Evidence map›Paper›PMID 25575678›Full record

ArticleMolecular neurobiology2016

SIL1 Rescued Bip Elevation-Related Tau Hyperphosphorylation in ER Stress.

Zan-Chao Liu, Jiang Chu, Li Lin, Jie Song, Lin-Na Ning, Hong-Bin Luo, Shu-Sheng Yang, Yan Shi, Qun Wang, Na Qu and 3 more

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular neurobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Liquid-liquid phase separation in Alzheimer's disease.Journal of molecular medicine (Berlin, Germany) · 2024
    Review
  7. Article
  8. Review
  9. Calcium Dyshomeostasis in Alzheimer's Disease Pathogenesis.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Review
  12. Role of the HSP70 Co-Chaperone SIL1 in Health and Disease.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Chaperone Sigma1R and Antidepressant Effect.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

13 authors at 2 institutions in 1 country.

Zan-Chao LiuDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Jiang ChuDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Li LinDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Jie SongDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Lin-Na NingDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Hong-Bin LuoDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Shu-Sheng YangDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Yan ShiDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Qun WangDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Na QuDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Qi ZhangDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China.
Jian-Zhi WangDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China. wangjz@mails.tjmu.edu.cn.
Qing TianDepartment of Pathology and Pathophysiology, School of Basic Medicine, Tongji Medical College; Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute of Brain Science, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, 430030, China. tianq@hust.edu.cn.
Huazhong University of Science and Technology · CNTongji University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoplasmic reticulum (ER) stress has been indicated in the early stage of Alzheimer's disease (AD), in which tau hyperphosphorylation is one major pathological alteration. The elevation of binding immunoglobulin protein (Bip), an important ER chaperon, was reported in AD brain. It is important to study the roles of ER-related chaperons in tau hyperphosphorylation. In this research, increased Bip was found in the brains of the AD model mice (Tg2576) compared to the age-matched control mice. Meanwhile, deficiency of SIL1, an important co-chaperon of Bip, was observed in brains of Tg2576 mice and in ER stress both in vivo and in vitro. Then, we transfected Bip-EGFP plasmid into HEK293 cells stably expressing the longest human tau (HEK293/tau) or N2a cells and found that increased Bip induced tau hyperphosphorylation via activating glycogen synthase kinase-3β (GSK-3β), an important tau kinase, and increased the association with tau and GSK-3β. When we overexpressed SIL1 in Bip-transfected HEK293/tau cells and thapsigargin-treated HEK293/tau cells, significantly reduced tau hyperphosphorylation and GSK-3β activation were observed. These results suggested the important roles of ER-related chaperons, Bip and SIL1, in AD-like tau hyperphosphorylation.

Indexed as

Endoplasmic Reticulum StressAnimalsBrainEndoplasmic Reticulum Chaperone BiPEnzyme ActivationGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGuanine Nucleotide Exchange FactorsHeat-Shock ProteinsHEK293 CellsHumansIndolesMaleimidesMice, Inbred C57BLMice, TransgenicModels, BiologicalEndoplasmic Reticulum Chaperone BiPGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGuanine Nucleotide Exchange FactorsHeat-Shock ProteinsIndolesMaleimidesSB 216763SIL1 protein, mousetau ProteinsThapsigarginAlzheimer’s diseaseBipGSK-3βSIL1Tau

Identifiers

PMID25575678
OpenAlexW1976766768

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.