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

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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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1 January 2007

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16 August 2017

74

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3

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145-158

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Principles of protein folding, misfolding and aggregation

16 August 2017

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Protein folding and misfolding

21 January 2018

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Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?

21 January 2018

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Hassles with taking out the garbage: aggravating aggresomes.

21 January 2018

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Roles of molecular chaperones in protein misfolding diseases

21 January 2018

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Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

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Aggresomes, inclusion bodies and protein aggregation

21 January 2018

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The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review

21 January 2018

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Apoptosis, necrosis and cellular senescence: chaperone occupancy as a potential switch

21 January 2018

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Roles of molecular chaperones in protein degradation

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Protein quality control: chaperones culling corrupt conformations

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Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases

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Aging and molecular chaperones

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Molecular chaperones and the stress of oncogenesis.

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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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Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease.

21 January 2018

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Protein aggregation and the ubiquitin proteasome pathway: gaining the UPPer hand on neurodegeneration

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Getting in and out of the proteasome

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Proteolysis: anytime, any place, anywhere?

21 January 2018

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Delivery of ubiquitinated substrates to protein-unfolding machines

21 January 2018

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Protein degradation and protection against misfolded or damaged proteins

21 January 2018

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Aggresomes: a cellular response to misfolded proteins

21 January 2018

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Cytoplasmic dynein/dynactin mediates the assembly of aggresomes

21 January 2018

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From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

21 January 2018

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Molecular mechanisms of amyloidosis

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Molecular recycling within amyloid fibrils

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Folding proteins in fatal ways

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The systemic amyloidoses

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The pathology of dialysis.

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Amyotrophic lateral sclerosis

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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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Relationship between multifunctional protein "clusterin" and Alzheimer disease

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Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases

21 January 2018

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Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation.

21 January 2018

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p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases

21 January 2018

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Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions.

21 January 2018

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Genetic prion disease: the EUROCJD experience.

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Recent advances in prion biology

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Practical genetics: alpha-1-antitrypsin deficiency and the serpinopathies

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Alpha(1)-antitrypsin deficiency, liver disease and emphysema

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Alcoholic and nonalcoholic steatohepatitis. Histopathologic and pathogenetic considerations

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Pathology of steatohepatitis

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Mallory body--a disease-associated type of sequestosome

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Lessons from keratin 18 knockout mice: formation of novel keratin filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates

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Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies

21 January 2018

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21 January 2018

Mallory bodies revisited

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Keratin 8 mutations in patients with cryptogenic liver disease

21 January 2018

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Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies.

21 January 2018

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Keratins turn over by ubiquitination in a phosphorylation-modulated fashion

21 January 2018

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The proteasome inhibitor, PS-341, causes cytokeratin aggresome formation

21 January 2018

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Insulin-like growth factor-1-mediated neuroprotection against oxidative stress is associated with activation of nuclear factor kappaB.

21 January 2018

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Roles of nuclear factor kappaB in neuronal survival and plasticity

21 January 2018

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Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation

21 January 2018

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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

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

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

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21 January 2018

Identifiers

DOI

10.1159/000103374

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16 August 2017

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