(Q50749960)

18 March 2018

title

Conversion of green fluorescent protein into a toxic, aggregation-prone protein by C-terminal addition of a short peptide. (English)

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18 March 2018

author

Brian Hiester

3

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18 March 2018

Michael A. Silverman

7

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18 March 2018

author name string

Christopher D Link

1

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18 March 2018

Virginia Fonte

2

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18 March 2018

John Yerg

4

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18 March 2018

Jmil Ferguson

5

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18 March 2018

Susan Csontos

6

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18 March 2018

Gretchen H Stein

8

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18 March 2018

language of work or name

English

0 references

publication date

19 October 2005

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18 March 2018

Journal of Biological Chemistry

published in

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18 March 2018

volume

281

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18 March 2018

page(s)

1808-1816

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18 March 2018

issue

3

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18 March 2018

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

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The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans

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Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae

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Impairment of the ubiquitin-proteasome system by protein aggregation

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Gene expression analysis in a transgenic Caenorhabditis elegans Alzheimer's disease model

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Interaction of intracellular beta amyloid peptide with chaperone proteins

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Mechanisms of Suppression of {alpha}-Synuclein Neurotoxicity by Geldanamycin in Drosophila.

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Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons.

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Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression

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Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation.

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Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation

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Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model.

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Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration

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Prefibrillar amyloid protein aggregates share common features of cytotoxicity.

21 January 2018

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

21 January 2018

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Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M505581200

1 reference

18 March 2018

PubMed ID

16239215

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18 March 2018