Publication

Heat shock proteins as potential targets for protective strategies in neurodegeneration

Kampinga, H. H. & Bergink, S., Jun-2016, In : Lancet Neurology. 15, 7, p. 748-759 12 p.

Research output: Contribution to journalReview articleAcademicpeer-review

APA

Kampinga, H. H., & Bergink, S. (2016). Heat shock proteins as potential targets for protective strategies in neurodegeneration. Lancet Neurology, 15(7), 748-759. https://doi.org/10.1016/S1474-4422(16)00099-5

Author

Kampinga, Harm H. ; Bergink, Steven. / Heat shock proteins as potential targets for protective strategies in neurodegeneration. In: Lancet Neurology. 2016 ; Vol. 15, No. 7. pp. 748-759.

Harvard

Kampinga, HH & Bergink, S 2016, 'Heat shock proteins as potential targets for protective strategies in neurodegeneration', Lancet Neurology, vol. 15, no. 7, pp. 748-759. https://doi.org/10.1016/S1474-4422(16)00099-5

Standard

Heat shock proteins as potential targets for protective strategies in neurodegeneration. / Kampinga, Harm H.; Bergink, Steven.

In: Lancet Neurology, Vol. 15, No. 7, 06.2016, p. 748-759.

Research output: Contribution to journalReview articleAcademicpeer-review

Vancouver

Kampinga HH, Bergink S. Heat shock proteins as potential targets for protective strategies in neurodegeneration. Lancet Neurology. 2016 Jun;15(7):748-759. https://doi.org/10.1016/S1474-4422(16)00099-5


BibTeX

@article{46def499b94a4f24958e76872233f632,
title = "Heat shock proteins as potential targets for protective strategies in neurodegeneration",
abstract = "Protein aggregates are hallmarks of nearly all age-related neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, and several polyglutamine diseases such as Huntington's disease and different forms of spinocerebellar ataxias (SCA; SCA1-3, SCA6, and SCA7). The collapse of cellular protein homoeostasis can be both a cause and a consequence of this protein aggregation. Boosting components of the cellular protein quality control system has been widely investigated as a strategy to counteract protein aggregates or their toxic consequences. Heat shock proteins (HSPs) play a central part in regulating protein quality control and contribute to protein aggregation and disaggregation. Therefore, HSPs are viable targets for the development of drugs aimed at reducing pathogenic protein aggregates that are thought to contribute to the development of so many neurodegenerative disorders.",
keywords = "AMYOTROPHIC-LATERAL-SCLEROSIS, SPINOCEREBELLAR ATAXIA TYPE-3, CHAPERONE-MEDIATED AUTOPHAGY, ALPHA-SYNUCLEIN, QUALITY-CONTROL, MOLECULAR CHAPERONES, HUNTINGTONS-DISEASE, POLYGLUTAMINE AGGREGATION, MISFOLDED PROTEINS, CONFORMATIONAL SWITCH",
author = "Kampinga, {Harm H.} and Steven Bergink",
note = "Copyright {\textcopyright} 2016 Elsevier Ltd. All rights reserved.",
year = "2016",
month = jun,
doi = "10.1016/S1474-4422(16)00099-5",
language = "English",
volume = "15",
pages = "748--759",
journal = "Lancet Neurology",
issn = "1474-4422",
publisher = "ELSEVIER SCIENCE INC",
number = "7",

}

RIS

TY - JOUR

T1 - Heat shock proteins as potential targets for protective strategies in neurodegeneration

AU - Kampinga, Harm H.

AU - Bergink, Steven

N1 - Copyright © 2016 Elsevier Ltd. All rights reserved.

PY - 2016/6

Y1 - 2016/6

N2 - Protein aggregates are hallmarks of nearly all age-related neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, and several polyglutamine diseases such as Huntington's disease and different forms of spinocerebellar ataxias (SCA; SCA1-3, SCA6, and SCA7). The collapse of cellular protein homoeostasis can be both a cause and a consequence of this protein aggregation. Boosting components of the cellular protein quality control system has been widely investigated as a strategy to counteract protein aggregates or their toxic consequences. Heat shock proteins (HSPs) play a central part in regulating protein quality control and contribute to protein aggregation and disaggregation. Therefore, HSPs are viable targets for the development of drugs aimed at reducing pathogenic protein aggregates that are thought to contribute to the development of so many neurodegenerative disorders.

AB - Protein aggregates are hallmarks of nearly all age-related neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, and several polyglutamine diseases such as Huntington's disease and different forms of spinocerebellar ataxias (SCA; SCA1-3, SCA6, and SCA7). The collapse of cellular protein homoeostasis can be both a cause and a consequence of this protein aggregation. Boosting components of the cellular protein quality control system has been widely investigated as a strategy to counteract protein aggregates or their toxic consequences. Heat shock proteins (HSPs) play a central part in regulating protein quality control and contribute to protein aggregation and disaggregation. Therefore, HSPs are viable targets for the development of drugs aimed at reducing pathogenic protein aggregates that are thought to contribute to the development of so many neurodegenerative disorders.

KW - AMYOTROPHIC-LATERAL-SCLEROSIS

KW - SPINOCEREBELLAR ATAXIA TYPE-3

KW - CHAPERONE-MEDIATED AUTOPHAGY

KW - ALPHA-SYNUCLEIN

KW - QUALITY-CONTROL

KW - MOLECULAR CHAPERONES

KW - HUNTINGTONS-DISEASE

KW - POLYGLUTAMINE AGGREGATION

KW - MISFOLDED PROTEINS

KW - CONFORMATIONAL SWITCH

U2 - 10.1016/S1474-4422(16)00099-5

DO - 10.1016/S1474-4422(16)00099-5

M3 - Review article

C2 - 27106072

VL - 15

SP - 748

EP - 759

JO - Lancet Neurology

JF - Lancet Neurology

SN - 1474-4422

IS - 7

ER -

ID: 31707869