Evidence map›Paper›PMID 28760994›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

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

Smriti Sangwan, Anni Zhao, Katrina L Adams, Christina K Jayson, Michael R Sawaya, Elizabeth L Guenther, Albert C Pan, Jennifer Ngo, Destaye M Moore, Angela B Soriaga and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
9.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

49 citing papers in PubMed, 118 citations in OpenAlex.

  1. Usefulness ofInternational journal of molecular sciences · 2026
    Article
  2. Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026
    Review
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  14. Probing differences among Aβ oligomers with two triangular trimers derived from Aβ.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

18 authors at 6 institutions in 1 country.

Smriti SangwanHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095.
Anni ZhaoHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095.
Katrina L AdamsDepartment of Neurobiology, Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095.
Christina K JaysonDepartment of Chemistry & Biochemistry, University of California, Los Angeles, CA 90095.
Michael R SawayaHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095.
Elizabeth L GuentherHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095.
Albert C PanD. E. Shaw Research, New York, NY 10036.
Jennifer NgoDepartment of Chemistry & Biochemistry, University of California, Los Angeles, CA 90095.
Destaye M MooreDepartment of Neurobiology, Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095.
Angela B SoriagaHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095.
Thanh D DoDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106.
Lukasz GoldschmidtHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095.
Rebecca NelsonHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095.
Michael T BowersDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106.
Carla M KoehlerDepartment of Chemistry & Biochemistry, University of California, Los Angeles, CA 90095.
David E ShawD. E. Shaw Research, New York, NY 10036.
Bennett G NovitchDepartment of Neurobiology, Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095.
David S EisenbergHoward Hughes Medical Institute, UCLA-DOE and Molecular Biology Institutes, Department of Biological Chemistry, University of California, Los Angeles, CA 90095; david@mbi.ucla.edu.
University of California, Los Angeles · USBroad Center · USHoward Hughes Medical Institute · USUniversity of California, Santa Barbara · USColumbia University · USD. E. Shaw Research · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Biogenesis of the mitochondrial inner membrane diversity supplementR01GM061721 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KOEHLER, CARLA M · 2000 to 2025
$8.1M
Structure and Inhibition of Amyloid in Alzheimer's DiseaseRF1AG054022 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2016 to 2018
$4.2M
Structural Biology of Amyloid DiseaseR01AG029430 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2007 to 2016
$3.9M
Amyloid Beta-Protein: Wild Type and Familial Mutant Assembly and InhibitionR01AG047116 · NIA · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI BOWERS, MICHAEL THOMAS · 2013 to 2016
$1.8M
Transcriptional regulation of neuronal differentiationR01NS072804 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI NOVITCH, BENNETT G · 2010 to 2014
$1.6M
Howard Hughes Medical InstituteNIA NIH HHS R01 AG029430NIA NIH HHS R01 AG047116NIA NIH HHS RF1 AG054022NIGMS NIH HHS R01 GM061721NIGMS NIH HHS T32 GM007185NINDS NIH HHS R01 NS072804
6 · The paper itself

Abstract

Fibrils and oligomers are the aggregated protein agents of neuronal dysfunction in ALS diseases. Whereas we now know much about fibril architecture, atomic structures of disease-related oligomers have eluded determination. Here, we determine the corkscrew-like structure of a cytotoxic segment of superoxide dismutase 1 (SOD1) in its oligomeric state. Mutations that prevent formation of this structure eliminate cytotoxicity of the segment in isolation as well as cytotoxicity of the ALS-linked mutants of SOD1 in primary motor neurons and in a

Indexed as

Amyotrophic Lateral SclerosisAnimalsCrystallography, X-RayMiceMotor NeuronsMutationProtein Conformation, beta-StrandSuperoxide Dismutase-1Superoxide Dismutase-1ALSoligomerSOD1

Identifiers

PMID28760994
PMCPMC5565441
OpenAlexW2740121245

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.