Evidence map›Paper›PMID 19584300›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2009

Structural changes in intermediate filament networks alter the activity of insulin-degrading enzyme.

Ying-Hao Chou, Wen-Liang Kuo, Marsha Rich Rosner, Wei-Jen Tang, Robert D Goldman

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.4field-weighted citation impact, top 39% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus.Trends in endocrinology and metabolism: TEM · 2016
    Review
  9. Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Article
  11. 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 2 institutions in 1 country.

Ying-Hao ChouDepartment of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, 303 East Chicago Ave., Chicago, IL 60611, USA.
Wen-Liang Kuo
Marsha Rich Rosner
Wei-Jen Tang
Robert D Goldman
University of Chicago · USNorthwestern University · US

Funding

Regulation and Catalysis of Human Insulin Degrading EnzymeR01GM081539 · NIGMS · UNIVERSITY OF CHICAGO · PI TANG, WEI-JEN · 2007 to 2015
$2.6M
NIGMS NIH HHS R01 GM081539
6 · The paper itself

Abstract

The intermediate filament (IF) protein nestin coassembles with vimentin and promotes the disassembly of these copolymers when vimentin is hyperphosphorylated during mitosis. The aim of this study is to determine the function of these nonfilamentous particles by identifying their interacting partners. In this study, we report that these disassembled vimentin/nestin complexes interact with insulin degrading enzyme (IDE). Both vimentin and nestin interact with IDE in vitro, but vimentin binds IDE with a higher affinity than nestin. Although the interaction between vimentin and IDE is enhanced by vimentin phosphorylation at Ser-55, the interaction between nestin and IDE is phosphorylation independent. Further analyses show that phosphorylated vimentin plays the dominant role in targeting IDE to the vimentin/nestin particles in vivo, while the requirement for nestin is related to its ability to promote vimentin IF disassembly. The binding of IDE to either nestin or phosphorylated vimentin regulates IDE activity differently, depending on the substrate. The insulin degradation activity of IDE is suppressed approximately 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2- to 3-fold. Taken together, our data demonstrate that the nestin-mediated disassembly of vimentin IFs generates a structure capable of sequestering and modulating the activity of IDE.

Indexed as

Amino Acid SequenceAnimalsCell LineCHO CellsCricetinaeCricetulusInsulysinIntermediate Filament ProteinsIntermediate FilamentsNerve Tissue ProteinsNestinPhosphorylationRatsVimentinInsulysinIntermediate Filament ProteinsNerve Tissue ProteinsNes protein, ratNestinVimentin

Identifiers

PMID19584300
PMCPMC2775012
OpenAlexW1982815464

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.