Evidence map›Paper›PMID 20303980›Full record

ArticleJournal of molecular biology2010

Structure of the minimal interface between ApoE and LRP.

Miklos Guttman, J Helena Prieto, Tracy M Handel, Peter J Domaille, Elizabeth A Komives

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
–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

39 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Megalin: from structure to function.Nature reviews. Nephrology · 2026
    Review
  3. ApoE Mimetic Peptides as Therapy for Traumatic Brain Injury.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2023
    Review
  4. Review
  5. Article
  6. Anti-inflammatory effect of ApoE23 onOpen medicine (Warsaw, Poland) · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Therapeutic Development of Apolipoprotein E Mimetics for Acute Brain Injury: Augmenting Endogenous Responses to Reduce Secondary Injury.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2020
    Review
  14. Article
  15. Article
  16. Immunization with the GlyTheranostics · 2020
    Article
  17. Review
  18. Molecular modeling of LDLR aids interpretation of genomic variants.Journal of molecular medicine (Berlin, Germany) · 2019
    Article
  19. Structural Biology and Protein Engineering of Thrombolytics.Computational and structural biotechnology journal · 2019
    Review
  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

5 authors.

Miklos GuttmanDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0378, USA.
J Helena Prieto
Tracy M Handel
Peter J Domaille
Elizabeth A Komives

Funding

Directed Proteomics of Alzheimer's Related ProteinsR01AG025343 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2004 to 2008
$1.5M
BIOPHYSICAL STUDIES OF LRP LIGANDS INTERACTIONSR01AG017992 · NIA · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2000 to 2003
$923k
NIA NIH HHS AG025343NIA NIH HHS R01 AG017992NIA NIH HHS R01 AG025343
6 · The paper itself

Abstract

Clusters of complement-type ligand-binding repeats (CRs) in the low-density lipoprotein receptor (LDLR) family are thought to mediate the interactions with their various ligands. Apolipoprotein E (ApoE), a key ligand for cholesterol homeostasis, has been shown to interact with LDLR-related protein 1 (LRP) through these clusters. The segment comprising the receptor-binding portion of ApoE (residues 130-149) has been found to have a weak affinity for isolated CRs. We have fused this region of ApoE to a high-affinity CR from LRP (CR17) for structural elucidation of the complex. The interface reveals a motif that has previously been observed in CR domains with other binding partners, but with several novel features. Comparison to free CR17 reveals that very few structural changes result from this binding event, but significant changes in intrinsic dynamics are observed upon binding. NMR perturbation experiments suggest that this interface may be similar to several other ligand interactions with LDLRs.

Indexed as

Amino Acid SequenceApolipoproteins EHumansLigandsLow Density Lipoprotein Receptor-Related Protein-1Molecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationProtein Structure, TertiarySequence AlignmentApolipoproteins ELigandsLow Density Lipoprotein Receptor-Related Protein-1

Identifiers

PMID20303980
PMCPMC2880916

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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.