(Q36887505)

16 August 2017

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title

How a cell deals with abnormal proteins. Pathogenetic mechanisms in protein aggregation diseases (English)

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16 August 2017

0 references

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Aigelsreiter A

1

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16 August 2017

Janig E

2

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16 August 2017

Stumptner C

3

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16 August 2017

Fuchsbichler A

4

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16 August 2017

Zatloukal K

5

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16 August 2017

Denk H

6

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16 August 2017

publication date

1 January 2007

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16 August 2017

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16 August 2017

volume

74

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16 August 2017

issue

3

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16 August 2017

page(s)

145-158

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Principles of protein folding, misfolding and aggregation

16 August 2017

cites work

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Protein quality control: chaperones culling corrupt conformations

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Aging and molecular chaperones

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Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state

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Proteolysis: anytime, any place, anywhere?

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Delivery of ubiquitinated substrates to protein-unfolding machines

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Protein degradation and protection against misfolded or damaged proteins

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Aggresomes: a cellular response to misfolded proteins

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Folding proteins in fatal ways

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The systemic amyloidoses

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Molecular basis of the neurodegenerative disorders

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Unfolding the role of protein misfolding in neurodegenerative diseases

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Protein aggregation and neurodegenerative disease

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Interaction of stress proteins with misfolded keratins

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Keratins turn over by ubiquitination in a phosphorylation-modulated fashion

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Signaling, polyubiquitination, trafficking, and inclusions: sequestosome 1/p62's role in neurodegenerative disease.

21 January 2018

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Toxic proteins in neurodegenerative disease

21 January 2018

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A century-old debate on protein aggregation and neurodegeneration enters the clinic

21 January 2018

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100 years and counting: prospects for defeating Alzheimer's disease

21 January 2018

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21 January 2018

Identifiers

DOI

10.1159/000103374

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16 August 2017

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