Evidence map›Paper›PMID 28650319›Full record

ArticleeLife2017

Somatostatin binds to the human amyloid β peptide and favors the formation of distinct oligomers.

Hansen Wang, Lisa D Muiznieks, Punam Ghosh, Declan Williams, Michael Solarski, Andrew Fang, Alejandro Ruiz-Riquelme, Régis Pomès, Joel C Watts, Avi Chakrabartty and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

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  20. Somatostatin, Olfaction, and Neurodegeneration.Frontiers in neuroscience · 2020
    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

13 authors at 3 institutions in 1 country.

Hansen WangTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Canada.ORCID 0000-0003-4414-3372
Lisa D MuiznieksMolecular Medicine Program, Research Institute, The Hospital for Sick Children, Toronto, Canada.
Punam GhoshDepartment of Medical Biophysics, University of Toronto, Toronto, Canada.
Declan WilliamsTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Canada.
Michael SolarskiTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Canada.
Andrew FangDepartment of Biochemistry, University of Alberta, Edmonton, Canada.
Alejandro Ruiz-RiquelmeTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Canada.ORCID 0000-0001-6581-7132
Régis PomèsMolecular Medicine Program, Research Institute, The Hospital for Sick Children, Toronto, Canada.ORCID 0000-0003-3068-9833
Joel C WattsTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Canada.
Avi ChakrabarttyDepartment of Medical Biophysics, University of Toronto, Toronto, Canada.
Holger WilleDepartment of Biochemistry, University of Alberta, Edmonton, Canada.ORCID 0000-0001-5102-8706
Simon SharpeMolecular Medicine Program, Research Institute, The Hospital for Sick Children, Toronto, Canada.
Gerold Schmitt-UlmsTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Canada.ORCID 0000-0001-6962-0919
University of Toronto · CAUniversity of Alberta · CAHospital for Sick Children · CA

Funding

CIHR
6 · The paper itself

Abstract

The amyloid β peptide (Aβ) is a key player in the etiology of Alzheimer disease (AD), yet a systematic investigation of its molecular interactions has not been reported. Here we identified by quantitative mass spectrometry proteins in human brain extract that bind to oligomeric Aβ1-42 (oAβ1-42) and/or monomeric Aβ1-42 (mAβ1-42) baits. Remarkably, the cyclic neuroendocrine peptide somatostatin-14 (SST14) was observed to be the most selectively enriched oAβ1-42 binder. The binding interface comprises a central tryptophan within SST14 and the N-terminus of Aβ1-42. The presence of SST14 inhibited Aβ aggregation and masked the ability of several antibodies to detect Aβ. Notably, Aβ1-42, but not Aβ1-40, formed in the presence of SST14 oligomeric assemblies of 50 to 60 kDa that were visualized by gel electrophoresis, nanoparticle tracking analysis and electron microscopy. These findings may be relevant for Aβ-directed diagnostics and may signify a role of SST14 in the etiology of AD.

Indexed as

Protein MultimerizationAmyloid beta-PeptidesBrainHormonesHumansMass SpectrometryMolecular WeightProtein BindingSomatostatinAmyloid beta-PeptidesHormonesSomatostatinabetaAlzheimer's diseasebiochemistryhumaninteractomemass spectrometrymouseneuroscienceoligomersomatostatin

Identifiers

PMID28650319
PMCPMC5505701
OpenAlexW2722645493

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.