Evidence map›Paper›PMID 36073854›Full record

ArticleInorganic chemistry2022

Alzheimer's Drug PBT2 Interacts with the Amyloid β 1-42 Peptide Differently than Other 8-Hydroxyquinoline Chelating Drugs.

Kelly L Summers, Graham Roseman, Kevin M Schilling, Natalia V Dolgova, M Jake Pushie, Dimosthenis Sokaras, Thomas Kroll, Hugh H Harris, Glenn L Millhauser, Ingrid J Pickering and 1 more

Open access · greenAbstract read
In one paragraph

Article in Inorganic chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Metal Ion Signaling in Biomedicine.Chemical reviews · 2025
    Review
  7. Review
  8. Review
  9. Article
  10. Chelator PBT2 Forms a Ternary CuInternational journal of molecular sciences · 2023
    Article
  11. Metals in Alzheimer's Disease.Biomedicines · 2023
    Review
  12. Review
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

11 authors at 4 institutions in 3 countries.

Kelly L SummersMolecular and Environmental Sciences Group, Department of Geological Sciences, College of Arts and Science, University of Saskatchewan, 114 Science Place, Saskatoon, SaskatchewanS7N 5E2, Canada.ORCID 0000-0001-9185-5052
Graham RosemanDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, 1156 High Street, Santa Cruz, California95064, United States.
Kevin M SchillingDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, 1156 High Street, Santa Cruz, California95064, United States.
Natalia V DolgovaMolecular and Environmental Sciences Group, Department of Geological Sciences, College of Arts and Science, University of Saskatchewan, 114 Science Place, Saskatoon, SaskatchewanS7N 5E2, Canada.
M Jake PushieDepartment of Surgery, University of Saskatchewan, 103 Hospital Drive, Saskatoon, SaskatchewanS7N 0W8, Canada.ORCID 0000-0001-7494-5427
Dimosthenis SokarasStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California94025, United States.
Thomas KrollStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California94025, United States.
Hugh H HarrisDepartment of Chemistry, University of Adelaide, Adelaide, SA5005, Australia.ORCID 0000-0002-3472-8628
Glenn L MillhauserDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, 1156 High Street, Santa Cruz, California95064, United States.ORCID 0000-0003-2442-7220
Ingrid J PickeringMolecular and Environmental Sciences Group, Department of Geological Sciences, College of Arts and Science, University of Saskatchewan, 114 Science Place, Saskatoon, SaskatchewanS7N 5E2, Canada.ORCID 0000-0002-0936-2994
Graham N GeorgeMolecular and Environmental Sciences Group, Department of Geological Sciences, College of Arts and Science, University of Saskatchewan, 114 Science Place, Saskatoon, SaskatchewanS7N 5E2, Canada.ORCID 0000-0002-0420-7493
University of Saskatchewan · CAUniversity of California, Santa Cruz · USSLAC National Accelerator Laboratory · USThe University of Adelaide · AU

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Supplement Request for Emergency Replacement of EPR Amplifier and Acquisition of a Low Volume Resonator for Membrane ProteinsR35GM131781 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI GLENN L MILLHAUSER · 2019 to 2026
$3.6M
NCRR NIH HHS P41 RR001209NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R35 GM131781
6 · The paper itself

Abstract

Although Alzheimer's disease (AD) was first described over a century ago, it remains the leading cause of age-related dementia. Innumerable changes have been linked to the pathology of AD; however, there remains much discord regarding which might be the initial cause of the disease. The "amyloid cascade hypothesis" proposes that the amyloid β (Aβ) peptide is central to disease pathology, which is supported by elevated Aβ levels in the brain before the development of symptoms and correlations of amyloid burden with cognitive impairment. The "metals hypothesis" proposes a role for metal ions such as iron, copper, and zinc in the pathology of AD, which is supported by the accumulation of these metals within amyloid plaques in the brain. Metals have been shown to induce aggregation of Aβ, and metal ion chelators have been shown to reverse this reaction

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesClioquinolChelating AgentsCopperHumansIonsMetalsOxyquinolinePeptide FragmentsSolventsZincAmyloid beta-Peptidesamyloid beta-protein (1-42)Chelating AgentsClioquinolCopperIonsMetalsOxyquinolinePBT2 compoundPeptide FragmentsSolventsZinc

Identifiers

PMID36073854
PMCPMC9957665
OpenAlexW4294992002

What OpenQuestion holds

Textmetadata
LicenceTDM
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.