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@ARTICLE{Groh:139668,
      author       = {Groh, Nicole and Gallotta, Ivan and Lechler, Marie C and
                      Huang, Chaolie and Jung, Raimund and David, Della C},
      title        = {{M}ethods to {S}tudy {C}hanges in {I}nherent {P}rotein
                      {A}ggregation with {A}ge in {C}aenorhabditis elegans.},
      journal      = {JoVE journal},
      volume       = {Biology},
      number       = {129},
      issn         = {1940-087X},
      address      = {New Delhi},
      publisher    = {JoVE124831},
      reportid     = {DZNE-2020-05990},
      pages        = {56464},
      year         = {2017},
      abstract     = {In the last decades, the prevalence of neurodegenerative
                      disorders, such as Alzheimer's disease (AD) and Parkinson's
                      disease (PD), has grown. These age-associated disorders are
                      characterized by the appearance of protein aggregates with
                      fibrillary structure in the brains of these patients.
                      Exactly why normally soluble proteins undergo an aggregation
                      process remains poorly understood. The discovery that
                      protein aggregation is not limited to disease processes and
                      instead part of the normal aging process enables the study
                      of the molecular and cellular mechanisms that regulate
                      protein aggregation, without using ectopically expressed
                      human disease-associated proteins. Here we describe
                      methodologies to examine inherent protein aggregation in
                      Caenorhabditis elegans through complementary approaches.
                      First, we examine how to grow large numbers of
                      age-synchronized C. elegans to obtain aged animals and we
                      present the biochemical procedures to isolate
                      highly-insoluble-large aggregates. In combination with a
                      targeted genetic knockdown, it is possible to dissect the
                      role of a gene of interest in promoting or preventing
                      age-dependent protein aggregation by using either a
                      comprehensive analysis with quantitative mass spectrometry
                      or a candidate-based analysis with antibodies. These
                      findings are then confirmed by in vivo analysis with
                      transgenic animals expressing fluorescent-tagged
                      aggregation-prone proteins. These methods should help
                      clarify why certain proteins are prone to aggregate with age
                      and ultimately how to keep these proteins fully functional.},
      keywords     = {Age Factors / Animals / Animals, Genetically Modified /
                      Caenorhabditis elegans: chemistry / Caenorhabditis elegans:
                      genetics / Caenorhabditis elegans: metabolism /
                      Caenorhabditis elegans Proteins: chemistry / Caenorhabditis
                      elegans Proteins: genetics / Caenorhabditis elegans
                      Proteins: metabolism / Models, Animal / Protein Aggregates /
                      Recombinant Proteins: chemistry / Recombinant Proteins:
                      genetics / Recombinant Proteins: metabolism / Caenorhabditis
                      elegans Proteins (NLM Chemicals) / Protein Aggregates (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals)},
      cin          = {AG David},
      ddc          = {570},
      cid          = {I:(DE-2719)1210004},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29286457},
      pmc          = {pmc:PMC5755480},
      doi          = {10.3791/56464},
      url          = {https://pub.dzne.de/record/139668},
}