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Frontiers in Molecular Neuroscience logoLink to Frontiers in Molecular Neuroscience
. 2020 Jan 21;12:311. doi: 10.3389/fnmol.2019.00311

Corrigendum: Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis

Luke McAlary 1,2, Steven S Plotkin 3,4, Justin J Yerbury 1,2, Neil R Cashman 5,*
PMCID: PMC6986233  PMID: 32038158

In the original article, there was a mistake in Table 1 as published. The incorrect original research articles were referenced for some of the table cells. The corrected Table 1 appears below.

Table 1.

Evidence supporting the prion-like characteristics of ALS-associated proteins.

Protein/Gene in vitro fibril formation in vitro fibril seeding Cell seeding with in vitro protein Cell-to-cell propagation Human to cell propagation in vitro to animal propagation Animal to animal propagation Human to animal propagation
SOD1
Chattopadhyay et al. (2008)

Chia et al. (2010)

Munch et al. (2011)

Grad et al. (2014)

Pokrishevsky et al. (2017)

Ayers et al. (2016a)

Ayers et al. (2014)

Ekhtiari Bidhendi et al. (2018)
TDP-43
Johnson et al. (2009)

Furukawa et al. (2011)

Furukawa et al. (2011)

Nonaka et al. (2013)

Nonaka et al. (2013)

Porta et al. (2018)
FUS
Nomura et al. (2014)

Nomura et al. (2014)
C9orf72 (DPRs)
Westergard et al. (2016)

The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.

References

  1. Ayers J. I., Diamond J., Sari A., Fromholt S., Galaleldeen A., Ostrow L. W., et al. (2016a). Distinct conformers of transmissible misfolded SOD1 distinguish human SOD1-FALS from other forms of familial and sporadic ALS. Acta Neuropathol. 132, 827–840. 10.1007/s00401-016-1623-4 [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ayers J. I., Fromholt S., Koch M., DeBosier A., McMahon B., Xu G., et al. (2014). Experimental transmissibility of mutant SOD1 motor neuron disease. Acta Neuropathol. 128, 791–803. 10.1007/s00401-014-1342-7 [DOI] [PubMed] [Google Scholar]
  3. Chattopadhyay M., Durazo A., Sohn S. H., Strong C. D., Gralla E. B., Whitelegge J. P., et al. (2008). Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc. Natl. Acad. Sci. U S A. 105, 18663–18668. 10.1073/pnas.0807058105 [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chia R., Tattum M. H., Jones S., Collinge J., Fisher E. M. C., Jackson G. S. (2010). Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis. PLoS ONE 5:e10627. 10.1371/journal.pone.0010627 [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ekhtiari Bidhendi E., Bergh J., Zetterström P., Forsberg K., Pakkenberg B., Andersen P. M., et al. (2018). Mutant superoxide dismutase aggregates from human spinal cord transmit amyotrophic lateral sclerosis. Acta Neuropathol. 136, 939–953. 10.1007/s00401-018-1915-y [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Furukawa Y., Kaneko K., Watanabe S., Yamanaka K., Nukina N. (2011). A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions. J. Biol. Chem. 286, 18664–18672. 10.1074/jbc.M111.231209 [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Grad L. I., Yerbury J. J., Turner B. J., Guest W. C., Pokrishevsky E., O'Neill M. A., et al. (2014). Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms. Proc. Natl. Acad. Sci. U.S.A. 111, 3620–3625. 10.1073/pnas.1312245111 [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Johnson B. S., Snead D., Lee J. J., McCaffery J. M., Shorter J., Gitler A. D. (2009). TDP-43 is intrinsically aggregation-prone and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284, 20329–20339. 10.1074/jbc.M109.010264 [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Munch C., O'Brien J., Bertolotti A. (2011). Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. U.S.A. 108, 3548–3553. 10.1073/pnas.1017275108 [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Nomura T., Watanabe S., Kaneko K., Yamanaka K., Nukina N., Furukawa Y. (2014). Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis. J. Biol. Chem. 289, 1192–1202. 10.1074/jbc.M113.516492 [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Nonaka T., Masuda-Suzukake M., Arai T., Hasegawa Y., Akatsu H., Obi T., et al. (2013). Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep. 4, 124–134. 10.1016/j.celrep.2013.06.007 [DOI] [PubMed] [Google Scholar]
  12. Pokrishevsky E., Hong R. H., Mackenzie I. R., Cashman N. R. (2017). Spinal cord homogenates from SOD1 familial amyotrophic lateral sclerosis induce SOD1 aggregation in living cells. PLOS ONE 12:e0184384. 10.1371/journal.pone.0184384 [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Porta S., Xu Y., Restrepo C. R., Kwong L. K., Zhang B., Brown H. J., et al. (2018). Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo. Nat. Commun. 9:4220. 10.1038/s41467-018-06548-9 [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Westergard T., Jensen B. K, Wen X., Cai J., Kropf E., Iacovitti L., et al. (2016). Cell-to-cell transmission of dipeptide repeat proteins linked to C9orf72-ALS/FTD. Cell Rep. 17, 645–652. 10.1016/j.celrep.2016.09.032 [DOI] [PMC free article] [PubMed] [Google Scholar]

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