Evidence map›Paper›PMID 38710967›Full record

ReviewCellular and molecular life sciences : CMLS2024

Physiological and pathological functions of TMEM106B in neurodegenerative diseases.

Min Zhu, Guoxin Zhang, Lanxia Meng, Tingting Xiao, Xin Fang, Zhentao Zhang

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. TMEM106B is a selective modulator of TDP-43 pathology in Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  3. Article
  4. A potential drug target in epilepsy and its role in other neurological disorders.Naunyn-Schmiedeberg's archives of pharmacology · 2026
    Article
  5. Structural insights into human signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
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.

Min Zhu *Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Guoxin Zhang *Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Lanxia MengDepartment of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Tingting XiaoDepartment of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Xin FangDepartment of Neurology, the First Affiliated Hospital of Nanchang University, Nanchang, 330000, China. fangx2011@163.com.
Zhentao ZhangDepartment of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China. zhentaozhang@whu.edu.cn.ORCID http://orcid.org/0000-0001-6708-1472

Funding

the Innovative Research Groups of Hubei Province 2022CFA026the National Key Research and Development Program of China 2019YFE0115900the New 20 Terms of Universities in Jinan No. 202228022the Project for Academic and Technical Leaders of Major Disciplines in Jiangxi Province 20213BCJL22049
6 · The paper itself

Abstract

As an integral lysosomal transmembrane protein, transmembrane protein 106B (TMEM106B) regulates several aspects of lysosomal function and is associated with neurodegenerative diseases. The TMEM106B gene mutations lead to lysosomal dysfunction and accelerate the pathological progression of Neurodegenerative diseases. Yet, the precise mechanism of TMEM106B in Neurodegenerative diseases remains unclear. Recently, different research teams discovered that TMEM106B is an amyloid protein and the C-terminal domain of TMEM106B forms amyloid fibrils in various Neurodegenerative diseases and normally elderly individuals. In this review, we discussed the physiological functions of TMEM106B. We also included TMEM106B gene mutations that cause neurodegenerative diseases. Finally, we summarized the identification and cryo-electronic microscopic structure of TMEM106B fibrils, and discussed the promising therapeutic strategies aimed at TMEM106B fibrils and the future directions for TMEM106B research in neurodegenerative diseases.

Indexed as

Membrane ProteinsNerve Tissue ProteinsNeurodegenerative DiseasesAmyloidAnimalsHumansLysosomesMutationAmyloidMembrane ProteinsNerve Tissue ProteinsTMEM106B protein, humanAmyloid fibrilsLysosomeNeurodegenerative diseasesNeurotherapyTransmembrane protein 106B

Identifiers

PMID38710967
PMCPMC11074223

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.