Evidence map›Paper›PMID 28649025›Full record

ArticleBiosensors & bioelectronics2017

Aβ plaque-selective NIR fluorescence probe to differentiate Alzheimer's disease from tauopathies.

K Rajasekhar, Nagarjun Narayanaswamy, N Arul Murugan, Keith Viccaro, Hyoung-Gon Lee, Kavita Shah, Thimmaiah Govindaraju

Abstract read
In one paragraph

Article in Biosensors & bioelectronics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 94 citations in OpenAlex.

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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

7 authors at 5 institutions in 3 countries.

K RajasekharBioorganic Chemistry Laboratory, New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur P.O., Bengaluru 560064, Karnataka, India.
Nagarjun NarayanaswamyBioorganic Chemistry Laboratory, New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur P.O., Bengaluru 560064, Karnataka, India.
N Arul MuruganDivision of Theoretical Chemistry and Biology, School of Biotechnology, KTH Royal Institute of Technology, S-106 91 Stockholm, Sweden.
Keith ViccaroDepartment of Chemistry, Purdue University Center for Cancer Research, 560 Oval Drive, West Lafayette, IN 47907, USA.
Hyoung-Gon LeeDepartment of Biology, The University of Texas at San Antonio, One UTSA Circle, San Antonio, TX 78249, USA.
Kavita ShahDepartment of Chemistry, Purdue University Center for Cancer Research, 560 Oval Drive, West Lafayette, IN 47907, USA.
Thimmaiah GovindarajuBioorganic Chemistry Laboratory, New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur P.O., Bengaluru 560064, Karnataka, India. Electronic address: tgraju@jncasr.ac.in.
Jawaharlal Nehru Centre for Advanced Scientific Research · INCenter for Cancer Research · USKTH Royal Institute of Technology · SEPurdue University West Lafayette · USThe University of Texas at San Antonio · US

Funding

Exploring FOXO Signaling in Promoting Neurodegeneration in ADR21AG047447 · NIA · PURDUE UNIVERSITY · PI SHAH, KAVITA · 2014 to 2015
$435k
NIA NIH HHS R21 AG047447
6 · The paper itself

Abstract

Selective detection and staining of toxic amyloid plaques, a potential biomarker present in the Alzheimer's disease (AD) brain is crucial for both clinical diagnosis and monitoring AD disease progression. Herein, we report a coumarin-quinoline (CQ) conjugate-based turn-on near-infrared (NIR) fluorescence probe for specific detection of β-amyloid (Aβ) aggregates. CQ probe is highly sensitive and exhibits ~100-fold fluorescence enhancement in vitro upon binding Aβ aggregates with enhanced quantum yield. Furthermore, the probe has ~10-fold higher binding affinity towards Aβ aggregates (86nM) compared to commonly used Thioflavin T. Most importantly, CQ probe displays unambiguous selectivity towards Aβ aggregates compared to other toxic protein aggregates such as tau, α-synuclein (α-Syn) and islet amyloid polypeptide (IAPP). In addition, CQ is nontoxic to neuronal cells and shows significant blood brain barrier permeability. Remarkably, CQ stains Aβ plaques in human brain tissue over co-existing tau aggregates and neurofibrillary tangles (NFTs), which are associated in AD and tauopathies. This is a highly desirable attribute to distinguish AD from tau pathology and mixed dementia.

Indexed as

Biosensing TechniquesAlzheimer DiseaseAmyloid beta-PeptidesBlood-Brain BarrierDiagnosis, DifferentialFluorescenceHumansNeuronsPlaque, AmyloidTauopathiestau ProteinsAmyloid beta-Peptidestau ProteinsAlzheimer's diseaseMixed dementiaNeurofibrillary tangles (NFTs)NIR fluorescence probesSelective detection of Aβ42 plaquesTauopathies

Identifiers

PMID28649025
PMCPMC6370041
OpenAlexW2713453502

What OpenQuestion holds

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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.