Evidence map›Paper›PMID 25377861›Full record

ArticleProtein science : a publication of the Protein Society2015

ApoE: the role of conserved residues in defining function.

Carl Frieden

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Alzheimer's Disease: A Suitable Case for Treatment with Precision Medicine?Medical principles and practice : international journal of the Kuwait University, Health Science Centre · 2024
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Transcriptome Profiling Revealed MultipleFrontiers in microbiology · 2020
    Article
  11. Review
  12. Article
  13. A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. TREM2-Ligand Interactions in Health and Disease.Journal of molecular biology · 2017
    Review
  15. Helical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. 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

1 author at 1 institution in 1 country.

Carl FriedenDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri, 63110.
Washington University in St. Louis · US

Funding

ALZHEIMER'S DISEASE: DEFINING THE APOE-AMYLOID-BETA INTERACTIONRF1AG044331 · NIA · WASHINGTON UNIVERSITY · PI FRIEDEN, CARL · 2014 to 2014
$1.6M
NIA NIH HHS RF1 AG044331NIA NIH HHS RF1AG044331
6 · The paper itself

Abstract

The amino acid sequences of apolipoprotein E (apoE) from 63 different mammalian species have been downloaded from the protein database. The sequences were compared to human apoE4 to determine conserved and non-conserved sequences of amino acids. ApoE4 is the major risk factor for the development of late onset Alzheimer's disease while apoE3, which differs from apoE4 by a single amino acid change at position 112, poses little or no risk for the development of this disease. Thus, the two proteins appear to be structurally and functionally different. Seven highly conserved regions, representing approximately 47 amino acids (of 299) have been found. These regions are distributed throughout the protein and reflect ligand binding sites as well as regions proposed to be involved in the propagation of the cysteine-arginine change at position 112 to distant regions of the protein in the N- and C-terminal domains. Highly non-conserved regions are at the N- and C-terminal ends of the apoE protein.

Indexed as

Alzheimer DiseaseAmino Acid SequenceAmyloid beta-PeptidesAnticoagulantsApolipoprotein E3Apolipoprotein E4Apolipoproteins EBinding SitesConserved SequenceHeparinHumansModels, MolecularMolecular Sequence DataProtein BindingReceptors, LDLAmyloid beta-PeptidesAnticoagulantsApolipoprotein E3Apolipoprotein E4Apolipoproteins EHeparinReceptors, LDLallosteric pathwayamino acid sequencesAβ bindingheparin bindingLDL receptor bindinglipoprotein binding

Identifiers

PMID25377861
PMCPMC4282419
OpenAlexW1559890486

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.