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• W2945757762 abstract "Members of the HSP40/DNAJ family comprise one of the largest groups of molecular chaperones, and are present in all living organisms from bacteria to humans. The hallmark of DNAJs is the presence of a J-domain, which is crucial for interaction with HSP70. DNAJs can be seen as the workforce that steers HSP70 machines, regulating client input and specificity. The different DNAJs are involved in processes such as (re)folding, intracellular transport across membranes, protein modifications, remodelling of protein complexes and protein degradation. In particular, different DNAJs are able to suppress aggregate formation of several amyloidogenic proteins linked to human diseases. On the other hand, mutations in many DNAJs give rise to a wide range of pathologies, attesting to their fundamental role in cellular homeostasis and general protein quality control. Key Concepts Chaperome is the interconnected network of chaperones and cochaperones that works cooperatively to maintain protein homeostasis (Brehme and Voisine, 2016). Molecular chaperone is a protein that assists folding, refolding, disaggregation and/or assembly of macromolecular complexes, but is not a permanent component of the final, native, functional structure. Chaperones can act as substrate ‘foldases’ in an ATP-dependent manner or as ‘holdases’ in an ATP-independent manner. Folding is the formation of an energetically stable three-dimensional conformation specific to a given protein sequence, also known as the native, functional conformation. On the other hand, misfolding happens when the protein does not reach its native conformation on a biologically relevant timescale. Amyloidogenic proteins are proteins with a high tendency of folding into energetically favourable aggregates, which catalyse the formation of protein fibrils and plaques, and are associated to cellular toxicity and degeneration. Protein disaggregation is the disentangling of protein aggregates through their resolubilization by chaperones, followed by their refolding or degradation." @default.
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• W2945757762 date "2018-05-17" @default.
• W2945757762 modified "2023-10-01" @default.
• W2945757762 title "HSP40/DNAJ Chaperones" @default.
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• W2945757762 doi "https://doi.org/10.1002/9780470015902.a0027633" @default.
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