Evidence map›Paper›PMID 25525276›Full record

ArticleThe Journal of biological chemistry2015

SorLA complement-type repeat domains protect the amyloid precursor protein against processing.

Arnela Mehmedbasic, Sofie K Christensen, Jonas Nilsson, Ulla Rüetschi, Camilla Gustafsen, Annemarie Svane Aavild Poulsen, Rikke W Rasmussen, Anja N Fjorback, Göran Larson, Olav M Andersen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 2 pooled it
2.4field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 2 syntheses or guidelines pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. LR11/SorLA and its role in cardiovascular disease.International journal of cardiology. Heart & vasculature · 2026
    Review
  4. FromCells · 2026
    Review
  5. Familial Alzheimer's disease mutation identifies novel role of SORLA in release of neurotrophic exosomes.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  6. Article
  7. TheProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Dimerization of the Alzheimer's disease pathogenic receptor SORLA regulates its association with retromer.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Sorting Out the Role of theJournal of Alzheimer's disease reports · 2020
    Review
  18. 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

10 authors at 3 institutions in 2 countries.

Arnela MehmedbasicFrom the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and.
Sofie K ChristensenFrom the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and.
Jonas Nilssonthe Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, University of Gothenburg, SE-413 45 Gothenburg, Sweden.
Ulla Rüetschithe Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, University of Gothenburg, SE-413 45 Gothenburg, Sweden.
Camilla GustafsenFrom the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and.
Annemarie Svane Aavild PoulsenFrom the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and.
Rikke W RasmussenFrom the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and.
Anja N FjorbackFrom the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and.
Göran Larsonthe Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, University of Gothenburg, SE-413 45 Gothenburg, Sweden.
Olav M AndersenFrom the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and o.andersen@biomed.au.dk.
Aarhus University · DKLundbeck Foundation · DKUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SorLA is a neuronal sorting receptor that is genetically associated with Alzheimer disease. SorLA interacts directly with the amyloid precursor protein (APP) and affects the processing of the precursor, leading to a decreased generation of the amyloid-β peptide. The SorLA complement-type repeat (CR) domains associate in vitro with APP, but the precise molecular determinants of SorLA·APP complex formation and the mechanisms responsible for the effect of binding on APP processing have not yet been elucidated. Here, we have generated protein expression constructs for SorLA devoid of the 11 CR-domains and for two SorLA mutants harboring substitutions of the fingerprint residues in the central CR-domains. We generated SH-SY5Y cell lines that stably express these SorLA variants to study the binding and processing of APP using co-immunoprecipitation and Western blotting/ELISAs, respectively. We found that the SorLA CR-cluster is essential for interaction with APP and that deletion of the CR-cluster abolishes the protection against APP processing. Mutation of identified fingerprint residues in the SorLA CR-domains leads to changes in the O-linked glycosylation of APP when expressed in SH-SY5Y cells. Our results provide novel information on the mechanisms behind the influence of SorLA activity on APP metabolism by controlling post-translational glycosylation in the Golgi, suggesting new strategies against amyloidogenesis in Alzheimer disease.

Indexed as

Protein Processing, Post-TranslationalAmyloid beta-Protein PrecursorBinding SitesCell Line, TumorGlycosylationHumansLDL-Receptor Related ProteinsMembrane Transport ProteinsProtein BindingProtein TransportAmyloid beta-Protein PrecursorLDL-Receptor Related ProteinsMembrane Transport ProteinsSORL1 protein, humanAlzheimer DiseaseAmyloid Precursor Protein (APP)CR-domainsFingerprint ResiduesGolgiIntracellular TraffickingMembrane ProteinO-GlycosylationSorLA

Identifiers

PMID25525276
PMCPMC4319007
OpenAlexW1732628185

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.