Evidence map›Paper›PMID 24970203›Full record

ReviewBiomolecules2013

The role of non-native interactions in the folding of knotted proteins: insights from molecular dynamics simulations.

Roberto Covino, Tatjana Skrbić, Silvio A Beccara, Pietro Faccioli, Cristian Micheletti

Abstract readReview
In one paragraph

Review in Biomolecules, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Folding kinetics of an entangled protein.PLoS computational biology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Topological descriptions of protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Review
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.

Roberto CovinoDepartment of Physics, University of Trento, Via Sommarive 14, Trento 38123, Italy. faccioli@science.unitn.it.
Tatjana SkrbićSISSA-Scuola Internazionale Superiore di Studi Avanzati, Via Bonomea 265, Trieste 34136, Italy. tatjana.skrbic@pd.infn.it.
Silvio A BeccaraInterdisciplinary Laboratory for Computational Science, FBK-CMM and University of Trento,Trento 38123, Italy. sabeccara@fbk.eu.
Pietro FaccioliDepartment of Physics, University of Trento, Via Sommarive 14, Trento 38123, Italy. faccioli@science.unitn.it.
Cristian MichelettiSISSA-Scuola Internazionale Superiore di Studi Avanzati, Via Bonomea 265, Trieste 34136, Italy. michelet@sissa.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For several decades, the presence of knots in naturally-occurring proteins was largely ruled out a priori for its supposed incompatibility with the efficiency and robustness of folding processes. For this very same reason, the later discovery of several unrelated families of knotted proteins motivated researchers to look into the physico-chemical mechanisms governing the concerted sequence of folding steps leading to the consistent formation of the same knot type in the same protein location. Besides experiments, computational studies are providing considerable insight into these mechanisms. Here, we revisit a number of such recent investigations within a common conceptual and methodological framework. By considering studies employing protein models with different structural resolution (coarse-grained or atomistic) and various force fields (from pure native-centric to realistic atomistic ones), we focus on the role of native and non-native interactions. For various unrelated instances of knotted proteins, non-native interactions are shown to be very important for favoring the emergence of conformations primed for successful self-knotting events.

Indexed as

Protein FoldingAnimalsHumansMolecular Dynamics SimulationProtein AggregatesProteinsProtein AggregatesProteins

Identifiers

PMID24970203
PMCPMC4030985

What OpenQuestion holds

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Registered trials

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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.