Evidence map›Paper›PMID 26374940›Full record

ArticleBiochimica et biophysica acta2015

Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.

Robin Altman, Sonny Ly, Silvia Hilt, Jitka Petrlova, Izumi Maezawa, Tamás Kálai, Kálmán Hideg, Lee-Way Jin, Ted A Laurence, John C Voss

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Oligomerization Alters Binding Affinity Between Amyloid Beta and a Modulator of Peptide Aggregation.The journal of physical chemistry. C, Nanomaterials and interfaces · 2017
    Article
  8. A Metal-Free Method for Producing MRI Contrast at Amyloid-β.Journal of Alzheimer's disease : JAD · 2017
    Article
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

10 authors at 3 institutions in 2 countries.

Robin AltmanDepartment of Biochemistry & Molecular Medicine, University of California Davis, Davis CA 95616, USA.
Sonny LyPhysical and Life Science Directorate, Lawrence Livermore National Laboratory, Livermore CA 94550, USA.
Silvia HiltDepartment of Biochemistry & Molecular Medicine, University of California Davis, Davis CA 95616, USA.
Jitka PetrlovaDepartment of Biochemistry & Molecular Medicine, University of California Davis, Davis CA 95616, USA.
Izumi MaezawaM.I.N.D. Institute and Department of Pathology and Laboratory Medicine, University of California Davis, Sacramento CA 95817, USA.
Tamás KálaiInstitute of Organic and Medicinal Chemistry, University of Pécs, H-7624 Pécs, Szigeti st. 12. Pécs, Hungary.
Kálmán HidegInstitute of Organic and Medicinal Chemistry, University of Pécs, H-7624 Pécs, Szigeti st. 12. Pécs, Hungary.
Lee-Way JinM.I.N.D. Institute and Department of Pathology and Laboratory Medicine, University of California Davis, Sacramento CA 95817, USA.
Ted A LaurencePhysical and Life Science Directorate, Lawrence Livermore National Laboratory, Livermore CA 94550, USA.
John C VossDepartment of Biochemistry & Molecular Medicine, University of California Davis, Davis CA 95616, USA. Electronic address: jcvoss@ucdavis.edu.
University of California, Davis · USLawrence Livermore National Laboratory · USUniversity of Pecs · HU

Funding

UC Davis Alzheimer's Disease Core CenterP30AG010129 · NIA · UNIVERSITY OF CALIFORNIA DAVIS · PI DECARLI, CHARLES · 1991 to 2020
$28.3M
NIA NIH HHS P30 AG010129
6 · The paper itself

Abstract

Alzheimer's disease is characterized by the presence of extracellular plaques comprised of amyloid beta (Aβ) peptides. Soluble oligomers of the Aβ peptide underlie a cascade of neuronal loss and dysfunction associated with Alzheimer's disease. Single particle analyses of Aβ oligomers in solution by fluorescence correlation spectroscopy (FCS) were used to provide real-time descriptions of how spin-labeled fluorenes (SLFs; bi-functional small molecules that block the toxicity of Aβ) prevent and disrupt oligomeric assemblies of Aβ in solution. Furthermore, the circular dichroism (CD) spectrum of untreated Aβ shows a continuous, progressive change over a 24-hour period, while the spectrum of Aβ treated with SLF remains relatively constant following initial incubation. These findings suggest the conformation of Aβ within the oligomer provides a complementary determinant of Aβ toxicity in addition to oligomer growth and size. Although SLF does not produce a dominant state of secondary structure in Aβ, it does induce a net reduction in beta secondary content compared to untreated samples of Aβ. The FCS results, combined with electron paramagnetic resonance spectroscopy and CD spectroscopy, demonstrate SLFs can inhibit the growth of Aβ oligomers and disrupt existing oligomers, while retaining Aβ as a population of smaller, yet largely disordered oligomers.

Indexed as

Spin LabelsAmyloid beta-PeptidesCell LineCircular DichroismFluorenesHumansProtein Structure, SecondaryAmyloid beta-PeptidesFluorenesSpin LabelsAmyloid betaCircular dichroism spectroscopyFluorescence correlation spectroscopyOligomerSecondary structureSpin-labeled fluorene

Identifiers

PMID26374940
PMCPMC4631661
OpenAlexW1884867387

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.