Evidence map›Paper›PMID 22412873›Full record

ArticlePloS one2012

The tempered polymerization of human neuroserpin.

Rosina Noto, Maria Grazia Santangelo, Stefano Ricagno, Maria Rosalia Mangione, Matteo Levantino, Margherita Pezzullo, Vincenzo Martorana, Antonio Cupane, Martino Bolognesi, Mauro Manno

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  6. Neuroserpin: structure, function, physiology and pathology.Cellular and molecular life sciences : CMLS · 2021
    Review
  7. Scaling Concepts in Serpin Polymer Physics.Materials (Basel, Switzerland) · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
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  14. Glycosylation Tunes Neuroserpin Physiological and Pathological Properties.International journal of molecular sciences · 2020
    Article
  15. Article
  16. Article
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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

10 authors at 3 institutions in 1 country.

Rosina NotoInstitute of Biophysics, National Research Council of Italy, Palermo, Italy.
Maria Grazia Santangelo
Stefano Ricagno
Maria Rosalia Mangione
Matteo Levantino
Margherita Pezzullo
Vincenzo Martorana
Antonio Cupane
Martino Bolognesi
Mauro Manno
National Research Council · ITUniversity of Milan · ITUniversity of Palermo · IT

Funding

Telethon GGP11057
6 · The paper itself

Abstract

Neuroserpin, a member of the serpin protein superfamily, is an inhibitor of proteolytic activity that is involved in pathologies such as ischemia, Alzheimer's disease, and Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB). The latter belongs to a class of conformational diseases, known as serpinopathies, which are related to the aberrant polymerization of serpin mutants. Neuroserpin is known to polymerize, even in its wild type form, under thermal stress. Here, we study the mechanism of neuroserpin polymerization over a wide range of temperatures by different techniques. Our experiments show how the onset of polymerization is dependent on the formation of an intermediate monomeric conformer, which then associates with a native monomer to yield a dimeric species. After the formation of small polymers, the aggregation proceeds via monomer addition as well as polymer-polymer association. No further secondary mechanism takes place up to very high temperatures, thus resulting in the formation of neuroserpin linear polymeric chains. Most interesting, the overall aggregation is tuned by the co-occurrence of monomer inactivation (i.e. the formation of latent neuroserpin) and by a mechanism of fragmentation. The polymerization kinetics exhibit a unique modulation of the average mass and size of polymers, which might suggest synchronization among the different processes involved. Thus, fragmentation would control and temper the aggregation process, instead of enhancing it, as typically observed (e.g.) for amyloid fibrillation.

Indexed as

HumansKineticsModels, MolecularNeuropeptidesNeuroserpinProtein FoldingProtein MultimerizationSerpinsTemperatureNeuropeptidesNeuroserpinSerpins

Identifiers

PMID22412873
PMCPMC3295756
OpenAlexW2033619534

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.