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  Proteostasis impairment in protein-misfolding and -aggregation diseases

Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014). Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends in Cell Biology, 24(9), 506-514. doi:10.1016/j.tcb.2014.05.003.

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Proteostasis impairment Final Autors Version.pdf (Preprint), 2MB
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Proteostasis impairment Final Autors Version.pdf
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 Creators:
Hipp, Mark S.1, Author              
Park, Sae-Hun1, Author              
Hartl, F. Ulrich1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: UBIQUITIN-PROTEASOME SYSTEM; INCLUSION-BODY FORMATION; HEAT-SHOCK RESPONSE; AMYOTROPHIC-LATERAL-SCLEROSIS; MARINESCO-SJOGREN-SYNDROME; HUNTINGTONS-DISEASE; QUALITY-CONTROL; PARKINSONS-DISEASE; MUTANT HUNTINGTIN; NEURODEGENERATIVE DISEASESproteostasis; protein aggregation; protein (mis)folding; degradation; molecular chaperones; neurodegenerative disease;
 Abstract: Cells possess an extensive network of components to safeguard proteome integrity and maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines in performance, as may be the case during aging, newly synthesized proteins are no longer able to fold efficiently and metastable proteins lose their functionally active conformations, particularly under conditions of cell stress. Apart from loss-of-function effects, a critical consequence of PN deficiency is the accumulation of cytotoxic protein aggregates, which are also associated with many age-dependent neurodegenerative diseases and other medical disorders. Here we discuss recent evidence that the chronic production of aberrantly folded and aggregated proteins in these diseases is harmful by overtaxing PN capacity, setting in motion a vicious cycle of increasing proteome imbalance that eventually leads to PN collapse and cell death.

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Language(s): eng - English
 Dates: 2014-09
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000341613600002
DOI: 10.1016/j.tcb.2014.05.003
 Degree: -

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Project name : ERC Synergy Grant (ToPAG)
Grant ID : 318987
Funding program : Funding Programme 7 (FP7)
Funding organization : European Commission (EC)

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Title: Trends in Cell Biology
  Other : Trends Cell Biol.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Elsevier Current Trends
Pages: - Volume / Issue: 24 (9) Sequence Number: - Start / End Page: 506 - 514 Identifier: ISSN: 0962-8924
CoNE: https://pure.mpg.de/cone/journals/resource/954925580131