Evidence map›Paper›PMID 29859874›Full record

ArticleNeurobiology of disease2018

Newfound effect of N-acetylaspartate in preventing and reversing aggregation of amyloid-beta in vitro.

Jean-Pierre Dollé, Jeffrey M Rodgers, Kevin D Browne, Thomas Troxler, Feng Gai, Douglas H Smith

Open access · greenAbstract read
In one paragraph

Article in Neurobiology of disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. The Emerging Role of N-Acetylaspartate in Cancer.International journal of molecular sciences · 2026
    Review
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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

6 authors at 2 institutions in 1 country.

Jean-Pierre DolléPenn Center for Brain Injury and Repair, Department of Neurosurgery, University of Pennsylvania, 220 South 33rd Street, 283 Towne Building, Philadelphia, PA 19104, USA.
Jeffrey M RodgersDepartment of Chemistry, The Ultrafast Optical Processes Laboratory, University of Pennsylvania, Philadelphia, PA 19104, USA.
Kevin D BrownePenn Center for Brain Injury and Repair, Department of Neurosurgery, University of Pennsylvania, 220 South 33rd Street, 283 Towne Building, Philadelphia, PA 19104, USA.
Thomas TroxlerDepartment of Chemistry, The Ultrafast Optical Processes Laboratory, University of Pennsylvania, Philadelphia, PA 19104, USA.
Feng GaiDepartment of Chemistry, The Ultrafast Optical Processes Laboratory, University of Pennsylvania, Philadelphia, PA 19104, USA.
Douglas H SmithPenn Center for Brain Injury and Repair, Department of Neurosurgery, University of Pennsylvania, 220 South 33rd Street, 283 Towne Building, Philadelphia, PA 19104, USA. Electronic address: smithdou@pennmedicine.upenn.edu.
University of Pennsylvania · USOptica · US

Funding

TBI: Uncovering Mechanisms of AD-like pathologyR01NS038104 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI SMITH, DOUGLAS HAMILTON · 1999 to 2020
$7.6M
BRIAN INJURY TRAINING GRANTT32NS043126 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI Douglas Hamilton Smith · 2003 to 2026
$5.9M
ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
Neuropathological Characterization of 'CTE'R01NS094003 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI Douglas Hamilton Smith, William Stewart · 2016 to 2026
$5.1M
Detection and Mechanisms of Mild Traumatic Brain InjuryR01NS092398 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI SMITH, DOUGLAS HAMILTON · 2015 to 2019
$1.9M
Uncovering mechanical mechanisms of traumatic axonal injuryR01EB021293 · NIBIB · UNIVERSITY OF PENNSYLVANIA · PI SHENOY, VIVEK, SMITH, DOUGLAS HAMILTON · 2016 to 2019
$1.4M
NIBIB NIH HHS R01 EB021293NIGMS NIH HHS P41 GM104605NINDS NIH HHS R01 NS038104NINDS NIH HHS R01 NS092398NINDS NIH HHS R01 NS094003NINDS NIH HHS T32 NS043126
6 · The paper itself

Abstract

Although N-acetylaspartate (NAA) has long been recognized as the most abundant amino acid in neurons by far, its primary role has remained a mystery. Based on its unique tertiary structure, we explored the potential of NAA to modulate aggregation of amyloid-beta (Aβ) peptide 1-42 via multiple corroborating aggregation assays along with electron microscopy. Thioflavin-T fluorescence assay demonstrated that at physiological concentrations, NAA substantially inhibited the initiation of Aβ fibril formation. In addition, NAA added after 25 min of Aβ aggregation was shown to break up preformed fibrils. Electron microscopy analysis confirmed the absence of mature fibrils following NAA treatment. Furthermore, fluorescence correlation spectroscopy and dynamic light scattering measurements confirmed significant reductions in Aβ fibril hydrodynamic radius following treatment with NAA. These results suggest that physiological levels of NAA could play an important role in controlling Aβ aggregation in vivo where they are both found in the same neuronal compartments.

Indexed as

AmyloidAmyloid beta-PeptidesAspartic AcidDose-Response Relationship, DrugHumansPeptide FragmentsProtein AggregatesAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-42)Aspartic AcidN-acetylaspartatePeptide FragmentsProtein AggregatesAggregation inhibitorAmyloid betaDynamic light scatteringFluorescence correlation spectroscopyN-AcetylaspartateThioflavin-TTransmission electron microscopy

Identifiers

PMID29859874
PMCPMC6553457
OpenAlexW2806419053

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.