Evidence map›Paper›PMID 39558004›Full record

ArticleMolecular psychiatry2025

The pathogenic APP N-terminal Val225Ala mutation alters tau protein liquid-liquid phase separation and exacerbates synaptic damage.

Jiang Chen, Song Li, Fengning Zhang, Junsheng Chen, Chuanbin Cai, Yi Guo, Zhifeng Lei, Ling-Hui Zeng, Dan Zi, Yong Shen and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular psychiatry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
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

11 authors.

Jiang Chen *Institute of Translational Medicine; Key Laboratory of Novel Targets and Drug Study for Neural Repair of Zhejiang Province, School of Medicine, Hangzhou City University, Hangzhou, 310015, China.
Song Li *Center for Clinical Research on Neurological Diseases, the First Affiliated Hospital of Dalian Medical University, Dalian, 116021, China.ORCID 0000-0003-2713-9136
Fengning ZhangKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, 550025, China.
Junsheng ChenKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, 550025, China.
Chuanbin CaiKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, 550025, China.
Yi GuoKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, 550025, China.
Zhifeng LeiKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, 550025, China.
Ling-Hui ZengInstitute of Translational Medicine; Key Laboratory of Novel Targets and Drug Study for Neural Repair of Zhejiang Province, School of Medicine, Hangzhou City University, Hangzhou, 310015, China.
Dan ZiDepartment of Obstetrics and Gynecology, Guizhou Provincial People's Hospital, Guiyang, 550025, China.
Yong ShenDepartment of Neurology, Institute on Aging and Brain Disorders, The First Affiliated Hospital of USTC, Neurodegenerative Disorder Research Center, Division of Biological and Medical Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China; CAS Key Laboratory of Brain Function and Disease, Anhui Provincial Key Laboratory of Biomedical Aging Research, University of Science and Technology of China, Hefei, 23006, China.ORCID 0000-0002-5048-8134
Jun TanInstitute of Translational Medicine; Key Laboratory of Novel Targets and Drug Study for Neural Repair of Zhejiang Province, School of Medicine, Hangzhou City University, Hangzhou, 310015, China. tanjun@anyuhz.cn.ORCID 0000-0002-1703-8596

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31530089National Natural Science Foundation of China (National Science Foundation of China) 82060211National Natural Science Foundation of China (National Science Foundation of China) 82171423National Natural Science Foundation of China (National Science Foundation of China) 82460263
6 · The paper itself

Abstract

Amyloid precursor protein (APP) is predominantly located in synapses of neurons and its mutations have been well recognized as the most important genetic causal factor for the familial Alzheimer's disease (AD). While most disease-causal mutations of APP occur within the Aβ-coding region or immediately proximal, the pathological impacts of mutations in the N-terminus of APP protein, which remote from the Aβ sequence, on neuron and synapse are still largely unknown. It was recently reported a pathogenic APP N-terminal Val225Ala mutation (APP

Indexed as

Amyloid beta-Protein Precursortau ProteinsAlzheimer DiseaseAmyloid beta-PeptidesAnimalsBrainEndocytosisHumansInduced Pluripotent Stem CellsMiceMice, TransgenicMutationNeuronsPhase SeparationPhosphorylationSynapsesAmyloid beta-PeptidesAmyloid beta-Protein Precursortau Proteins

Identifiers

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.