Evidence map›Paper›PMID 15800373›Full record

ArticleJournal of molecular neuroscience : MN2005

Insulysin: an allosteric enzyme as a target for Alzheimer's disease.

Eun Suk Song, Louis B Hersh

Abstract read
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In one paragraph

Article in Journal of molecular neuroscience : MN, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 29 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Eun Suk SongDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536, USA.
Louis B Hersh
University of Kentucky · US

Funding

DEGRADATION OF OPIOID PEPTIDESR01DA002243 · NIDA · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 1985 to 2011
$3.4M
Neprilysin and Abeta-degradation in Alzheimer's diseaseR01AG019323 · NIA · UNIVERSITY OF KENTUCKY · PI KINDY, MARK S · 2002 to 2005
$958k
NIA NIH HHS AG19323NIDA NIH HHS DA02243
6 · The paper itself

Abstract

That the zinc metalloendopeptidase insulysin (insulin-degrading enzyme IDE) is a major b-amyloid (A(beta)) peptide-degrading enzyme in vivo is shown by the higher A(beta) peptide levels in the brain of an insulysin-deficient mouse. Insulysin was shown to initially cleave A(beta)1-40and A(beta)1-42 at His13-Gln14, His14-Gln15, and Phe19-Phe20. The insulysin-dependent cleavage of A(beta) prevents both the neurotoxic effects of the peptide as well as the ability of A(beta) to deposit onto synthetic amyloid plaques. The kinetics of the reaction of insulysin with the synthetic peptide substrate Abz-G-G-F-L-R-K-H-G-Q-EDDnp displays allosteric properties indicative of a regulated enzyme. Small peptide substrates increase the activity of insulysin toward the hydrolysis of A(beta)1-40 without affecting the activity of the enzyme toward insulin. These studies indicate that insulysin is a target for drug development in which small-molecule peptide analogs can be used to increase the rate of A(beta) clearance without affecting insulin levels.

Indexed as

Allosteric RegulationAlzheimer DiseaseAmino Acid SequenceAmyloid beta-PeptidesAnimalsCell LineDrug DesignInsectaInsulysinMiceMice, Mutant StrainsMolecular Sequence DataNeuronsRatsZincAmyloid beta-PeptidesInsulysinZinc

Identifiers

PMID15800373
OpenAlexW1973247083

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.