Evidence map›Paper›PMID 16174739›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Dissecting the mechanical unfolding of ubiquitin.

Anders Irbäck, Simon Mitternacht, Sandipan Mohanty

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Insights into Ligand-Protein Binding from Local Mechanical Response.Journal of chemical theory and computation · 2011
    Article
  11. Article
  12. Minimum energy compact structures in force-quench polyubiquitin folding are domain swapped.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Water's role in the force-induced unfolding of ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  14. Article
  15. Article
  16. Direct observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  17. Osmolyte-induced separation of the mechanical folding phases of ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Article
  19. Article
  20. 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

3 authors.

Anders IrbäckComplex Systems Division, Department of Theoretical Physics, Lund University, Sölvegatan 14A, SE-223 62 Lund, Sweden. anders@thep.lu.se
Simon Mitternacht
Sandipan Mohanty

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolding behavior of ubiquitin under the influence of a stretching force recently was investigated experimentally by single-molecule constant-force methods. Many observed unfolding traces had a simple two-state character, whereas others showed clear evidence of intermediate states. Here, we use Monte Carlo simulations to investigate the force-induced unfolding of ubiquitin at the atomic level. In agreement with experimental data, we find that the unfolding process can occur either in a single step or through intermediate states. In addition to this randomness, we find that many quantities, such as the frequency of occurrence of intermediates, show a clear systematic dependence on the strength of the applied force. Despite this diversity, one common feature can be identified in the simulated unfolding events, which is the order in which the secondary-structure elements break. This order is the same in two- and three-state events and at the different forces studied. The observed order remains to be verified experimentally but appears physically reasonable.

Indexed as

Models, MolecularProtein FoldingMonte Carlo MethodProtein DenaturationProtein Structure, SecondaryStructure-Activity RelationshipUbiquitinUbiquitin

Identifiers

PMID16174739
PMCPMC1224613

What OpenQuestion holds

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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.