Evidence map›Paper›PMID 16888322›Full record

ArticleRNA (New York, N.Y.)2006

RNA aptamers selectively modulate protein recruitment to the cytoplasmic domain of beta-secretase BACE1 in vitro.

Andrea Rentmeister, Anke Bill, Tina Wahle, Jochen Walter, Michael Famulok

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
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, 54 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Aptamer Applications in Neuroscience.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Aptamer and its applications in neurodegenerative diseases.Cellular and molecular life sciences : CMLS · 2017
    Review
  11. Review
  12. Article
  13. Review
  14. RNA aptamers and their therapeutic and diagnostic applications.International journal of biochemistry and molecular biology · 2013
    Article
  15. Article
  16. The selection of aptamers specific for membrane molecular targets.Cellular & molecular biology letters · 2011
    Review
  17. Article
  18. Review
  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

5 authors at 1 institution in 1 country.

Andrea RentmeisterLIMES Program Unit Chemical Biology & Medicinal Chemistry, Universität Bonn, 53121 Bonn, Germany.
Anke Bill
Tina Wahle
Jochen Walter
Michael Famulok
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The beta-amyloid peptide (Abeta) is a major component of the Alzheimer's disease (AD)-associated senile plaques and is generated by sequential cleavage of the beta-amyloid precursor protein (APP) by beta-secretase and gamma-secretase. Since BACE1 initiates Abeta generation it represents a valuable target to interfere with Abeta production and treatment of AD. While the enzymatic activity of BACE1 resides in the extracellular domain, the protein also contains a short cytoplasmic tail (B1-CT). This domain serves as a binding site for at least two proteins, the copper chaperone for superoxide dismutase-1 (CCS), and the Golgi-localized, gamma-ear-containing, ADP ribosylation factor-binding (GGA1) protein, and contains a single phosphorylation site. However, the precise role of the B1-CT for the overall biological function of this protein is largely unknown. Functional studies focusing on the activity of this domain would strongly benefit from the availability of domain-specific inhibitors. Here we describe the isolation and characterization of RNA aptamers that selectively target the B1-CT. We show that these RNAs bind to authentic BACE1 and provide evidence that the binding site is restricted to the membrane-proximal half of the C terminus. Aptamer-binding specifically interferes with the recruitment of CCS, but still permits GGA1 association and casein kinase-dependent phosphorylation, consistent with selective binding site targeting within this short peptide. Because phosphorylation and GGA1 binding to B1-CT regulate BACE1 transport, these RNA inhibitors could be applied to investigate B1-CT activity without affecting the subcellular localization of BACE1.

Indexed as

Adaptor Proteins, Vesicular TransportADP-Ribosylation FactorsAlzheimer DiseaseAmino Acid MotifsAmino Acid SequenceAmyloid Precursor Protein SecretasesAptamers, NucleotideAspartic Acid EndopeptidasesBase SequenceBinding SitesCell MembraneCytoplasmEndopeptidasesGlutathione TransferaseIn Vitro TechniquesMolecular ChaperonesAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsAmyloid Precursor Protein SecretasesAptamers, NucleotideAspartic Acid EndopeptidasesBACE1 protein, humanCCS protein, humanEndopeptidasesGGA adaptor proteinsGlutathione TransferaseMolecular ChaperonesProteinsRecombinant Fusion Proteins

Identifiers

PMID16888322
PMCPMC1557694
OpenAlexW2120070003

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.