Evidence map›Paper›PMID 25232037›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Selective filtering defect at the axon initial segment in Alzheimer's disease mouse models.

Xiaqin Sun, Yu Wu, Mingxue Gu, Zhuo Liu, Yuanlin Ma, Jun Li, Yan Zhang

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.7field-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

43 citing papers in PubMed, 65 citations in OpenAlex.

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  14. Extracellular Tau Oligomers Damage the Axon Initial Segment.Journal of Alzheimer's disease : JAD · 2023
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Xiaqin SunState Key Laboratory of Biomembrane and Membrane Biotechnology, College of Life Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing 100871, China; and.
Yu WuState Key Laboratory of Biomembrane and Membrane Biotechnology, College of Life Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing 100871, China; and.
Mingxue GuState Key Laboratory of Biomembrane and Membrane Biotechnology, College of Life Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing 100871, China; and.
Zhuo LiuState Key Laboratory of Biomembrane and Membrane Biotechnology, College of Life Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing 100871, China; and.
Yuanlin MaPeking University Sixth Hospital, Beijing 100191, China.
Jun LiPeking University Sixth Hospital, Beijing 100191, China.
Yan ZhangState Key Laboratory of Biomembrane and Membrane Biotechnology, College of Life Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing 100871, China; and yanzhang@pku.edu.cn.
Peking University · CNPeking University Sixth Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Axon pathology has been widely reported in Alzheimer's disease (AD) patients and AD mouse models. Herein we report that increased miR-342-5p down-regulates the expression of ankyrin G (AnkG), a protein known to play a critical role in establishing selective filtering machinery at the axon initial segment (AIS). Diminished AnkG expression leads to defective AIS filtering in cultured hippocampal neurons from AD mouse models, as monitored by selective exclusion of large macromolecules from the axons. Furthermore, AnkG-deficiency impairs AIS localization of Nav 1.6 channels and confines NR2B to the somatodendritic compartments. The expression of exogenous AnkG improved the cognitive performance of 12-mo-old APP/PS1 mice; thus, our data suggest that AnkG and impairment of AIS filtering may play important roles in AD pathology.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorAnimalsAnkyrinsAxonsCells, CulturedDisease Models, AnimalDown-RegulationHumansMaleMiceMice, TransgenicMicroRNAsMutant ProteinsPresenilin-1Receptors, N-Methyl-D-AspartateAmyloid beta-Protein PrecursorAnk3 protein, mouseAnkyrinsAPP protein, humanMicroRNAsMirn342 microRNA, mouseMutant ProteinsNR2B NMDA receptorPresenilin-1PSEN1 protein, humanReceptors, N-Methyl-D-Aspartate

Identifiers

PMID25232037
PMCPMC4191768
OpenAlexW1996616735

What OpenQuestion holds

Textmetadata
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.