Evidence map›Paper›PMID 37984409›Full record

ArticleMolecular systems biology2023

A multi-layered network model identifies Akt1 as a common modulator of neurodegeneration.

Dokyun Na, Do-Hwan Lim, Jae-Sang Hong, Hyang-Mi Lee, Daeahn Cho, Myeong-Sang Yu, Bilal Shaker, Jun Ren, Bomi Lee, Jae Gwang Song and 12 more

Open access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 9 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

22 authors at 7 institutions in 3 countries.

Dokyun Na *Department of Biomedical Engineering, Chung-Ang University, Seoul, Republic of Korea.ORCID 0000-0002-9107-7040
Do-Hwan Lim *College of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.ORCID 0000-0002-2054-1416
Jae-Sang HongCollege of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.ORCID 0000-0002-7664-6639
Hyang-Mi LeeDepartment of Biomedical Engineering, Chung-Ang University, Seoul, Republic of Korea.
Daeahn ChoDepartment of Biomedical Engineering, Chung-Ang University, Seoul, Republic of Korea.
Myeong-Sang YuDepartment of Biomedical Engineering, Chung-Ang University, Seoul, Republic of Korea.
Bilal ShakerDepartment of Biomedical Engineering, Chung-Ang University, Seoul, Republic of Korea.
Jun RenDepartment of Biomedical Engineering, Chung-Ang University, Seoul, Republic of Korea.
Bomi LeeCollege of Life Sciences, Sejong University, Seoul, Republic of Korea.
Jae Gwang SongCollege of Life Sciences, Sejong University, Seoul, Republic of Korea.ORCID 0000-0002-6015-9393
Yuna OhKorea Institute of Science and Technology, Seoul, Republic of Korea.ORCID 0000-0001-5544-0503
Kyungeun LeeKorea Institute of Science and Technology, Seoul, Republic of Korea.
Kwang-Seok OhInformation-based Drug Research Center, Korea Research Institute of Chemical Technology, Deajeon, Republic of Korea.ORCID 0000-0002-4242-0818
Mi Young LeeInformation-based Drug Research Center, Korea Research Institute of Chemical Technology, Deajeon, Republic of Korea.ORCID 0009-0007-0933-4022
Min-Seok ChoiCollege of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.
Han Saem ChoiCollege of Life Sciences, Sejong University, Seoul, Republic of Korea.
Yang-Hee KimCollege of Life Sciences, Sejong University, Seoul, Republic of Korea.
Jennifer M BuiDepartment of Biochemistry and Molecular Biology, Michael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.
Kangseok LeeDepartment of Life Science, Chung-Ang University, Seoul, Republic of Korea.ORCID 0000-0002-0060-6884
Hyung Wook KimCollege of Life Sciences, Sejong University, Seoul, Republic of Korea.
Young Sik LeeCollege of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.ORCID 0000-0002-6709-3809
Jörg GsponerDepartment of Biochemistry and Molecular Biology, Michael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.ORCID 0000-0003-3672-6594
Chung-Ang University · KRSejong University · KRKorea Institute of Science and Technology · KRKorea University · KRKorea Research Institute of Chemical Technology · KRUniversity of British Columbia · CASoongsil University · KR

Funding

Gouvernement du Canada | Canadian Institutes of Health Research (IRSC) CIHR-AWD-017620National Research Foundation of Korea (NRF) NRF-2018R1A5A1025077National Research Foundation of Korea (NRF) NRF-2021R1A2C1006353National Research Foundation of Korea (NRF) NRF-2022M3A9B6082687National Research Foundation of Korea (NRF) NRF-2022M3E5F3081268
6 · The paper itself

Abstract

The accumulation of misfolded and aggregated proteins is a hallmark of neurodegenerative proteinopathies. Although multiple genetic loci have been associated with specific neurodegenerative diseases (NDs), molecular mechanisms that may have a broader relevance for most or all proteinopathies remain poorly resolved. In this study, we developed a multi-layered network expansion (MLnet) model to predict protein modifiers that are common to a group of diseases and, therefore, may have broader pathophysiological relevance for that group. When applied to the four NDs Alzheimer's disease (AD), Huntington's disease, and spinocerebellar ataxia types 1 and 3, we predicted multiple members of the insulin pathway, including PDK1, Akt1, InR, and sgg (GSK-3β), as common modifiers. We validated these modifiers with the help of four Drosophila ND models. Further evaluation of Akt1 in human cell-based ND models revealed that activation of Akt1 signaling by the small molecule SC79 increased cell viability in all models. Moreover, treatment of AD model mice with SC79 enhanced their long-term memory and ameliorated dysregulated anxiety levels, which are commonly affected in AD patients. These findings validate MLnet as a valuable tool to uncover molecular pathways and proteins involved in the pathophysiology of entire disease groups and identify potential therapeutic targets that have relevance across disease boundaries. MLnet can be used for any group of diseases and is available as a web tool at http://ssbio.cau.ac.kr/software/mlnet.

Indexed as

Alzheimer DiseaseHuntington DiseaseProteostasis DeficienciesAnimalsGlycogen Synthase Kinase 3 betaHumansMiceProto-Oncogene Proteins c-aktSignal TransductionAKT1 protein, humanAkt1 protein, mouseGlycogen Synthase Kinase 3 betaProto-Oncogene Proteins c-aktcommon modifierinsulin signaling pathwaymulti-layered network expansionneurodegenerative diseasesproteostasis

Identifiers

PMID37984409
PMCPMC10698508
OpenAlexW4388852098

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.