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The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms

Grad, Leslie I., Yerbury, Justin J., Turner, Bradley J., Guest, William C., Pokrishevsky, Edward, O’Neill, Megan A., Yanai, Anat, Silverman, Judith M., Zeineddine, Rafaa, Corcoran, Lisa, Kumita, Janet R., Luheshi, Leila M., Yousefi, Masoud, Coleman, Bradley M., Hill, Andrew F., Plotkin, Steven S., Mackenzie, Ian R., Cashman, Neil R.·2014·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1312245111
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Abstract

Significance: Amyotrophic lateral sclerosis (ALS), an incurable motor neuron disease, is associated with mutation and misfolding of the Cu/Zn superoxide dismutase (SOD1) protein. Prior studies found that mutant misfolded SOD1 can convert wild-type (WT) SOD1 to a misfolded form inside living cells in a prion-like fashion. We now report that misfolded WT SOD1 can be transmitted from cell to cell, and that propagated protein misfolding can be perpetuated. Misfolded SOD1 transmission between cells can be mediated through release and uptake of protein aggregates or via small membrane-bounded transport vesicles called exosomes. These mechanisms may help explain why sporadic ALS, without a known genetic cause, can spread systematically from region to region in a progressive manner.

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Research works printed but not linked: 29

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Metadata

Authors
Grad, L. I., Yerbury, J. J., Turner, B. J., Guest, W. C., Pokrishevsky, E., O’Neill, M. A., Yanai, A., Silverman, J. M., Zeineddine, R., Corcoran, L., Kumita, J. R., Luheshi, L. M., Yousefi, M., Coleman, B. M., Hill, A. F., Plotkin, S. S., Mackenzie, I. R., & Cashman, N. R.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2014-02-18
Volume
111
Issue
9
Pages
3620-3625
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.1312245111
Cited by
414
References
5
Language
en

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