the ATPase Reaction of Hsp90 to the Progression of the Chaperone Cycle
TL;DR: A model is proposed that correlates the ordered assembly of the Hsp90 co-chaperones with distinct steps of the ATP hydrolysis reaction during the chaperone cycle.