Evidence map›Paper›PMID 23410248›Full record

ArticleMicrobial cell factories2013

Why and how protein aggregation has to be studied in vivo.

Diletta Ami, Antonino Natalello, Marina Lotti, Silvia Maria Doglia

Abstract read
In one paragraph

Article in Microbial cell factories, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Pathological ATX3 Expression Induces Cell Perturbations inInternational journal of molecular sciences · 2021
    Article
  5. MultidirectionalJournal of enzyme inhibition and medicinal chemistry · 2020
    Article
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  15. Review
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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

4 authors.

Diletta AmiDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy. silviamaria.doglia@unimib.it
Antonino Natalello
Marina Lotti
Silvia Maria Doglia

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The understanding of protein aggregation is a central issue in different fields of protein science, from the heterologous protein production in biotechnology to amyloid aggregation in several neurodegenerative and systemic diseases. To this goal, it became more and more evident the crucial relevance of studying protein aggregation in the complex cellular environment, since it allows to take into account the cellular components affecting protein aggregation, such as chaperones, proteases, and molecular crowding. Here, we discuss the use of several biochemical and biophysical approaches that can be employed to monitor protein aggregation within intact cells, focusing in particular on bacteria that are widely employed as microbial cell factories.

Indexed as

AmyloidBenzothiazolesHumansMagnetic Resonance SpectroscopyMolecular ChaperonesNeurodegenerative DiseasesPeptide HydrolasesProteinsRecombinant Fusion ProteinsSpectroscopy, Fourier Transform InfraredThiazolesAmyloidBenzothiazolesMolecular ChaperonesPeptide HydrolasesProteinsRecombinant Fusion ProteinsThiazolesthioflavin T

Identifiers

PMID23410248
PMCPMC3583745

What OpenQuestion holds

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LicenceCC BY
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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.