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Andreas Bracher
Researcher at Max Planck Society
Publications - 102
Citations - 10577
Andreas Bracher is an academic researcher from Max Planck Society. The author has contributed to research in topics: Protein folding & Chaperone (protein). The author has an hindex of 44, co-authored 99 publications receiving 9108 citations. Previous affiliations of Andreas Bracher include European Bioinformatics Institute & Leipzig University.
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Molecular chaperones in protein folding and proteostasis
TL;DR: It is suggested that an age-related decline in proteostasis capacity allows the manifestation of various protein-aggregation diseases, including Alzheimer's disease and Parkinson's disease, which may spring from a detailed understanding of the pathways underlying proteome maintenance.
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Molecular Chaperone Functions in Protein Folding and Proteostasis
TL;DR: This review focuses on recent advances in understanding the mechanisms of chaperone action in promoting and regulating protein folding and on the pathological consequences of protein misfolding and aggregation.
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Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry
Franz Herzog,Abdullah Kahraman,Daniel Boehringer,Raymond H. Mak,Andreas Bracher,Thomas Walzthoeni,Alexander Leitner,Martin Beck,Franz-Ulrich Hartl,Nenad Ban,Lars Malmström,Ruedi Aebersold +11 more
TL;DR: This study establishes XL-MS as an integral part of hybrid structural biology approaches for the analysis of endogenous protein complexes by gaining distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying an adaptedXL-MS protocol.
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Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
TL;DR: The Hsp110 homologues significantly increase the rate and yield of Hsp70‐mediated re‐folding of thermally denatured firefly Luciferase in vitro and deletion of SSE1 causes a firefly luciferase folding defect in yeast cells under heat stress in vivo.
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The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding
TL;DR: Different models of chaperonin action are reviewed and issues of current debate are discussed, providing insights into how the physical environment of the chaper onin cage actively promotes protein folding, in addition to preventing aggregation.