Evidence map›Paper›PMID 30215158›Full record

ArticleMolecular neurobiology2019

Trpm2 Ablation Accelerates Protein Aggregation by Impaired ADPR and Autophagic Clearance in the Brain.

Yongwoo Jang, Byeongjun Lee, Hyungsup Kim, Seungmoon Jung, Sung Hoon Lee, So-Young Lee, Ji Hyun Jeon, In-Beom Kim, Seo-Ho Lee, Byung-Ju Kim and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular neurobiology, 2019. 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
1.3field-weighted citation impact, top 19% 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, 19 citations in OpenAlex.

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  5. Review
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  8. Research progress on transient receptor potential melastatin 2 channel in nervous system diseases.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2021
    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

15 authors at 9 institutions in 3 countries.

Yongwoo JangCollege of Pharmacy, Seoul National University, Seoul, 02862, South Korea.
Byeongjun LeeSensory Research Center, Brain Science Institute, Korea Institute of Science and Technology, 5 Hwarang-ro 14-gil, Seongbuk-gu, Seoul, 02792, South Korea.
Hyungsup KimSensory Research Center, Brain Science Institute, Korea Institute of Science and Technology, 5 Hwarang-ro 14-gil, Seongbuk-gu, Seoul, 02792, South Korea.
Seungmoon JungDepartment of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology, Daejeon, 305-701, South Korea.
Sung Hoon LeeCollege of Pharmacy, Chung-ang University, Seoul, 06974, South Korea.
So-Young LeeDepartment of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology, Daejeon, 305-701, South Korea.
Ji Hyun JeonDepartment of Anatomy, College of Medicine, Catholic University of Korea, Seoul, 137-701, South Korea.
In-Beom KimDepartment of Anatomy, College of Medicine, Catholic University of Korea, Seoul, 137-701, South Korea.
Seo-Ho LeeDepartment of Biochemistry, College of Medicine, Chonbuk National University, Jeonju, South Korea.
Byung-Ju KimDepartment of Biochemistry, College of Medicine, Chonbuk National University, Jeonju, South Korea.
Uh-Hyun KimDepartment of Biochemistry, College of Medicine, Chonbuk National University, Jeonju, South Korea.
Yunjong LeeDepartment of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Samsung Biomedical Research Institute, Suwon, 446-746, South Korea.
Sung Min KimDepartment of Active Aging Industry, Hanyang University, Seoul, 04763, South Korea.
Daejong JeonDepartment of Neurology, Comprehensive Epilepsy Center, Biomedical Research Institute, Seoul National University Hospital, Seoul, 110-744, South Korea.
Uhtaek OhCollege of Pharmacy, Seoul National University, Seoul, 02862, South Korea. utoh@kist.ac.kr.ORCID http://orcid.org/0000-0002-8935-8863
Korea Advanced Institute of Science and Technology · KRCatholic University of Korea · KRJeonbuk National University · KRKorean Association Of Science and Technology Studies · KRHanyang University · KRHarvard University · USNational University College · PRSamsung (South Korea) · KRSeoul National University Hospital · KR

Funding

National Research Foundation of Korea 2011-0018358
6 · The paper itself

Abstract

TRPM2 a cation channel is also known to work as an enzyme that hydrolyzes highly reactive, neurotoxic ADP-ribose (ADPR). Although ADPR is hydrolyzed by NUT9 pyrophosphatase in major organs, the enzyme is defective in the brain. The present study questions the role of TRPM2 in the catabolism of ADPR in the brain. Genetic ablation of Trpm2 results in the disruption of ADPR catabolism that leads to the accumulation of ADPR and reduction in AMP. Trpm2

Indexed as

AutophagyGene DeletionProtein AggregatesAdenosine Diphosphate RiboseAnimalsBrainCognitionHippocampusHydrolysisMemoryMice, Inbred C57BLMice, KnockoutNerve DegenerationNeuronal PlasticityNeuronsSynaptic TransmissionAdenosine Diphosphate RiboseProtein AggregatesTRPM2 protein, mouseTRPM Cation ChannelsADPRAMPAutophagyProtein aggregationTRPM2

Identifiers

PMID30215158
PMCPMC6477016
OpenAlexW2890895249

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.