Evidence map›Paper›PMID 33023225›Full record

ArticleNutrients2020

Discovery of Sulforaphane as a Potent BACE1 Inhibitor Based on Kinetics and Computational Studies.

Kumju Youn, Jeong-Hyun Yoon, Nayoung Lee, Gyutae Lim, Jinhyuk Lee, Shengmin Sang, Chi-Tang Ho, Mira Jun

Open access · goldAbstract read
In one paragraph

Article in Nutrients, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

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  14. Efficacy of Sulforaphane in Neurodegenerative Diseases.International journal of molecular sciences · 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

8 authors at 4 institutions in 2 countries.

Kumju YounDepartment of Food Science and Nutrition, College of Health Sciences, Dong-A University, Busan 49315, Korea.ORCID 0000-0002-3124-2665
Jeong-Hyun YoonDepartment of Food Science and Nutrition, College of Health Sciences, Dong-A University, Busan 49315, Korea.
Nayoung LeeDepartment of Food Science and Nutrition, College of Health Sciences, Dong-A University, Busan 49315, Korea.
Gyutae LimGraduate Korean Bioinformation Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Korea.
Jinhyuk LeeGraduate Korean Bioinformation Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Korea.
Shengmin SangCenter for Excellence in Post-Harvest Technologies, North Carolina Agricultural and Technical State University, 500 Laureate Way, Kannapolis, NC 28081, USA.
Chi-Tang HoDepartment of Food Science, Rutgers University, New Brunswick, NJ 08901, USA.
Mira JunDepartment of Food Science and Nutrition, College of Health Sciences, Dong-A University, Busan 49315, Korea.
Dong-A University · KRKorea Research Institute of Bioscience and Biotechnology · KRNorth Carolina Agricultural and Technical State University · USRutgers, The State University of New Jersey · US

Funding

National Research Foundation of Korea NRF-2019R1A2C2006237
6 · The paper itself

Abstract

BACE1 is the rate-limiting enzyme involved in the production and deposition of β-amyloid (Aβ). Since neurotoxic Aβ plays a critical role in Alzheimer's disease (AD) pathogenesis, BACE1 has emerged as a key target for preventing AD. In the present study, the potential of sulforaphane, an isothiocyanate found in cruciferous vegetables, as a BACE1 inhibitor has been investigated. Sulforaphane exhibited six times more potent activity against BACE1 compared to well-known positive controls including resveratrol and quercetin. Sulforaphane presented selective and non-competitive BACE1 inhibitory activity with low off-target inhibition of BACE2 and other aspartic and serine proteases. In addition, sulforaphane presented negative binding energy, suggesting that the compound had a high affinity for BACE1. It interacted with locations other than the active binding sites of BACE1 through van der Waals forces. Overall, sulforaphane appeared to be a promising candidate with potent and selective BACE1 inhibitory properties that play an important role in AD prevention.

Indexed as

Amyloid beta-PeptidesAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesComputational BiologyHumansIsothiocyanatesMolecular Docking SimulationQuercetinResveratrolSulfoxidesAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBACE1 protein, humanIsothiocyanatesQuercetinResveratrolsulforaphaneSulfoxidesAlzheimer’s disease (AD)BACE1in silico dockingsulforaphane

Identifiers

PMID33023225
PMCPMC7601397
OpenAlexW3091103975

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.