Evidence map›Paper›PMID 33374126›Full record

ReviewBiomedicines2020

Modulatory Effects of Autophagy on APP Processing as a Potential Treatment Target for Alzheimer's Disease.

Md Ataur Rahman, Md Saidur Rahman, M D Hasanur Rahman, Mohammad Rasheduzzaman, Anm Mamun-Or-Rashid, Md Jamal Uddin, Md Rezanur Rahman, Hongik Hwang, Myung-Geol Pang, Hyewhon Rhim

Open access · goldAbstract readReview
In one paragraph

Review in Biomedicines, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 60 citations in OpenAlex.

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  9. Functional Relationships between L1CAM, LC3, ATG12, and Aβ.International journal of molecular sciences · 2024
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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

10 authors at 7 institutions in 4 countries.

Md Ataur RahmanCenter for Neuroscience, Brain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea.ORCID 0000-0001-6649-3694
Md Saidur RahmanDepartment of Animal Science & Technology and BET Research Institute, Chung-Ang University, Anseong 456-756, Korea.
M D Hasanur RahmanDepartment of Biotechnology and Genetic Engineering, Bangabandhu Sheikh Mujibur Rahman Science and Technology University, Gopalganj 8100, Bangladesh.ORCID 0000-0001-9238-3149
Mohammad RasheduzzamanSchool of Biomedical Sciences, Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, QLD 4059, Australia.ORCID 0000-0002-5047-8120
Anm Mamun-Or-RashidAnti-Aging Medical Research Center and Glycation Stress Research Center, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto 602-8566, Japan.ORCID 0000-0002-0155-4676
Md Jamal UddinGraduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 03760, Korea.ORCID 0000-0003-2911-3255
Md Rezanur RahmanDepartment of Biochemistry and Biotechnology, School of Biomedical Science, Khwaja Yunus Ali University, Sirajgonj 6751, Bangladesh.ORCID 0000-0002-8739-8714
Hongik HwangCenter for Neuroscience, Brain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea.
Myung-Geol PangDepartment of Animal Science & Technology and BET Research Institute, Chung-Ang University, Anseong 456-756, Korea.ORCID 0000-0003-2019-3789
Hyewhon RhimCenter for Neuroscience, Brain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea.
Chung-Ang University · KRKorea Institute of Brain Science · KRDoshisha University · JPEwha Womans University · KRGopalganj Science and Technology University · BDIslamic University · BDQueensland University of Technology · AU

Funding

National Research Foundation of Korea 2016M3C7A1913845
6 · The paper itself

Abstract

Alzheimer's disease (AD) is characterized by the formation of intracellular aggregate composed of heavily phosphorylated tau protein and extracellular deposit of amyloid-β (Aβ) plaques derived from proteolysis cleavage of amyloid precursor protein (APP). Autophagy refers to the lysosomal-mediated degradation of cytoplasmic constituents, which plays a critical role in maintaining cellular homeostasis. Importantly, recent studies reported that dysregulation of autophagy is associated in the pathogenesis of AD, and therefore, autophagy modulation has gained attention as a promising approach to treat AD pathogenesis. In AD, both the maturation of autolysosomes and its retrograde transports have been obstructed, which causes the accumulation of autophagic vacuoles and eventually leads to degenerating and dystrophic neurites function. However, the mechanism of autophagy modulation in APP processing and its pathogenesis have not yet been fully elucidated in AD. In the early stage of AD, APP processing and Aβ accumulation-mediated autophagy facilitate the removal of toxic protein aggregates via mTOR-dependent and -independent pathways. In addition, a number of autophagy-related genes (Atg) and APP are thought to influence the development of AD, providing a bidirectional link between autophagy and AD pathology. In this review, we summarized the current observations related to autophagy regulation and APP processing in AD, focusing on their modulation associated with the AD progression. Moreover, we emphasizes the application of small molecules and natural compounds to modulate autophagy for the removal and clearance of APP and Aβ deposits in the pathological condition of AD.

Indexed as

Alzheimer’s disease (AD)amyloid precursor protein (APP)autophagymTORβ-amyloid (Aβ)

Identifiers

PMID33374126
PMCPMC7824196
OpenAlexW3113709514

What Socratic 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 Socratic graph.