Evidence map›Paper›PMID 28470663›Full record

ArticleAngewandte Chemie (International ed. in English)2017

Mechanical Deformation Accelerates Protein Ageing.

Jessica Valle-Orero, Jaime Andrés Rivas-Pardo, Rafael Tapia-Rojo, Ionel Popa, Daniel J Echelman, Shubhasis Haldar, Julio M Fernández

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Ephemeral states in protein folding under force captured with a magnetic tweezers design.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Force-Clamp Rheometry for Characterizing Protein-based Hydrogels.Journal of visualized experiments : JoVE · 2018
    Article
  16. Review
  17. Article
  18. Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017
    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

7 authors at 2 institutions in 1 country.

Jessica Valle-OreroDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.ORCID 0000-0002-7010-1734
Jaime Andrés Rivas-PardoDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Rafael Tapia-RojoDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Ionel PopaDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Daniel J EchelmanDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Shubhasis HaldarDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Julio M FernándezDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Columbia University · USUniversity of Wisconsin–Milwaukee · US

Funding

Single Molecule Studies of Titin ElasticityR01HL061228 · NHLBI · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI FERNANDEZ, JULIO M · 1999 to 2017
$7.4M
Nanomechanics of bacterial adhesionR01GM116122 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI FERNANDEZ, JULIO M · 2015 to 2018
$1.4M
NHLBI NIH HHS R01 HL061228NIGMS NIH HHS R01 GM116122
6 · The paper itself

Abstract

A hallmark of tissue ageing is the irreversible oxidative modification of its proteins. We show that single proteins, kept unfolded and extended by a mechanical force, undergo accelerated ageing in times scales of minutes to days. A protein forced to be continuously unfolded completely loses its ability to contract by folding, becoming a labile polymer. Ageing rates vary among different proteins, but in all cases they lose their mechanical integrity. Random oxidative modification of cryptic side chains exposed by mechanical unfolding can be slowed by the addition of antioxidants such as ascorbic acid, or accelerated by oxidants. By contrast, proteins kept in the folded state and probed over week-long experiments show greatly reduced rates of ageing. We demonstrate a novel approach whereby protein ageing can be greatly accelerated: the constant unfolding of a protein for hours to days is equivalent to decades of exposure to free radicals under physiological conditions.

Indexed as

AntioxidantsMechanical PhenomenaProtein DenaturationProtein FoldingProteinsAntioxidantsProteinsforce spectroscopyoxidative damageprotein foldingprotein structuresingle-molecule studies

Identifiers

PMID28470663
PMCPMC5540753
OpenAlexW2611675287

What OpenQuestion holds

Textmetadata
LicenceTDM
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.