Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)

doi:10.1073/pnas.1705091114

Title: Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)

Authors:: Sangwan, Smriti; Zhao, Anni; Adams, Katrina L.; Jayson, Christina K.; Sawaya, Michael R.; Guenther, Elizabeth L.; Pan, Albert C.; Ngo, Jennifer; Moore, Destaye M.; Soriaga, Angela B.; Do, Thanh D.; Goldschmidt, Lukasz; Nelson, Rebecca; Bowers, Michael T.; Koehler, Carla M.; Shaw, David E.; Novitch, Bennett G.; Eisenberg, David S.

Publication Date:: 2017-07-31

Research Org.:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Org.:: DOE - BASIC ENERGY SCIENCESNIHHHMI

OSTI Identifier:: 1390865

Resource Type:: Journal Article

Journal Name:: Proceedings of the National Academy of Sciences of the United States of America

Additional Journal Information:: Journal Volume: 114; Journal Issue: 33; Journal ID: ISSN 0027-8424

Publisher:: National Academy of Sciences, Washington, DC (United States)

Country of Publication:: United States

Language:: ENGLISH

Citation Formats


                    Sangwan, Smriti, Zhao, Anni, Adams, Katrina L., Jayson, Christina K., Sawaya, Michael R., Guenther, Elizabeth L., Pan, Albert C., Ngo, Jennifer, Moore, Destaye M., Soriaga, Angela B., Do, Thanh D., Goldschmidt, Lukasz, Nelson, Rebecca, Bowers, Michael T., Koehler, Carla M., Shaw, David E., Novitch, Bennett G., and Eisenberg, David S. Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS).  United States: N. p., 2017. 
        Web.  doi:10.1073/pnas.1705091114.

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                    Sangwan, Smriti, Zhao, Anni, Adams, Katrina L., Jayson, Christina K., Sawaya, Michael R., Guenther, Elizabeth L., Pan, Albert C., Ngo, Jennifer, Moore, Destaye M., Soriaga, Angela B., Do, Thanh D., Goldschmidt, Lukasz, Nelson, Rebecca, Bowers, Michael T., Koehler, Carla M., Shaw, David E., Novitch, Bennett G., & Eisenberg, David S. Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS).  United States.  doi:10.1073/pnas.1705091114.

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                    Sangwan, Smriti, Zhao, Anni, Adams, Katrina L., Jayson, Christina K., Sawaya, Michael R., Guenther, Elizabeth L., Pan, Albert C., Ngo, Jennifer, Moore, Destaye M., Soriaga, Angela B., Do, Thanh D., Goldschmidt, Lukasz, Nelson, Rebecca, Bowers, Michael T., Koehler, Carla M., Shaw, David E., Novitch, Bennett G., and Eisenberg, David S. Mon .  
        "Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)".  United States.  doi:10.1073/pnas.1705091114.

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@article{osti_1390865,

  title        = {Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)},

  author       = {Sangwan, Smriti and Zhao, Anni and Adams, Katrina L. and Jayson, Christina K. and Sawaya, Michael R. and Guenther, Elizabeth L. and Pan, Albert C. and Ngo, Jennifer and Moore, Destaye M. and Soriaga, Angela B. and Do, Thanh D. and Goldschmidt, Lukasz and Nelson, Rebecca and Bowers, Michael T. and Koehler, Carla M. and Shaw, David E. and Novitch, Bennett G. and Eisenberg, David S.},

  abstractNote = {},

  doi          = {10.1073/pnas.1705091114},

  journal      = {Proceedings of the National Academy of Sciences of the United States of America},

  issn         = {0027-8424},

  number       = 33,

  volume       = 114,

  place        = {United States},

  year         = {2017},

  month        = {7}

}

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DOI: 10.1073/pnas.1705091114

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An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
journal, June 1995

Wong, Philip C.; Pardo, Carlos A.; Borchelt, David R.
Neuron, Vol. 14, Issue 6
DOI: 10.1016/0896-6273(95)90259-7

Dali server: conservation mapping in 3D
journal, May 2010

Holm, Liisa; Rosenstrï¿½m, Pï¿½ivi
Nucleic Acids Research, Vol. 38, Issue suppl_2
DOI: 10.1093/nar/gkq366

Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation
journal, March 2008

Hoyer, Wolfgang; Grönwall, Caroline; Jonsson, Andreas
Proceedings of the National Academy of Sciences, Vol. 105, Issue 13
DOI: 10.1073/pnas.0711731105

Atomic View of a Toxic Amyloid Small Oligomer
journal, March 2012

Laganowsky, Arthur; Liu, Cong; Sawaya, Michael R.
Science, Vol. 335, Issue 6073
DOI: 10.1126/science.1213151

An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1
journal, March 2012

Guareschi, S.; Cova, E.; Cereda, C.
Proceedings of the National Academy of Sciences, Vol. 109, Issue 13
DOI: 10.1073/pnas.1115402109

Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution
journal, June 1997

Beamer, L. J.
Science, Vol. 276, Issue 5320
DOI: 10.1126/science.276.5320.1861

Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels
journal, January 2016

Do, Thanh D.; LaPointe, Nichole E.; Nelson, Rebecca
Journal of the American Chemical Society, Vol. 138, Issue 2
DOI: 10.1021/jacs.5b09536

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
journal, March 2016

Tuttle, Marcus D.; Comellas, Gemma; Nieuwkoop, Andrew J.
Nature Structural & Molecular Biology, Vol. 23, Issue 5
DOI: 10.1038/nsmb.3194

Out-of-register -sheets suggest a pathway to toxic amyloid aggregates
journal, December 2012

Liu, C.; Zhao, M.; Jiang, L.
Proceedings of the National Academy of Sciences, Vol. 109, Issue 51
DOI: 10.1073/pnas.1218792109

Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS
journal, December 2013

Ivanova, M. I.; Sievers, S. A.; Guenther, E. L.
Proceedings of the National Academy of Sciences, Vol. 111, Issue 1
DOI: 10.1073/pnas.1320786110

Structural Studies of Amyloid Proteins at the Molecular Level
journal, June 2017

Eisenberg, David S.; Sawaya, Michael R.
Annual Review of Biochemistry, Vol. 86, Issue 1
DOI: 10.1146/annurev-biochem-061516-045104

Misfolded CuZnSOD and amyotrophic lateral sclerosis
journal, March 2003

Valentine, J. S.; Hart, P. J.
Proceedings of the National Academy of Sciences, Vol. 100, Issue 7
DOI: 10.1073/pnas.0730423100

Atomic structures of amyloid cross-β spines reveal varied steric zippers
journal, April 2007

Sawaya, Michael R.; Sambashivan, Shilpa; Nelson, Rebecca
Nature, Vol. 447, Issue 7143
DOI: 10.1038/nature05695

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
journal, March 1993

Rosen, Daniel R.; Siddique, Teepu; Patterson, David
Nature, Vol. 362, Issue 6415
DOI: 10.1038/362059a0

Ligand binding and aggregation of pathogenic SOD1
journal, April 2013

Wright, Gareth S. A.; Antonyuk, Svetlana V.; Kershaw, Neil M.
Nature Communications, Vol. 4, Issue 1
DOI: 10.1038/ncomms2750

Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure
journal, April 2012

Celej, María Soledad; Sarroukh, Rabia; Goormaghtigh, Erik
Biochemical Journal, Vol. 443, Issue 3
DOI: 10.1042/BJ20111924

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
journal, July 2016

Wälti, Marielle Aulikki; Ravotti, Francesco; Arai, Hiromi
Proceedings of the National Academy of Sciences, Vol. 113, Issue 34
DOI: 10.1073/pnas.1600749113

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Title: Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)

Citation Formats

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